Recherche / Départements scientifiques / Biologie cellulaire et infection / Unités et groupes / Unité des Interactions Bactéries-Cellules / 2004-2008 (AERES)
2004-2008 Scientific Work Report (AERES)
1. The discovery and /or characterization of several new virulence factors and regulatory circuits controlling L. monocytogenes virulence
2. The discovery of non-coding RNAs in Listeria
3. The elucidation of the role of lipid rafts in the entry of Listeria into cells
4. The discovery of several key cellular components allowing internalin-mediated entry
5. The discovery of successive post-translational modifications of E-cadherin during internalin-mediated entry
6. The identification of new factors essential for the InlB-dependent entry pathway
7. The discovery of a new role for clathrin in bacterial invasion and adhesion
8. The first report on a role for a septin in bacterial invasion
9. The discovery of a peptidoglycan modification allowing bacterial escape from the host immune system
10. The discovery of histone modifications induced by a family of bacterial toxins
11. The discovery that the main transcriptomic response to Listeria in the intestine is due to listeriolysin O
12. The demonstration that InlB, as internalin, has a species-specificity and that InlB plays no role in the crossing of the intestinal barrier
13. The validation of the role of internalin in human listeriosis by an epidemiological survey of a large collection of food and clinical strains
14. The identification of the conjugated action of internalin and InlB in placental listeriosis
15. The discovery of a novel actin nucleator produced by Rickettisa conorii
16. The identification of the first Rickettsia receptor and of its bacterial ligand
2. The discovery of non-coding RNAs in Listeria
3. The elucidation of the role of lipid rafts in the entry of Listeria into cells
4. The discovery of several key cellular components allowing internalin-mediated entry
5. The discovery of successive post-translational modifications of E-cadherin during internalin-mediated entry
6. The identification of new factors essential for the InlB-dependent entry pathway
7. The discovery of a new role for clathrin in bacterial invasion and adhesion
8. The first report on a role for a septin in bacterial invasion
9. The discovery of a peptidoglycan modification allowing bacterial escape from the host immune system
10. The discovery of histone modifications induced by a family of bacterial toxins
11. The discovery that the main transcriptomic response to Listeria in the intestine is due to listeriolysin O
12. The demonstration that InlB, as internalin, has a species-specificity and that InlB plays no role in the crossing of the intestinal barrier
13. The validation of the role of internalin in human listeriosis by an epidemiological survey of a large collection of food and clinical strains
14. The identification of the conjugated action of internalin and InlB in placental listeriosis
15. The discovery of a novel actin nucleator produced by Rickettisa conorii
16. The identification of the first Rickettsia receptor and of its bacterial ligand
1. The discovery and/or characterization of several virulence factors and regulatory circuits controlling L. monocytogenes virulence
We have discovered several new Listeria virulence genes: FbpA is a fibronectin-binding protein involved in bacterial adhesion which seems to also act as a chaperone for InlB and listeriolysin O (Dramsi et al. 2004). Auto is an autolysin involved in entry into cells (Cabanes et al. 2004). Vip is a surface protein which interacts with Gp96, a protein involved in the control of the immune response in particular by regulating the subcellular localization of toll like receptors (Cabanes et al. 2005). VirR is a major new pleiotropic regulator of virulence which activates or represses several genes involved in modifications of bacterial cell surface components (Mandin et al. 2005). The ser/thr phosphatase Stp (Archambaud et al. 2005) controls in particular the activity of the superoxyde dismutase (SOD). This SOD is particularly interesting as it is secreted by the secA2 pathway; it is negatively regulated by phosphorylation and this inactivation may also occur via a kinase from the host cell when it is secreted in the cytoplasm of infected cells (Archambaud et al. 2006). InlJ is a protein of the internalin family which does not seem to play any role in cellular systems in vitro (Sabet et al. 2005). Recent results indicate that InlJ is not expressed in vitro and is specifically expressed in vivo (Sabet et al. 2008).
2. The discovery of non-coding RNAs in Listeria
We have used in silico-based approaches to analyze the intergenic regions of the chromosome of strain EGD-e and have identified twelve non coding RNAs(ncRNAs). Among them, nine are novel and specific to the Listeria genus and two of these ncRNAs are expressed in a growth-dependent manner. Three of the ncRNAs are transcribed in opposite direction to overlapping open reading frames (ORFs), suggesting that they act as antisense on the corresponding mRNAs. The other ncRNA genes appear as single transcription units. One of them displays five repeats of 29 nucleotides. Five of these new ncRNAs are absent from the non pathogenic species L. innocua, raising the possibility that they might be involved in virulence. To predict mRNA targets of the ncRNAs, we developped a computational method based on thermodynamic pairing energies and known ncRNA-mRNA hybrids. Three ncRNAs including one of the putative antisense ncRNAs, were predicted to have more than one mRNA target. Several of them were shown to bind efficiently to the ncRNAs suggesting that our in silico approach could be used as a general tool to search for mRNA targets of ncRNAs (Mandin et al. 2007).
3. The elucidation of the role of lipid rafts in the entry of Listeria
Listeria enters into cells via two pathways, the internalin(InlA)- E-cadherin pathway and the InlB-Met pathway. By using classical techniques to investigate if the presence of rafts in membranes affects Listeria entry, we showed that entry via the InlA pathway is affected, if rafts are disorganised by cholesterol depletion, at the step of adhesion and that the InlB mediated way of entry is affected not at the stage of bacterial adhesion but later in the process of entry, at the level of signals that trigger actin rearrangements (Seveau et al. 2004). We then used a fluorescence resonance energy transfer (FRET)-based microscopic method to analyze signaling events in living cells. Phosphoinositide 3-kinase activity and Rac1 signalling induced by Listeria interacting with epithelial cells were first monitored as well as signaling induced by soluble InlB and the Met natural ligand HGF. We found that InlB and HGF induced similar kinetics of PI 3-kinase and Rac activation. Cholesterol depletion experiments were then performed to address the role of lipid rafts in Met signalling. The amount of 3’-phosphoinositides produced by PI-3 kinase was not affected by cholesterol depletion. Rac1 activation, downstream from PI 3 kinase was cholesterol-dependent suggesting that the spatial distribution of 3’ phosphoinositides within membrane microdomains is critical for Rac1 activation and consequently for F-actin assembly at bacterial entry site (Seveau et al. 2007).
4. The discovery of several key cellular components allowing internalin-mediated entry
By studying the internalin-dependent entry, we have contributed to demonstrate the key role of the transmembrane protein vezatin and that of a non conventional myosin, myosinVIIa in E-cadherin function (Sousa et al. 2004). We have also identified ARHGAP10, a novel ligand of α-catenin which is necessary for Listeria entry and quite importantly required for the recruitment of α-catenin to cellular junctions (Sousa et al. 2005). Finally, in our search to identify the proteins regulating the transient actin polymerization required for entry, we demonstrated the key role of Arp2/3. Using a variety of approaches including siRNA, expression of dominant negative derivatives and pharmacological inhiboitors, we demonstrated the crucial role of cortactin in the activation of Arp2/3. We also showed the requirement for the small GTPase Rac and that of Src-tyrosine kinase activity to promote Listeria internalisation. Together, these data suggested a model in which Src tyrosine kinase and Rac1 promote recruitment of cortactin and activation of Arp2/3 at Listeria entry site, mimicking events that occur during adherens junction formation (Sousa et al. 2007).
5. The discovery of successive post-translational modifications of E-cadherin during internalin mediated entry
We have shown that InlA triggers two succesive E-cadherin post-translational modifications, i.e. the Src mediated tyrosine phosphorylation of E-cadherin followed by its ubiquitination by the ubiquitin ligase Hakai. E-cadherin ubiquitination induces the recruitment of clathrin that is required for optimal bacterial internalization. We also showed that the initial clustering of E-cadherin at the bacterial entry site requitres caveolin, a protein normally involved in clathrin independent endocytosis. We showed that strikingly clathrin and caveolin are also recruited at the site of entry of E-cadherin-coated sepharose beads and functional experiments demonstrate that these two proteins are required for bead entry. Together these results not only documented how the endocytosis machinery is recruited and involved in the internalization of a zippering bacterium but also strongly suggested a functional link between E-cadherin endocytosis and the formation of adherens junction (Bonazzi et al. 2008).
Figure 1: Schematic diagram of InlA and InlB induced signaling cascades.
Figure 1: Schematic diagram of InlA and InlB induced signaling cascades.
6. The identification of new factors essential for the InlB-dependent entry pathway
A series of cellular components critical for the actin rearrangements taking place during infection have been identified. The results highlighted the incredible capacity of Listeria to exploit all the elements of the cytoskeleton in particular cofilin, LIM kinase, the Arp2/3 complex, the N-WASP and Wave proteins and also the Ena/Vasp proteins (Bierne et al. 2005). These studies have been carried out in parallel with InlB and HGF and have demonstrated the striking functional similarity between HGF and InB although these proteins are totally different in structure (Veiga and Cossart, 2007).
We have purified phagosomes containing InlB-coated beads and showed that they display a strong type II phosphatidylinositol 4-kinase activity (PI4K) activity. In human epithelial HeLa cells, both PI4KIIalpha and PI4KIIbeta isoforms are co-recruited with Met around InlB beads or wild type Listeria during the early steps of internalization and phosphatidylinositol 4-phosphate (PI(4)P is detected at the entry site. We have demonstrated that PI4KIIalpha or beta knockdown, but not type III PI4K downdown inhibits Listeria internalization. Production of of PI(4)P derivatives such as phosphatidylinositol 3,4,5, triphosphate (PI(3, 4, 5)P(3)) upon InlB stimulation is not affected by PI4KIIalpha or PI4KIIbeta knockdown, suggesting that these phospholinitides are generated by a type III PI4K. Strikingly, knockdown of PI(4)P ligand and clatrhin adaptor AP-1 strongly inhibits bacterial entry. Together our results have revealed a yet non described role for type II PI4Ks in phagocytosis (Pizarro-Cerda et al. 2007).
We have purified phagosomes containing InlB-coated beads and showed that they display a strong type II phosphatidylinositol 4-kinase activity (PI4K) activity. In human epithelial HeLa cells, both PI4KIIalpha and PI4KIIbeta isoforms are co-recruited with Met around InlB beads or wild type Listeria during the early steps of internalization and phosphatidylinositol 4-phosphate (PI(4)P is detected at the entry site. We have demonstrated that PI4KIIalpha or beta knockdown, but not type III PI4K downdown inhibits Listeria internalization. Production of of PI(4)P derivatives such as phosphatidylinositol 3,4,5, triphosphate (PI(3, 4, 5)P(3)) upon InlB stimulation is not affected by PI4KIIalpha or PI4KIIbeta knockdown, suggesting that these phospholinitides are generated by a type III PI4K. Strikingly, knockdown of PI(4)P ligand and clatrhin adaptor AP-1 strongly inhibits bacterial entry. Together our results have revealed a yet non described role for type II PI4Ks in phagocytosis (Pizarro-Cerda et al. 2007).
7. The discovery of a new role for clathrin in bacterial invasion and adhesion
Guided by the fact that InlB interacts with a growth factor receptor, Met, which is known to be monoubiquitinated, endocytosed and degraded in lysosomes, upon HGF signaling, we demonstrated that inlB also induces Met monoubiquitination and its endocytosis. We then showed that components of the endocytosis machinery, in particular clathrin and dynamin are engaged in the entry of Listeria challenging a well established dogma that clathrin-mediated endocytosis is not involved in the entry of large particles (Veiga and Cossart, 2005). We then investigated whether the use of the endocytosis machinery was a widespread requirement. We analyzed infection models using diverse bacteria. We demonstrated that bacteria that enter cells following binding to cellular receptors (termed « zippering » bacteria) invade in a clathrin dependent manner. In contrast, bacteria that inject effector proteins into host cells in order to gain entry (« triggering bacteria ») invade in a clathrin-independent manner. Strikingly enteropathogenic Escherichia coli (EPEC) required clathrin to form actin-rich pedestals in host cells beneath adhering bacteria, even though this pathogen remains extracellular. Furthermore, clathrin accumulation preceded the actin rearrangements necessary for Listeria entry. These data provide evidence for a clathrin-based entry pathway allowing internalization of large objects (bacteria and ligand-coated beads) and used by zippering bacteria as part of a general mechanism to invade host mammalian cells. We also revealed a non-endocytic role for clathrin required for extracellular EPEC infections (Veiga et al. 2007).
Figure 2: Clathrin recruitment a the EPEC site of infection. Immunofluorescence microscopy of HeLa cells infected with wild type EPEC. Bacteria are shown in blue, actin in red and Clathrin in green.
Figure 2: Clathrin recruitment a the EPEC site of infection. Immunofluorescence microscopy of HeLa cells infected with wild type EPEC. Bacteria are shown in blue, actin in red and Clathrin in green.
8. The first report on a role for a septin in bacterial invasion
Septins are conserved GTPases that form filaments and are required in many organisms for a variety of processes including cytokinesis. We previously identified SEPT9 associated with Listeria phagosomes in mammalian cells. Given the well-established association of septins with the cytoskeleton, and the importance of the cytoskeleton in bacterial invasion, we investigated whether septins play any role during infection of invasive bacteria in non-phagocytic cells. We first investigated if septins were recruited at the site of entry. We discovered that septins were recruited and formed rings or collars around entering bacteria. These rings did not colocalize with actin. In contrast they were next to the site of actin accumulation which is clearly visible next to the pole of entering bacteria. We were able to show that not only septin 9 but also its interactors septin 2 and septin 11 form collars. Using RNAi knockdown we could show that septin 2 is critical for entry demonstrating for the first time a role for septins in the entry of bacteria (Mostowy et al 2008).
9. The discovery of a peptidoglycan modification allowing escape from the host immune system
L. monocytogenes is able to survive in the gastrointestinal environment and replicate in macrophages, thus bypassing the early innate immune defenses. Peptidoglycan (PG) is an essential component of the bacterial cell wall readily exposed to the host and, thus, an important target for the innate immune system. Characterization of the PG from L. monocytogenes demonstrated deacetylation of N-acetylglucosamine residues. We identified a PG N-deacetylase gene, pgdA, in L. monocytogenes genome sequence. Inactivation of pgdA revealed the key role of this PG modification in bacterial virulence because the mutant was extremely sensitive to the bacteriolytic activity of lysozyme, and growth was severely impaired after oral and i.v. inoculations. Within macrophage vacuoles, the mutant was rapidly destroyed and induced a massive IFN-beta response in a TLR2 and Nod1-dependent manner. Together, these results reveal that PG N-deacetylation is a highly efficient mechanism used by Listeria to evade innate host defenses. The presence of deacetylase genes in other pathogenic bacteria indicates that PG N-deacetylation could be a general mechanism used by bacteria to evade the host innate immune system.
10. The discovery of histone modifications induced by a family of bacterial toxins
The now well established fact that genetic reprogramming is induced by the concerted activation/repression of transcription factors and various histone modifications that control DNA accessibility in chromatin, was the basis of a new investigation. This study revealed that Listeria induces a dramatic dephosphorylation of histone H3 as well as a deacetylation of histone H4 during early phases of infection. This effect is mediated by the major listerial toxin listeriolysin O (LLO) in a pore-forming independent manner. Strikingly, a similar effect is also observed with other toxins of the same family such Clostridium perfringens perfringolysin (PFO) and Streptococcus pneumoniae pneumolysin (PLY). The decreased levels of histone modifications correlate with a reduced transcriptional activity of a subset of host genes, including key immunity genes. Thus manipulation of the epigenetic information emerges as an unsuspected function shared by several bacterial toxins, highlighting a common strategy used by intracellular and extracellular pathogens to modulate the host response early during infection.
11. The discovery that the main transcriptomic response to Listeria in the intestine is due to listeriolysin
Active translocation of L. monocytogenes across the intestinal epithelial barrier is mediated by interaction of internalin (InlA) and its species-specific host receptor, E-cadherin, whereas translocation across Peyer's patches through M-cells is InlA-independent. To define microbial determinants and molecular correlates of the host response to translocation via these two routes, germ-free transgenic mice expressing the human enterocyte-associated E-cadherin receptor were colonized with wild-type (WT) or mutant L. monocytogenes strains, or its nonpathogenic noninvasive relative Listeria innocua, or with Bacteroides thetaiotaomicron, a prominent intestinal symbiont. Mouse Gene-Chips, combined with Ingenuity Pathway software, were used to identify canonical signaling pathways in the response to wild type L. monocytogenes versus the other species. Experiments with various L. innocua and L. monocytogenes strains, respectively, demonstrated that the 773-member transcriptional signature of the response to WT L. monocytogenes is largely conserved in the inlA mutant. Internalin-dependent responses include down-regulation of gene networks involved in various aspects of lipid, amino acid, and energy metabolism and up-regulation of immunoinflammatory responses. The host response is markedly attenuated in a listeriolysin mutant despite its ability to be translocated to the lamina propria. Together, these studies established that listeriolysin O , rather than bacterial invasion of the lamina propria mediated by InlA, is a dominant determinant of the intensity of the host response to L. monocytogenes infection via the oral route (Lecuit et al. 2007).
12. The demonstration that InlB, as internalin, has a species-specificity and plays no role in the crossing of the intestinal barrier
Previous work had established that internalin interacts with human and guinea pig E-cadherins but not with the mouse or rat E-cadherins. These findings had led us to generate a transgenic mouse expressing human E-cadherin in the intestine. This small animal model was instrumental in showing that internalin allows eficent crossing of the intestinal barrier. We have now shown that InlB interacts with the murine Met receptor but does not interact with that of guinea pig (a species which is permissive to the internalin pathway) or that of rabbit, pointing to the fact that InlA and InlB synergy cannot be addressed in the mouse or in the guinea pig (Khelef et al. 2006). By using the transgenic mouse, we showed that InlB plays no role in the crossing of the intestinal barrier ((Khelef et al. 2006).
Figure 3: Schematic diagram illustrating the species specificity of L. monocytogenes internalins.
Figure 3: Schematic diagram illustrating the species specificity of L. monocytogenes internalins.
13. The validation of the role of internalin in human listeriosis by an epidemiological survey of a large collection of food and clinical strains
Non sense mutations in the inlA gene result in a truncated secreted internalin unable to promote entry of Listeria into cells expressing E-cadherin. We analyzed a large panel of strains of food or clinical origin and showed that clinical strains (98%) express a full length internalin in contrast to food strains which contain a much higher proportion of truncated internalins (65% of full length internalin) (Jacquet et al. 2004). In epidemic strains, internalin has always its full length showing that internalin is a critical factor for human listeriosis. We proposed to use the identification of the nature and length of internalin in food products as a marker for virulent strains.
14. The identification of the conjugated action of internalin and InlB in placental listeriosis
The epidemiological survey described above revealed in particular that all strains associated with fetoplacental listeriosis express a full length internalin, suggesting a role for internalin in the Listeria tropism for the materno-fetal barrier (Jacquet et al. 2004). By a combination of in vivo observations, in vitro infections of cell lines and ex vivo infections of healthy human placental explants, we demonstrated that internalin interacts with E-cadherin present on the apical face of syncitiotrophoblasts to allow Listeria to target and cross the placental barrier (Lecuit et al. 2004). Such an interaction between a pathogen and its cellular ligand that mediates targeting and crossing of the placental barrier has never been observed. We have now used two novel and complementary animal models for human listeriosis: the gerbil, a natural host for L. monocytogenes, and a knock-in mouse line ubiquitously expressing humanized E-cadherin. Using these two models, we have uncovered the essential and interdependent roles of InlA and InlB in fetoplacental listeriosis.We have thus deciphered for the first time the molecular mechanism underlying the ability of a microbe to target and cross the placental barrier (Disson et al. 2008).
15. The discovery of a novel actin nucleator produced by Rickettisa conorii
By comparing Listeria, Shigella, and Rickettsia actin-based motilities, we highlighted a novel type of actin-based movement. The actin tails of Rickettsia are made of long filaments and are different from those generated by Listeria and Shigella, suggesting a novel mechanism which might explain other types of actin-based mechanisms such as filopodia formation. To identify the gene responsible for the actin-based motility of Rickettsia, we compared the genome of R. conorii to that of R. prowaseki which does not polymerize actin and identified a candidate that we named RickA. We demonstrated that RickA activates and uses transiently the Arp2/3 complex thereby producing actin-bundles (Gouin et al. 2004). The intriguing underlying mechanism is under study.
16. The identification of the first Rickettsia receptor and of its bacterial ligand
Rickettsia conorii, hijacks host cell signal transduction pathways to induce its entry into normally non-phagocytic target cells (Martinez et al. 2004). We identified the first host cell receptor, Ku70, involved in the induced entry of a rickettsial species (Martinez et al. 2005). Ku70 is normally and mostly present in the nucleus and plays a role in DNA repair. It can be present at the plasma membrane. Ku70 represents a novel type of receptor for a bacterial species. We have also identified the outer-membrane adhesin/invasin-like protein, rOmpB, as a ligand for Ku70. This is the first receptor ligand interaction characterized in Rickettsia species.
Peer-Reviewed articles
1. Cabanes, D., O. Dussurget, P. Dehoux, and P. Cossart (2004). Auto, a surface associated autolysin of Listeria monocytogenes required for entry into eukaryotic cells and virulence. Mol Microbiol, 51:1601-14.
2. Cossart, P. (2004). Bacterial invasion: a new strategy to dominate cytoskeleton plasticity. Dev Cell, 6:314-5.
3. Cossart, P., and P. J. Sansonetti (2004). Bacterial invasion: the paradigms of enteroinvasive pathogens. Science, 304:242-8.
4. Doumith, M., C. Cazalet, N. Simoes, L. Frangeul, C. Jacquet, F. Kunst, P. Martin, P. Cossart, P. Glaser, and C. Buchrieser (2004). New aspects regarding evolution and virulence of Listeria monocytogenes revealed by comparative genomics and DNA arrays. Infect Immun, 72:1072-83.
5. Dramsi, S., F. Bourdichon, D. Cabanes, M. Lecuit, H. Fsihi, and P. Cossart (2004). FbpA, a novel multifunctional Listeria monocytogenes virulence factor. Mol Microbiol, 53:639-49.
6. Dussurget, O., J. Pizarro-Cerda, and P. Cossart (2004). Molecular determinants of Listeria monocytogenes virulence. Annu Rev Microbiol, 58:587-610.
7. Gouin, E., C. Egile, P. Dehoux, V. Villiers, J. Adams, F. Gertler, R. Li, and P. Cossart (2004). The RickA protein of Rickettsia conorii activates the Arp2/3 complex. Nature, 427:457-61.
8. Jacquet, C., M. Doumith, J. I. Gordon, P. M. Martin, P. Cossart, and M. Lecuit (2004). A molecular marker for evaluating the pathogenic potential of foodborne Listeria monocytogenes. J Infect Dis, 189:2094-100.
9. Lecuit, M., D. M. Nelson, S. D. Smith, H. Khun, M. Huerre, M. C. Vacher-Lavenu, J. I. Gordon, and P. Cossart (2004). Targeting and crossing of the human maternofetal barrier by Listeria monocytogenes: role of internalin interaction with trophoblast E-cadherin. Proc Natl Acad Sci USA, 101:6152-7.
10. Marino, M., M. Banerjee, J. Copp, S. Dramsi, T. Chapman, P. van der Geer, P. Cossart, and P. Ghosh (2004). Characterization of the calcium-binding sites of Listeria monocytogenes InlB. Biochem Biophys Res Commun, 316:379-86.
11. Martinez, J. J., and P. Cossart (2004). Early signaling events involved in the entry of Rickettsia conorii into mammalian cells. J Cell Sci, 117:5097-106.
12. Milohanic, E., R. Jonquieres, P. Glaser, P. Dehoux, C. Jacquet, P. Berche, P. Cossart, and J. L. Gaillard (2004). Sequence and binding activity of the autolysin-adhesin Ami from epidemic Listeria monocytogenes 4b. Infect Immun, 72:4401-9.
13. Pizarro-Cerda, J., and P. Cossart (2004). Subversion of phosphoinositide metabolism by intracellular bacterial pathogens. Nat Cell Biol, 6:1026-33.
14. Seveau, S., H. Bierne, S. Giroux, M. C. Prevost, and P. Cossart (2004). Role of lipid rafts in E-cadherin-- and HGF-R/Met--mediated entry of Listeria monocytogenes into host cells. J Cell Biol, 166:743-53.
15. Sousa, S., D. Cabanes, A. El-Amraoui, C. Petit, M. Lecuit, and P. Cossart (2004). Unconventional myosin VIIa and vezatin, two proteins crucial for Listeria entry into epithelial cells. J Cell Sci, 117:2121-30.
16. Archambaud, C., E. Gouin, J. Pizarro-Cerda, P. Cossart, and O. Dussurget (2005). Translation elongation factor EF-Tu is a target for Stp, a serine-threonine phosphatase involved in virulence of Listeria monocytogenes. Mol Microbiol, 56:383-96.
17. Bierne, H., H. Miki, M. Innocenti, G. Scita, F. B. Gertler, T. Takenawa, and P. Cossart (2005). WASP-related proteins, Abi1 and Ena/VASP are required for Listeria invasion induced by the Met receptor. J Cell Sci, 118:1537-47.
18. Cabanes, D., S. Sousa, A. Cebria, M. Lecuit, F. Garcia-del Portillo, and P. Cossart (2005). Gp96 is a receptor for a novel Listeria monocytogenes virulence factor, Vip, a surface protein. Embo J, 24:2827-38.
19. Calvo, E., M. G. Pucciarelli, H. Bierne, P. Cossart, J. P. Albar, and F. Garcia-Del Portillo (2005). Analysis of the Listeria cell wall proteome by two-dimensional nanoliquid chromatography coupled to mass spectrometry. Proteomics, 5:433-43.
20. Dussurget, O., E. Dumas, C. Archambaud, I. Chafsey, C. Chambon, M. Hebraud, and P. Cossart (2005). Listeria monocytogenes ferritin protects against multiple stresses and is required for virulence. FEMS Microbiol Lett, 250:253-61.
21. Gouin, E., M. D. Welch, and P. Cossart (2005). Actin-based motility of intracellular pathogens. Curr Opin Microbiol, 8:35-45.
22. Guimaraes, V. D., J. E. Gabriel, F. Lefevre, D. Cabanes, A. Gruss, P. Cossart, V. Azevedo, and P. Langella (2005). Internalin-expressing Lactococcus lactis is able to invade small intestine of guinea pigs and deliver DNA into mammalian epithelial cells. Microbes Infect, 7:836-44.
23. Herro, R., S. Poncet, P. Cossart, C. Buchrieser, E. Gouin, P. Glaser, and J. Deutscher (2005). How seryl-phosphorylated HPr inhibits PrfA, a transcription activator of Listeria monocytogenes virulence genes. J Mol Microbiol Biotechnol, 9:224-34.
24. Lecuit, M. (2005). Understanding how Listeria monocytogenes targets and crosses host barriers. Clin Microbiol Infect, 11:430-6.
25. Lecuit, M., and P. Cossart (2005). [Molecular basis of Listeria monocytogenes fetoplacental tropism]. Med Sci (Paris), 21:17-9.
26. Mandin, P., H. Fsihi, O. Dussurget, M. Vergassola, E. Milohanic, A. Toledo-Arana, I. Lasa, J. Johansson, and P. Cossart (2005). VirR, a response regulator critical for Listeria monocytogenes virulence. Mol Microbiol, 57:1367-80.
27. Martinez, J. J., S. Seveau, E. Veiga, S. Matsuyama, and P. Cossart (2005). Ku70, a component of DNA-dependent protein kinase, is a mammalian receptor for Rickettsia conorii. Cell, 123:1013-23.
28. Pucciarelli, M. G., E. Calvo, C. Sabet, H. Bierne, P. Cossart, and F. Garcia-del Portillo (2005). Identification of substrates of the Listeria monocytogenes sortases A and B by a non-gel proteomic analysis. Proteomics, 5:4808-17.
29. Roche, S. M., P. Gracieux, E. Milohanic, I. Albert, I. Virlogeux-Payant, S. Temoin, O. Grepinet, A. Kerouanton, C. Jacquet, P. Cossart, and P. Velge (2005). Investigation of specific substitutions in virulence genes characterizing phenotypic groups of low-virulence field strains of Listeria monocytogenes. Appl Environ Microbiol, 71:6039-48.
30. Sabet, C., M. Lecuit, D. Cabanes, P. Cossart, and H. Bierne (2005). LPXTG protein InlJ, a newly identified internalin involved in Listeria monocytogenes virulence. Infect Immun, 73:6912-22.
31. Sousa, S., D. Cabanes, C. Archambaud, F. Colland, E. Lemichez, M. Popoff, S. Boisson-Dupuis, E. Gouin, M. Lecuit, P. Legrain, and P. Cossart (2005). ARHGAP10 is necessary for alpha-catenin recruitment at adherens junctions and for Listeria invasion. Nat Cell Biol, 7:954-60.
32. Sousa, S., M. Lecuit, and P. Cossart (2005). Microbial strategies to target, cross or disrupt epithelia. Curr Opin Cell Biol, 17:489-98.
33. Veiga, E., and P. Cossart (2005). Ubiquitination of intracellular bacteria: a new bacteria-sensing system? Trends Cell Biol, 15:2-5.
34. Veiga, E., and P. Cossart (2005). Listeria hijacks the clathrin-dependent endocytic machinery to invade mammalian cells. Nat Cell Biol, 7:894-900.
35. Dramsi S, Trieu-Cuot P, Bierne H. (2005) Sorting sortases: a nomenclature proposal for the various sortases of Gram-positive bacteria. Res Microbiol. 156(3):289-97.
36. Archambaud, C., M. A. Nahori, J. Pizarro-Cerda, P. Cossart, and O. Dussurget (2006). Control of Listeria superoxide dismutase by phosphorylation. J Biol Chem, 281:31812-22.
37. Hamon, M., H. Bierne, and P. Cossart (2006). Listeria monocytogenes: a multifaceted model. Nat Rev Microbiol, 4:423-34.
38. Khelef, N., M. Lecuit, H. Bierne, and P. Cossart (2006). Species specificity of the Listeria monocytogenes InlB protein. Cell Microbiol, 8:457-70.
39. Pizarro-Cerda, J., and P. Cossart (2006). Bacterial adhesion and entry into host cells. Cell, 124:715-27.
40. Veiga, E., and P. Cossart (2006). The role of clathrin-dependent endocytosis in bacterial internalization. Trends Cell Biol, 16:499-504.
41. Lebreton, A., Saveanu, C., Decourty, L., Rain, J-C., Jacquier, A. et Fromont-Racine, M. (2006) A functional network involved in the recycling of nucleo-cytoplasmic pre-60S factors. J. Cell Biol. 173(3):349-60.
42. Lebreton, A., Saveanu C., Decourty, L., Jacquier, A. et Fromont-Racine, M. (2006) Nsa2, an unstable, conserved factor required for the maturation of 27SB pre-rRNAs. J. Biol. Chem. 281(37):27099-108.
43. Boyer L., Doye A., Rolando M., Flatau G., Munro P., Gounon P., Clément R., Pulcini C., Popoff M.R., Mettouchi A., Landraud L., Dussurget O. and Lemichez L. (2006) Induction of transient macroapertures in endothelial cells through RhoA inhibition by Staphylococcus aureus factors. J Cell Biol 173: 809-819.
44. Bierne, H., and P. Cossart (2007). Listeria monocytogenes surface proteins: from genome predictions to function. Microbiol Mol Biol Rev, 71:377-97.
45. Bierne, H., C. Sabet, N. Personnic, and P. Cossart (2007). Internalins: a complex family of leucine-rich repeat-containing proteins in Listeria monocytogenes. Microbes Infect, 9:1156-66.
46. Birmingham, C. L., V. Canadien, E. Gouin, E. B. Troy, T. Yoshimori, P. Cossart, D. E. Higgins, and J. H. Brumell (2007). Listeria monocytogenes evades killing by autophagy during colonization of host cells. Autophagy, 3:442-51.
47. Boneca, I. G., O. Dussurget, D. Cabanes, M. A. Nahori, S. Sousa, M. Lecuit, E. Psylinakis, V. Bouriotis, J. P. Hugot, M. Giovannini, A. Coyle, J. Bertin, A. Namane, J. C. Rousselle, N. Cayet, M. C. Prevost, V. Balloy, M. Chignard, D. J. Philpott, P. Cossart, and S. E. Girardin (2007). A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system. Proc Natl Acad Sci U S A, 104:997-1002.
48. Cossart, P. (2007). Listeriology (1926-2007): the rise of a model pathogen. Microbes Infect, 9:1143-6.
49. Garcia-del Portillo, F., and P. Cossart (2007). An important step in listeria lipoprotein research. J Bacteriol, 189:294-7.
50. Hain, T., S. S. Chatterjee, R. Ghai, C. T. Kuenne, A. Billion, C. Steinweg, E. Domann, U. Karst, L. Jansch, J. Wehland, W. Eisenreich, A. Bacher, B. Joseph, J. Schar, J. Kreft, J. Klumpp, M. J. Loessner, J. Dorscht, K. Neuhaus, T. M. Fuchs, S. Scherer, M. Doumith, C. Jacquet, P. Martin, P. Cossart, C. Rusniock, P. Glaser, C. Buchrieser, W. Goebel, and T. Chakraborty (2007). Pathogenomics of Listeria spp. Int J Med Microbiol, 297:541-57.
51. Hamon, M. A., E. Batsche, B. Regnault, T. N. Tham, S. Seveau, C. Muchardt, and P. Cossart (2007). Histone modifications induced by a family of bacterial toxins. Proc Natl Acad Sci U S A, 104:13467-72.
52. Lecuit, M., J. L. Sonnenburg, P. Cossart, and J. I. Gordon (2007). Functional genomic studies of the intestinal response to a foodborne enteropathogen in a humanized gnotobiotic mouse model. J Biol Chem, 282:15065-72.
53. Mandin, P., F. Repoila, M. Vergassola, T. Geissmann, and P. Cossart (2007). Identification of new noncoding RNAs in Listeria monocytogenes and prediction of mRNA targets. Nucleic Acids Res, 35:962-74.
54. Pizarro-Cerda, J., B. Payrastre, Y. J. Wang, E. Veiga, H. L. Yin, and P. Cossart (2007). Type II phosphatidylinositol 4-kinases promote Listeria monocytogenes entry into target cells. Cell Microbiol, 9:2381-90.
55. Seveau, S., J. Pizarro-Cerda, and P. Cossart (2007). Molecular mechanisms exploited by Listeria monocytogenes during host cell invasion. Microbes Infect, 9:1167-75.
56. Seveau, S., T. N. Tham, B. Payrastre, A. D. Hoppe, J. A. Swanson, and P. Cossart (2007). A FRET analysis to unravel the role of cholesterol in Rac1 and PI 3-kinase activation in the InlB/Met signalling pathway. Cell Microbiol, 9:790-803.
57. Sousa, S., D. Cabanes, L. Bougneres, M. Lecuit, P. Sansonetti, G. Tran-Van-Nhieu, and P. Cossart (2007). Src, cortactin and Arp2/3 complex are required for E-cadherin-mediated internalization of Listeria into cells. Cell Microbiol, 9:2629-43.
58. Toledo-Arana, A., F. Repoila, and P. Cossart (2007). Small noncoding RNAs controlling pathogenesis. Curr Opin Microbiol, 10:182-8.
59. Veiga, E., and P. Cossart (2007). Listeria InlB takes a different route to met. Cell, 130:218-9.
60. Veiga, E., J. A. Guttman, M. Bonazzi, E. Boucrot, A. Toledo-Arana, A. E. Lin, J. Enninga, J. Pizarro-Cerda, B. B. Finlay, T. Kirchhausen, and P. Cossart (2007). Invasive and adherent bacterial pathogens co-Opt host clathrin for infection. Cell Host Microbe, 2:340-51.
61. Velge, P., M. Herler, J. Johansson, S. M. Roche, S. Temoin, A. A. Fedorov, P. Gracieux, S. C. Almo, W. Goebel, and P. Cossart (2007). A naturally occurring mutation K220T in the pleiotropic activator PrfA of Listeria monocytogenes results in a loss of virulence due to decreasing DNA-binding affinity. Microbiology, 153:995-1005.
62. Pertschy, B., Saveanu, C., Zisser, G., Lebreton, A., Tengg, M., Jacquier, A., Liebminger, E., Nobis, B., Kappel, L., van der Klei, I., Högenauer, G., Fromont-Racine, M. et Bergler, H. (2007). Cytoplasmic recycling of 60S pre-ribosomal factors depends on the AAA-protein Drg1. Mol. Cell. Biol. 27:6581-92.
63. Severino, P., Dussurget, O., Vencio, R.Z., Dumas, E., Garrido, P., Padilla, G., Piveteau, P., Lemaitre, J.P., Kunst, F., Glaser, P., Buchrieser, C. (2007) Comparative transcriptome analysis of Listeria monocytogenes strains of the two major lineages reveals differences in virulence, cell wall and stress response. Appl Environ Microbiol 73: 6078-88.
64. Brinster S, Posteraro B, Bierne H, Alberti A, Makhzami S, Sanguinetti M, Serror P. (2007) Enterococcal leucine-rich repeat-containing protein involved in virulence and host inflammatory response. Infect Immun. 75(9):4463-71.
2008
65. Bublitz, M., C. Holland, C. Sabet, J. Reichelt, P. Cossart, D. W. Heinz, H. Bierne, and W. D. Schubert (2008). Crystal structure and standardized geometric analysis of InlJ, a listerial virulence factor and leucine-rich repeat protein with a novel cysteine ladder. J Mol Biol, 378:87-96.
66. Cabanes, D., M. Lecuit, and P. Cossart (2008). Animal models of listeria infection. Curr Protoc Microbiol, 9: in press.
67. Lambrechts, A., K. Gevaert, P. Cossart, J. Vandekerckhove, and M. Van Troys (2008). Listeria comet tails: the actin-based motility machinery at work. Trends Cell Biol, 18:220-7.
68. Linden, S. K., H. Bierne, C. Sabet, C. W. Png, T. H. Florin, M. A. McGuckin, and P. Cossart (2008). Listeria monocytogenes internalins bind to the human intestinal mucin MUC2. Arch Microbiol, 190:101-4.
69. Sabet, C., A. Toledo-Arana, N. Personnic, M. Lecuit, S. Dubrac, O. Poupel, E. Gouin, M. A. Nahori, P. Cossart, and H. Bierne (2008). The Listeria monocytogenes virulence factor InlJ is specifically expressed in vivo and behaves as an adhesin. Infect Immun, 76:1368-78.
70. Van Troys, M., A. Lambrechts, V. David, H. Demol, M. Puype, J. Pizarro-Cerda, K. Gevaert, P. Cossart, and J. Vandekerckhove (2008). The actin propulsive machinery: The proteome of Listeria monocytogenes tails. Biochem Biophys Res Commun, 375:194-9.
71. Hamon, M. A., and P. Cossart (2008). Histone modifications and chromatin remodeling during bacterial infections. Cell Host Microbe, 4:100-9.
72. Cossart, P., and E. Veiga (2008). Non-classical use of clathrin during bacterial infections. J Microsc, 231:524-8.
73. Cossart, P., and A. Toledo-Arana (2008). Listeria monocytogenes, a unique model in infection biology: An overview. Microbes Infect., 10:1041-50.
74. Bonazzi, M., E. Veiga, J. P. Cerda, and P. Cossart (2008). Successive post-translational modifications of E-cadherin are required for InlA-mediated internalisation of Listeria monocytogenes. Cell Microbiol. in press.
75. Disson, O., Grayo, S., Huillet, E., Nikitas, G., Langa-Vives, F., Dussurget, O., Ragon, M., Le Monnier, A., Babinet, C., P. Cossart and M. Lecuit (2008) Conjugated action of two species-specific invasion proteins for fetoplacental listeriosis. Nature, 455(7216):1114-8.
76. Lebreton A, Rafal T, Dziembowski A et Séraphin B. (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature. 456: In press.
77. Lebreton, A. et Séraphin, B. (2008) Exosome-mediated quality control: substrate recruitment and molecular activity. BBA – Gene Regulatory Mechanisms. 1779: 558-65.
78. Lebreton, A., Rousselle, J.C., Lenormand, P., Namane, A., Jacquier, A., Fromont-Racine, M. et Saveanu, C. (2008) Large ribosomal subunit assembly dynamics defined by semi-quantitative mass spectrometry of purified complexes. Nucleic Acids Res. 36:4988-4999.
79. Grayo, S., Lott-Desroches, M.C., Dussurget, O., Respaud, R., Fontanet, A., Join-Lambert, O., Singlas, E. and Le Monnier, A. (2008) Rapid eradication of Listeria monocytogenes by moxifloxacin in a murine model of central nervous system listeriosis. Antimicrob Agents Chemother 52: 3210-5.
80. Gueriri, I., Cyncynatus, C., Dubrac, S., Arana, A.T., Dussurget, O. and Msadek, T. (2008) The DegU orphan response regulator of Listeria monocytogenes autorepresses its own synthesis and is required for bacterial motility, virulence and biofilm formation. Microbiology 154:2251-64.
81. Brock, M., Jouvion, G., Droin-Bergère, S., Dussurget, O., Nicola, M.A. and Ibrahim-Granet, O. (2008) Bioluminescent Aspergillus fumigatus, a new tool for drug efficiency testing and in vivo monitoring of invasive aspergillosis. Appl Environ Microbiol 74:7023-35.
82. Mostowy, S., To Tham, N., Danckaert, A., Guadagnini, S., Boisson-Dupuis, S., Pizarro-Cerdá, J., and Cossart, P. Septins regulate the InlB/Met-mediated entry of Listeria monocytogenes into host cells. PLOS One: In Press.
2. Cossart, P. (2004). Bacterial invasion: a new strategy to dominate cytoskeleton plasticity. Dev Cell, 6:314-5.
3. Cossart, P., and P. J. Sansonetti (2004). Bacterial invasion: the paradigms of enteroinvasive pathogens. Science, 304:242-8.
4. Doumith, M., C. Cazalet, N. Simoes, L. Frangeul, C. Jacquet, F. Kunst, P. Martin, P. Cossart, P. Glaser, and C. Buchrieser (2004). New aspects regarding evolution and virulence of Listeria monocytogenes revealed by comparative genomics and DNA arrays. Infect Immun, 72:1072-83.
5. Dramsi, S., F. Bourdichon, D. Cabanes, M. Lecuit, H. Fsihi, and P. Cossart (2004). FbpA, a novel multifunctional Listeria monocytogenes virulence factor. Mol Microbiol, 53:639-49.
6. Dussurget, O., J. Pizarro-Cerda, and P. Cossart (2004). Molecular determinants of Listeria monocytogenes virulence. Annu Rev Microbiol, 58:587-610.
7. Gouin, E., C. Egile, P. Dehoux, V. Villiers, J. Adams, F. Gertler, R. Li, and P. Cossart (2004). The RickA protein of Rickettsia conorii activates the Arp2/3 complex. Nature, 427:457-61.
8. Jacquet, C., M. Doumith, J. I. Gordon, P. M. Martin, P. Cossart, and M. Lecuit (2004). A molecular marker for evaluating the pathogenic potential of foodborne Listeria monocytogenes. J Infect Dis, 189:2094-100.
9. Lecuit, M., D. M. Nelson, S. D. Smith, H. Khun, M. Huerre, M. C. Vacher-Lavenu, J. I. Gordon, and P. Cossart (2004). Targeting and crossing of the human maternofetal barrier by Listeria monocytogenes: role of internalin interaction with trophoblast E-cadherin. Proc Natl Acad Sci USA, 101:6152-7.
10. Marino, M., M. Banerjee, J. Copp, S. Dramsi, T. Chapman, P. van der Geer, P. Cossart, and P. Ghosh (2004). Characterization of the calcium-binding sites of Listeria monocytogenes InlB. Biochem Biophys Res Commun, 316:379-86.
11. Martinez, J. J., and P. Cossart (2004). Early signaling events involved in the entry of Rickettsia conorii into mammalian cells. J Cell Sci, 117:5097-106.
12. Milohanic, E., R. Jonquieres, P. Glaser, P. Dehoux, C. Jacquet, P. Berche, P. Cossart, and J. L. Gaillard (2004). Sequence and binding activity of the autolysin-adhesin Ami from epidemic Listeria monocytogenes 4b. Infect Immun, 72:4401-9.
13. Pizarro-Cerda, J., and P. Cossart (2004). Subversion of phosphoinositide metabolism by intracellular bacterial pathogens. Nat Cell Biol, 6:1026-33.
14. Seveau, S., H. Bierne, S. Giroux, M. C. Prevost, and P. Cossart (2004). Role of lipid rafts in E-cadherin-- and HGF-R/Met--mediated entry of Listeria monocytogenes into host cells. J Cell Biol, 166:743-53.
15. Sousa, S., D. Cabanes, A. El-Amraoui, C. Petit, M. Lecuit, and P. Cossart (2004). Unconventional myosin VIIa and vezatin, two proteins crucial for Listeria entry into epithelial cells. J Cell Sci, 117:2121-30.
16. Archambaud, C., E. Gouin, J. Pizarro-Cerda, P. Cossart, and O. Dussurget (2005). Translation elongation factor EF-Tu is a target for Stp, a serine-threonine phosphatase involved in virulence of Listeria monocytogenes. Mol Microbiol, 56:383-96.
17. Bierne, H., H. Miki, M. Innocenti, G. Scita, F. B. Gertler, T. Takenawa, and P. Cossart (2005). WASP-related proteins, Abi1 and Ena/VASP are required for Listeria invasion induced by the Met receptor. J Cell Sci, 118:1537-47.
18. Cabanes, D., S. Sousa, A. Cebria, M. Lecuit, F. Garcia-del Portillo, and P. Cossart (2005). Gp96 is a receptor for a novel Listeria monocytogenes virulence factor, Vip, a surface protein. Embo J, 24:2827-38.
19. Calvo, E., M. G. Pucciarelli, H. Bierne, P. Cossart, J. P. Albar, and F. Garcia-Del Portillo (2005). Analysis of the Listeria cell wall proteome by two-dimensional nanoliquid chromatography coupled to mass spectrometry. Proteomics, 5:433-43.
20. Dussurget, O., E. Dumas, C. Archambaud, I. Chafsey, C. Chambon, M. Hebraud, and P. Cossart (2005). Listeria monocytogenes ferritin protects against multiple stresses and is required for virulence. FEMS Microbiol Lett, 250:253-61.
21. Gouin, E., M. D. Welch, and P. Cossart (2005). Actin-based motility of intracellular pathogens. Curr Opin Microbiol, 8:35-45.
22. Guimaraes, V. D., J. E. Gabriel, F. Lefevre, D. Cabanes, A. Gruss, P. Cossart, V. Azevedo, and P. Langella (2005). Internalin-expressing Lactococcus lactis is able to invade small intestine of guinea pigs and deliver DNA into mammalian epithelial cells. Microbes Infect, 7:836-44.
23. Herro, R., S. Poncet, P. Cossart, C. Buchrieser, E. Gouin, P. Glaser, and J. Deutscher (2005). How seryl-phosphorylated HPr inhibits PrfA, a transcription activator of Listeria monocytogenes virulence genes. J Mol Microbiol Biotechnol, 9:224-34.
24. Lecuit, M. (2005). Understanding how Listeria monocytogenes targets and crosses host barriers. Clin Microbiol Infect, 11:430-6.
25. Lecuit, M., and P. Cossart (2005). [Molecular basis of Listeria monocytogenes fetoplacental tropism]. Med Sci (Paris), 21:17-9.
26. Mandin, P., H. Fsihi, O. Dussurget, M. Vergassola, E. Milohanic, A. Toledo-Arana, I. Lasa, J. Johansson, and P. Cossart (2005). VirR, a response regulator critical for Listeria monocytogenes virulence. Mol Microbiol, 57:1367-80.
27. Martinez, J. J., S. Seveau, E. Veiga, S. Matsuyama, and P. Cossart (2005). Ku70, a component of DNA-dependent protein kinase, is a mammalian receptor for Rickettsia conorii. Cell, 123:1013-23.
28. Pucciarelli, M. G., E. Calvo, C. Sabet, H. Bierne, P. Cossart, and F. Garcia-del Portillo (2005). Identification of substrates of the Listeria monocytogenes sortases A and B by a non-gel proteomic analysis. Proteomics, 5:4808-17.
29. Roche, S. M., P. Gracieux, E. Milohanic, I. Albert, I. Virlogeux-Payant, S. Temoin, O. Grepinet, A. Kerouanton, C. Jacquet, P. Cossart, and P. Velge (2005). Investigation of specific substitutions in virulence genes characterizing phenotypic groups of low-virulence field strains of Listeria monocytogenes. Appl Environ Microbiol, 71:6039-48.
30. Sabet, C., M. Lecuit, D. Cabanes, P. Cossart, and H. Bierne (2005). LPXTG protein InlJ, a newly identified internalin involved in Listeria monocytogenes virulence. Infect Immun, 73:6912-22.
31. Sousa, S., D. Cabanes, C. Archambaud, F. Colland, E. Lemichez, M. Popoff, S. Boisson-Dupuis, E. Gouin, M. Lecuit, P. Legrain, and P. Cossart (2005). ARHGAP10 is necessary for alpha-catenin recruitment at adherens junctions and for Listeria invasion. Nat Cell Biol, 7:954-60.
32. Sousa, S., M. Lecuit, and P. Cossart (2005). Microbial strategies to target, cross or disrupt epithelia. Curr Opin Cell Biol, 17:489-98.
33. Veiga, E., and P. Cossart (2005). Ubiquitination of intracellular bacteria: a new bacteria-sensing system? Trends Cell Biol, 15:2-5.
34. Veiga, E., and P. Cossart (2005). Listeria hijacks the clathrin-dependent endocytic machinery to invade mammalian cells. Nat Cell Biol, 7:894-900.
35. Dramsi S, Trieu-Cuot P, Bierne H. (2005) Sorting sortases: a nomenclature proposal for the various sortases of Gram-positive bacteria. Res Microbiol. 156(3):289-97.
36. Archambaud, C., M. A. Nahori, J. Pizarro-Cerda, P. Cossart, and O. Dussurget (2006). Control of Listeria superoxide dismutase by phosphorylation. J Biol Chem, 281:31812-22.
37. Hamon, M., H. Bierne, and P. Cossart (2006). Listeria monocytogenes: a multifaceted model. Nat Rev Microbiol, 4:423-34.
38. Khelef, N., M. Lecuit, H. Bierne, and P. Cossart (2006). Species specificity of the Listeria monocytogenes InlB protein. Cell Microbiol, 8:457-70.
39. Pizarro-Cerda, J., and P. Cossart (2006). Bacterial adhesion and entry into host cells. Cell, 124:715-27.
40. Veiga, E., and P. Cossart (2006). The role of clathrin-dependent endocytosis in bacterial internalization. Trends Cell Biol, 16:499-504.
41. Lebreton, A., Saveanu, C., Decourty, L., Rain, J-C., Jacquier, A. et Fromont-Racine, M. (2006) A functional network involved in the recycling of nucleo-cytoplasmic pre-60S factors. J. Cell Biol. 173(3):349-60.
42. Lebreton, A., Saveanu C., Decourty, L., Jacquier, A. et Fromont-Racine, M. (2006) Nsa2, an unstable, conserved factor required for the maturation of 27SB pre-rRNAs. J. Biol. Chem. 281(37):27099-108.
43. Boyer L., Doye A., Rolando M., Flatau G., Munro P., Gounon P., Clément R., Pulcini C., Popoff M.R., Mettouchi A., Landraud L., Dussurget O. and Lemichez L. (2006) Induction of transient macroapertures in endothelial cells through RhoA inhibition by Staphylococcus aureus factors. J Cell Biol 173: 809-819.
44. Bierne, H., and P. Cossart (2007). Listeria monocytogenes surface proteins: from genome predictions to function. Microbiol Mol Biol Rev, 71:377-97.
45. Bierne, H., C. Sabet, N. Personnic, and P. Cossart (2007). Internalins: a complex family of leucine-rich repeat-containing proteins in Listeria monocytogenes. Microbes Infect, 9:1156-66.
46. Birmingham, C. L., V. Canadien, E. Gouin, E. B. Troy, T. Yoshimori, P. Cossart, D. E. Higgins, and J. H. Brumell (2007). Listeria monocytogenes evades killing by autophagy during colonization of host cells. Autophagy, 3:442-51.
47. Boneca, I. G., O. Dussurget, D. Cabanes, M. A. Nahori, S. Sousa, M. Lecuit, E. Psylinakis, V. Bouriotis, J. P. Hugot, M. Giovannini, A. Coyle, J. Bertin, A. Namane, J. C. Rousselle, N. Cayet, M. C. Prevost, V. Balloy, M. Chignard, D. J. Philpott, P. Cossart, and S. E. Girardin (2007). A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system. Proc Natl Acad Sci U S A, 104:997-1002.
48. Cossart, P. (2007). Listeriology (1926-2007): the rise of a model pathogen. Microbes Infect, 9:1143-6.
49. Garcia-del Portillo, F., and P. Cossart (2007). An important step in listeria lipoprotein research. J Bacteriol, 189:294-7.
50. Hain, T., S. S. Chatterjee, R. Ghai, C. T. Kuenne, A. Billion, C. Steinweg, E. Domann, U. Karst, L. Jansch, J. Wehland, W. Eisenreich, A. Bacher, B. Joseph, J. Schar, J. Kreft, J. Klumpp, M. J. Loessner, J. Dorscht, K. Neuhaus, T. M. Fuchs, S. Scherer, M. Doumith, C. Jacquet, P. Martin, P. Cossart, C. Rusniock, P. Glaser, C. Buchrieser, W. Goebel, and T. Chakraborty (2007). Pathogenomics of Listeria spp. Int J Med Microbiol, 297:541-57.
51. Hamon, M. A., E. Batsche, B. Regnault, T. N. Tham, S. Seveau, C. Muchardt, and P. Cossart (2007). Histone modifications induced by a family of bacterial toxins. Proc Natl Acad Sci U S A, 104:13467-72.
52. Lecuit, M., J. L. Sonnenburg, P. Cossart, and J. I. Gordon (2007). Functional genomic studies of the intestinal response to a foodborne enteropathogen in a humanized gnotobiotic mouse model. J Biol Chem, 282:15065-72.
53. Mandin, P., F. Repoila, M. Vergassola, T. Geissmann, and P. Cossart (2007). Identification of new noncoding RNAs in Listeria monocytogenes and prediction of mRNA targets. Nucleic Acids Res, 35:962-74.
54. Pizarro-Cerda, J., B. Payrastre, Y. J. Wang, E. Veiga, H. L. Yin, and P. Cossart (2007). Type II phosphatidylinositol 4-kinases promote Listeria monocytogenes entry into target cells. Cell Microbiol, 9:2381-90.
55. Seveau, S., J. Pizarro-Cerda, and P. Cossart (2007). Molecular mechanisms exploited by Listeria monocytogenes during host cell invasion. Microbes Infect, 9:1167-75.
56. Seveau, S., T. N. Tham, B. Payrastre, A. D. Hoppe, J. A. Swanson, and P. Cossart (2007). A FRET analysis to unravel the role of cholesterol in Rac1 and PI 3-kinase activation in the InlB/Met signalling pathway. Cell Microbiol, 9:790-803.
57. Sousa, S., D. Cabanes, L. Bougneres, M. Lecuit, P. Sansonetti, G. Tran-Van-Nhieu, and P. Cossart (2007). Src, cortactin and Arp2/3 complex are required for E-cadherin-mediated internalization of Listeria into cells. Cell Microbiol, 9:2629-43.
58. Toledo-Arana, A., F. Repoila, and P. Cossart (2007). Small noncoding RNAs controlling pathogenesis. Curr Opin Microbiol, 10:182-8.
59. Veiga, E., and P. Cossart (2007). Listeria InlB takes a different route to met. Cell, 130:218-9.
60. Veiga, E., J. A. Guttman, M. Bonazzi, E. Boucrot, A. Toledo-Arana, A. E. Lin, J. Enninga, J. Pizarro-Cerda, B. B. Finlay, T. Kirchhausen, and P. Cossart (2007). Invasive and adherent bacterial pathogens co-Opt host clathrin for infection. Cell Host Microbe, 2:340-51.
61. Velge, P., M. Herler, J. Johansson, S. M. Roche, S. Temoin, A. A. Fedorov, P. Gracieux, S. C. Almo, W. Goebel, and P. Cossart (2007). A naturally occurring mutation K220T in the pleiotropic activator PrfA of Listeria monocytogenes results in a loss of virulence due to decreasing DNA-binding affinity. Microbiology, 153:995-1005.
62. Pertschy, B., Saveanu, C., Zisser, G., Lebreton, A., Tengg, M., Jacquier, A., Liebminger, E., Nobis, B., Kappel, L., van der Klei, I., Högenauer, G., Fromont-Racine, M. et Bergler, H. (2007). Cytoplasmic recycling of 60S pre-ribosomal factors depends on the AAA-protein Drg1. Mol. Cell. Biol. 27:6581-92.
63. Severino, P., Dussurget, O., Vencio, R.Z., Dumas, E., Garrido, P., Padilla, G., Piveteau, P., Lemaitre, J.P., Kunst, F., Glaser, P., Buchrieser, C. (2007) Comparative transcriptome analysis of Listeria monocytogenes strains of the two major lineages reveals differences in virulence, cell wall and stress response. Appl Environ Microbiol 73: 6078-88.
64. Brinster S, Posteraro B, Bierne H, Alberti A, Makhzami S, Sanguinetti M, Serror P. (2007) Enterococcal leucine-rich repeat-containing protein involved in virulence and host inflammatory response. Infect Immun. 75(9):4463-71.
2008
65. Bublitz, M., C. Holland, C. Sabet, J. Reichelt, P. Cossart, D. W. Heinz, H. Bierne, and W. D. Schubert (2008). Crystal structure and standardized geometric analysis of InlJ, a listerial virulence factor and leucine-rich repeat protein with a novel cysteine ladder. J Mol Biol, 378:87-96.
66. Cabanes, D., M. Lecuit, and P. Cossart (2008). Animal models of listeria infection. Curr Protoc Microbiol, 9: in press.
67. Lambrechts, A., K. Gevaert, P. Cossart, J. Vandekerckhove, and M. Van Troys (2008). Listeria comet tails: the actin-based motility machinery at work. Trends Cell Biol, 18:220-7.
68. Linden, S. K., H. Bierne, C. Sabet, C. W. Png, T. H. Florin, M. A. McGuckin, and P. Cossart (2008). Listeria monocytogenes internalins bind to the human intestinal mucin MUC2. Arch Microbiol, 190:101-4.
69. Sabet, C., A. Toledo-Arana, N. Personnic, M. Lecuit, S. Dubrac, O. Poupel, E. Gouin, M. A. Nahori, P. Cossart, and H. Bierne (2008). The Listeria monocytogenes virulence factor InlJ is specifically expressed in vivo and behaves as an adhesin. Infect Immun, 76:1368-78.
70. Van Troys, M., A. Lambrechts, V. David, H. Demol, M. Puype, J. Pizarro-Cerda, K. Gevaert, P. Cossart, and J. Vandekerckhove (2008). The actin propulsive machinery: The proteome of Listeria monocytogenes tails. Biochem Biophys Res Commun, 375:194-9.
71. Hamon, M. A., and P. Cossart (2008). Histone modifications and chromatin remodeling during bacterial infections. Cell Host Microbe, 4:100-9.
72. Cossart, P., and E. Veiga (2008). Non-classical use of clathrin during bacterial infections. J Microsc, 231:524-8.
73. Cossart, P., and A. Toledo-Arana (2008). Listeria monocytogenes, a unique model in infection biology: An overview. Microbes Infect., 10:1041-50.
74. Bonazzi, M., E. Veiga, J. P. Cerda, and P. Cossart (2008). Successive post-translational modifications of E-cadherin are required for InlA-mediated internalisation of Listeria monocytogenes. Cell Microbiol. in press.
75. Disson, O., Grayo, S., Huillet, E., Nikitas, G., Langa-Vives, F., Dussurget, O., Ragon, M., Le Monnier, A., Babinet, C., P. Cossart and M. Lecuit (2008) Conjugated action of two species-specific invasion proteins for fetoplacental listeriosis. Nature, 455(7216):1114-8.
76. Lebreton A, Rafal T, Dziembowski A et Séraphin B. (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature. 456: In press.
77. Lebreton, A. et Séraphin, B. (2008) Exosome-mediated quality control: substrate recruitment and molecular activity. BBA – Gene Regulatory Mechanisms. 1779: 558-65.
78. Lebreton, A., Rousselle, J.C., Lenormand, P., Namane, A., Jacquier, A., Fromont-Racine, M. et Saveanu, C. (2008) Large ribosomal subunit assembly dynamics defined by semi-quantitative mass spectrometry of purified complexes. Nucleic Acids Res. 36:4988-4999.
79. Grayo, S., Lott-Desroches, M.C., Dussurget, O., Respaud, R., Fontanet, A., Join-Lambert, O., Singlas, E. and Le Monnier, A. (2008) Rapid eradication of Listeria monocytogenes by moxifloxacin in a murine model of central nervous system listeriosis. Antimicrob Agents Chemother 52: 3210-5.
80. Gueriri, I., Cyncynatus, C., Dubrac, S., Arana, A.T., Dussurget, O. and Msadek, T. (2008) The DegU orphan response regulator of Listeria monocytogenes autorepresses its own synthesis and is required for bacterial motility, virulence and biofilm formation. Microbiology 154:2251-64.
81. Brock, M., Jouvion, G., Droin-Bergère, S., Dussurget, O., Nicola, M.A. and Ibrahim-Granet, O. (2008) Bioluminescent Aspergillus fumigatus, a new tool for drug efficiency testing and in vivo monitoring of invasive aspergillosis. Appl Environ Microbiol 74:7023-35.
82. Mostowy, S., To Tham, N., Danckaert, A., Guadagnini, S., Boisson-Dupuis, S., Pizarro-Cerdá, J., and Cossart, P. Septins regulate the InlB/Met-mediated entry of Listeria monocytogenes into host cells. PLOS One: In Press.
Non peer reviewed chapters, reviews and books
1. Pizarro-Cerda, J., S. Sousa and P. Cossart (2004). Exploitation of host cell cytoskeleton and signalling during Listeria monocytogenes entry into mammalian cells. C. R. Biol., 327 : 115-123. Cellular Microbiology, 2nd Edition. (2005) Edited by P. Cossart, P. Boquet, S. Normak and R. Rappuoli. ASM Press, Washington, DC.
2. Cossart, P., J. Pizarro-Cerda and M. Lecuit (2005) Microbiol pathogens : an overview. In Cellular Microbiology, 2nd Edition. Edited by P. Cossart, P. Boquet, S. Normark and R. Rappuoli. ASM Press, Washington, DC.
3. Lecuit, M., and P. Cossart (2005) Bases moléculaires du tropisme foetoplacentaire de Listeria monocytogenes. Med. Sci. (Paris), 21 : 17-19.
4. Galan, J.-E., and P. Cossart (2005) Host-pathogen interactions : a diversity of themes, a variety of molecular machines. Curr. Opin. Microbiol., 8 :1-3.
5. Cossart, P. (2005) Host specificity : the Listeria paradigm. Nova Acta Leopold., NF92, 344 : 163-166.
6. Cossart, P. (2005) Physiologie moléculaire des infections bactériennes : un dialogue complexe entre les bactéries pathogènes et leurs cibles. La Lettre de l’Académie des sciences 17 : 8-9.
7. Khelef, N., M. Lecuit, C. Buchrieser, D. Cabanes, O. Dussurget and P. Cossart « Listeria monocytogenes and the Genus Listeria ». In The Prokaryotes : an evolving electronic resource for the microbiological community. (2005) Edited by M. Dworkin, S. Falkow, E. Rosenberg, K-H. Schleifer, and E., Stackebrandt, eds.3rd edition, release 3.XX, Month 2005, Springer, New York.
8. Pizarro-Cerda, J., and P. Cossart (2006) The cell biology of invasion and intracellular growth by Listeria monocytogenes. In Gram Positive Pathogens. 2nd Edition. Edited by V. Fischetti and D. Portnoy. ASM Press, Washington, DC. 646-656.
9. Pizarro-Cerda, J., and P. Cossart (2006). Listeria monocytogenes : Techniques to analyze bacterial infection in vitro. In Cell biology : a laboratory handbook, 3rd Edition. Edited by J. E. Celis. Academic Press, London. 407-415.
10. Pizarro-Cerda, J., and P. Cossart (2006) Subversion of cellular functions by Listeria monocytogenes. J. Pathol., 208 : 215-223.
11. Bonazzi, M., and P. Cossart (2006) Bacterial entry into cells : a role for the endocytic machinery. FEBS Lett., 580 : 2962-2967.
12. Pizarro-Cerda, J., and P. Cossart (2007). Invasion of Host Cells by Listeria monocytogenes : In Listeria monocytogenes : Pathogenesis and Host Response, (Chapter 8), 1st Edition. Edited by H. Goldfine and J. Shen, Springer.
13. Swaminathan, B., D. Cabanes, W. Zhang and P. Cossart Listeria monocytogenes (Chapter 21) in Food Microbiology, 3rd edition. Edited by Michael P.Doyle and Larry R. Beuchat, ASM Press, Washington, D.C. 457-491.
14. Davies, J., P. Cossart and L. Cole (2007) Current Opinion in Microbiology: 10th Anniversary Volume. Curr. Opin. Microbiol., 10 : 91-92.
15. Buchrieser, C., and P. Cossart (2007) What has genomics taught us about intra-cellular pathogens: The example of Listeria monocytogenes; Ed Mark Pallen, Steven Gill, Karen Nelson and Gail Preston, ASM Press, Washington D. C, pp 361-391
16. Hain, T., Chatterjee SS, Ghai R, Kuenne CT, Billion A, Steinweg C, Domann E, Kärst U, Jänsch L, Wehland J, Eisenreich W, Bacher A, Joseph B, Schär J, Kreft J, Klumpp J, Loessner MJ, Dorscht J, Neuhaus K, Fuchs TM, Scherer S, Doumith M, Jacquet C, Martin P, Cossart P, Rusniock C, Glaser P, Buchrieser C, Goebel W and T Chakraborty (2007). Pathogenomics of Listeria spp. Intern J Med Microbiol 297(7-8):541-57
17. Cossart, P., C Buchrieser and J Kreft (2007) The evolution of Listeria monocytogenes. In: Introduction to the Evolutionary Biology of Bacterial and Fungal Pathogens; Eds César Nombela, Fernando Baquero and José A. Gutiérrez-Fuentes, The Lilly Foundation, in press
18. Cossart, P., C Buchrieser and J. Kreft (2008) Evolution of Listeria monocytogenes. In Evolutionary Biology of Bacterial and Fungal Pathogens. Edited by F Baquero, C. Nombela, G. H. Cassel, J.A. Gutiérrez-Fuentes. ASM Press, Washington, DC . 491-499.
19. Cabanes, D., M. Lecuit and P Cossart (2008) Animal models of Listeria infection. In Current Protocols in Microbiology, In Wiley Interscience.
20. Ribet, D., and P. Cossart (2008) Facteurs de virulene de Listeria monocytogenes et détournement des fonctions cellulaires de l’hôte. Journal de l’association des anciens élèves de l’Institut Pasteur, n° 195 vol 50 : 65-70.
21. D. Balestrino and P. Cossart (2008) Listeria. In Intracellular Niches of Pathogens – A microbe’s guide through The Host Cell. Edited by U.E. Schaibe and A. Hass. Wiley-VCH Publishers, London. (in press).
2. Cossart, P., J. Pizarro-Cerda and M. Lecuit (2005) Microbiol pathogens : an overview. In Cellular Microbiology, 2nd Edition. Edited by P. Cossart, P. Boquet, S. Normark and R. Rappuoli. ASM Press, Washington, DC.
3. Lecuit, M., and P. Cossart (2005) Bases moléculaires du tropisme foetoplacentaire de Listeria monocytogenes. Med. Sci. (Paris), 21 : 17-19.
4. Galan, J.-E., and P. Cossart (2005) Host-pathogen interactions : a diversity of themes, a variety of molecular machines. Curr. Opin. Microbiol., 8 :1-3.
5. Cossart, P. (2005) Host specificity : the Listeria paradigm. Nova Acta Leopold., NF92, 344 : 163-166.
6. Cossart, P. (2005) Physiologie moléculaire des infections bactériennes : un dialogue complexe entre les bactéries pathogènes et leurs cibles. La Lettre de l’Académie des sciences 17 : 8-9.
7. Khelef, N., M. Lecuit, C. Buchrieser, D. Cabanes, O. Dussurget and P. Cossart « Listeria monocytogenes and the Genus Listeria ». In The Prokaryotes : an evolving electronic resource for the microbiological community. (2005) Edited by M. Dworkin, S. Falkow, E. Rosenberg, K-H. Schleifer, and E., Stackebrandt, eds.3rd edition, release 3.XX, Month 2005, Springer, New York.
8. Pizarro-Cerda, J., and P. Cossart (2006) The cell biology of invasion and intracellular growth by Listeria monocytogenes. In Gram Positive Pathogens. 2nd Edition. Edited by V. Fischetti and D. Portnoy. ASM Press, Washington, DC. 646-656.
9. Pizarro-Cerda, J., and P. Cossart (2006). Listeria monocytogenes : Techniques to analyze bacterial infection in vitro. In Cell biology : a laboratory handbook, 3rd Edition. Edited by J. E. Celis. Academic Press, London. 407-415.
10. Pizarro-Cerda, J., and P. Cossart (2006) Subversion of cellular functions by Listeria monocytogenes. J. Pathol., 208 : 215-223.
11. Bonazzi, M., and P. Cossart (2006) Bacterial entry into cells : a role for the endocytic machinery. FEBS Lett., 580 : 2962-2967.
12. Pizarro-Cerda, J., and P. Cossart (2007). Invasion of Host Cells by Listeria monocytogenes : In Listeria monocytogenes : Pathogenesis and Host Response, (Chapter 8), 1st Edition. Edited by H. Goldfine and J. Shen, Springer.
13. Swaminathan, B., D. Cabanes, W. Zhang and P. Cossart Listeria monocytogenes (Chapter 21) in Food Microbiology, 3rd edition. Edited by Michael P.Doyle and Larry R. Beuchat, ASM Press, Washington, D.C. 457-491.
14. Davies, J., P. Cossart and L. Cole (2007) Current Opinion in Microbiology: 10th Anniversary Volume. Curr. Opin. Microbiol., 10 : 91-92.
15. Buchrieser, C., and P. Cossart (2007) What has genomics taught us about intra-cellular pathogens: The example of Listeria monocytogenes; Ed Mark Pallen, Steven Gill, Karen Nelson and Gail Preston, ASM Press, Washington D. C, pp 361-391
16. Hain, T., Chatterjee SS, Ghai R, Kuenne CT, Billion A, Steinweg C, Domann E, Kärst U, Jänsch L, Wehland J, Eisenreich W, Bacher A, Joseph B, Schär J, Kreft J, Klumpp J, Loessner MJ, Dorscht J, Neuhaus K, Fuchs TM, Scherer S, Doumith M, Jacquet C, Martin P, Cossart P, Rusniock C, Glaser P, Buchrieser C, Goebel W and T Chakraborty (2007). Pathogenomics of Listeria spp. Intern J Med Microbiol 297(7-8):541-57
17. Cossart, P., C Buchrieser and J Kreft (2007) The evolution of Listeria monocytogenes. In: Introduction to the Evolutionary Biology of Bacterial and Fungal Pathogens; Eds César Nombela, Fernando Baquero and José A. Gutiérrez-Fuentes, The Lilly Foundation, in press
18. Cossart, P., C Buchrieser and J. Kreft (2008) Evolution of Listeria monocytogenes. In Evolutionary Biology of Bacterial and Fungal Pathogens. Edited by F Baquero, C. Nombela, G. H. Cassel, J.A. Gutiérrez-Fuentes. ASM Press, Washington, DC . 491-499.
19. Cabanes, D., M. Lecuit and P Cossart (2008) Animal models of Listeria infection. In Current Protocols in Microbiology, In Wiley Interscience.
20. Ribet, D., and P. Cossart (2008) Facteurs de virulene de Listeria monocytogenes et détournement des fonctions cellulaires de l’hôte. Journal de l’association des anciens élèves de l’Institut Pasteur, n° 195 vol 50 : 65-70.
21. D. Balestrino and P. Cossart (2008) Listeria. In Intracellular Niches of Pathogens – A microbe’s guide through The Host Cell. Edited by U.E. Schaibe and A. Hass. Wiley-VCH Publishers, London. (in press).