Recherche / Départements scientifiques / Biologie cellulaire et infection / Unités et groupes / Unité des Interactions Bactéries-Cellules / 1994-2006
1994-2006 Scientific Work Report
Couverture du rapport des 12 ans
Our scientific activity during the last twelve years has essentially led to :
1. The discovery and/or characterization of several virulence factors of L. monocytogenes,
2. The discovery of a new type of regulation mediated by an RNA thermosensor,
3. The determination of the complete genome sequences of L. monocytogenes and of L. innocua, a closely related non pathogenic species,
4. The discovery of the internalin receptor, E-cadherin,
5. The discovery of several key cellular components allowing the internalin-mediated entry,
6. The demonstration of the internalin/E-cadherin and InlB/Met species specificities,
7. The dissection of the complex signaling pathways triggered during the InlB-mediated entry, and the identification of two InlB receptors,
8. The elucidation of the role of rafts in the entry of Listeria,
9. The identification of the unexpected critical role of the endocytic machinery in bacterial entry,
10. The clarification of the mechanism used by Listeria to polymerize actin and move,
11. The discovery of the Vaccinia virus capacity to polymerize actin,
12. The identification of a novel actin nucleator produced by Rickettsia conorii,
13. The identification of the role of internalin in the crossing of the intestinal barrier, after generating the first transgenic model used to analyze a bacterial human disease,
14. The validation of the role of internalin in human listeriosis by an epidemiological survey of a large collection of food and clinical strains,
15. The identification of the role of internalin in targeting the placental barrier,
16. The identification of the first Rickettsia receptor and of its bacterial ligand.
Key papers have been cited in the paragraphs below.
1. The discovery and/or characterization of several virulence factors of L. monocytogenes,
2. The discovery of a new type of regulation mediated by an RNA thermosensor,
3. The determination of the complete genome sequences of L. monocytogenes and of L. innocua, a closely related non pathogenic species,
4. The discovery of the internalin receptor, E-cadherin,
5. The discovery of several key cellular components allowing the internalin-mediated entry,
6. The demonstration of the internalin/E-cadherin and InlB/Met species specificities,
7. The dissection of the complex signaling pathways triggered during the InlB-mediated entry, and the identification of two InlB receptors,
8. The elucidation of the role of rafts in the entry of Listeria,
9. The identification of the unexpected critical role of the endocytic machinery in bacterial entry,
10. The clarification of the mechanism used by Listeria to polymerize actin and move,
11. The discovery of the Vaccinia virus capacity to polymerize actin,
12. The identification of a novel actin nucleator produced by Rickettsia conorii,
13. The identification of the role of internalin in the crossing of the intestinal barrier, after generating the first transgenic model used to analyze a bacterial human disease,
14. The validation of the role of internalin in human listeriosis by an epidemiological survey of a large collection of food and clinical strains,
15. The identification of the role of internalin in targeting the placental barrier,
16. The identification of the first Rickettsia receptor and of its bacterial ligand.
Key papers have been cited in the paragraphs below.
The discovery and/or characterization of several virulence factors of <i>L. monocytogenes </i>
Our laboratory had identified the major virulence factors of L. monocytogenes : LLO which mediates the escape of the vacuole, ActA the protein that allows the intra- and inter-cellular movements, the two phosphoipases PlcA and PlcB, which are critical for the escape from the secondary vacuole and in some cases from the primary vacuole and the invasion protein internalin (also called InlA). We also had identifed PrfA as the major virulence activator protein (43, 112) .
Since 1994,
- By gene disruption, we discovered InlB, the second main invasion protein (8, 32, 38, 49).
- By using signature tagged mutagenesis, we discovered FbpA, a surface protein which binds fibronectin but also acts as a chaperon for LLO and InlB (110), the regulon VirR/VirS which regulates genes involved in the modification of membrane or cell wall components (124).
- By a classical genetic approach, we identified the autolysin Ami as an adhesin (71, 113).
- By post-genomic approaches, we identifed Bsh, a bile salt hydrolase that allows persistence in the intestine (87), Auto, an autolysin that is involved in entry (106). By mutating the sortase A, we highlighted that LPXTG proteins other than internalin should be important for virulence in oral listeriosis (83). We then identifed Vip, a protein involved in entry and survival in the host (123), and InlJ, a surface protein whose role in virulence is still unclear (128). We identified Stp, a serine/ threonine phosphatase involved in the stress response, which phosphorylates EF-Tu (120).
The discovery of a new type of regulation mediated by an RNA thermosensor
The key virulence genes are under the regulation of the pleiotropic activator protein PrfA, a protein similar to the cyclic AMP receptor protein, CAP in E. coli (17, 21, 28, 95).
We have shown that expression of this protein is increased upon cell contact or in the presence of cell extracts (57). However, the mechanism underlying this activation is unknown.
By analyzing why virulence genes are expressed at 37°C and not at 30°C, we discovered that the untranslated region of the mRNA encoding PrfA can adopt at low temperatures a secondary structure that hides the ribosome binding site and prevents translation (89). This structure melts at high temperatures, allowing PrfA expression and consequently virulence gene expression. This study represented the first example of a regulation of virulence genes by an RNA thermosensor (100).
The determination of the complete genome sequences of <i>L. monocytogenes</i> and of <i>L. innocua</i>, a closely related non pathogenic species
I have coordinated - together with P. Glaser, in the frame work of a European consortium - the sequencing of the genomes of L. monocytogenes and L. innocua with the aim of identifying new virulence factors (80, 85, 102). Our efforts have been particularly well supported by the Pasteur Institute and collaborative studies with the Centre de Reference have followed which have led to the identification of proteins absent from L. innocua and present in all L. monocytogenes strains, and thus putative candidate as virulence factors that are now under study.
The discovery of the internalin receptor, E-cadherin
An affinity chromatography approach has led to the identification of E-cadherin as the receptor for internalin (19). Listeria is so far the only bacterium using E-cadherin as a portal of entry. E-cadherin is a transmembrane protein particularly well suited to act as a receptor (66). The distribution of E-cadherin in infected hosts appears critical for tissue tropism during disease (55, 78, 104). Listeria appears as a very instrumental tool to addres the cell biology underlying E-cadherin function.
The discovery of several key cellular components allowing the internalin-mediated way of entry
We first took a candidate based approach to investigate if the intracytoplasmic domain of E-cadherin and the catenins that bind to it are required for entry (66). We then analyzed if an unconventional myosinVII, that we had contributed to identify at the adherens junctions (67), was also used by Listeria (108). Finally, we recently took a two hybrid screen approach to identify new molecules involved in entry and identified ARHGAP10, a new ligand of a-catenin and a protein required for a-catenin recruitment at the junctions (130).
The demonstration of the internalin/E-cadherin and InlB/Met species specificity
Unexpected observations and a series of mutagenesis studies converged to demonstrate that L. monocytogenes internalin interacts with human E-cadherin and not with mouse E-cadherin, that this specificty is due to a single amino-acid at position 16 of E-cadherin, and that this specificity prevents the use of mice to analyze the role of internalin in vivo (55). Interestingly, guinea pigs are permissive to oral listeriosis and have a proline at position 16 of their E-cadherin just as humans. These observations led to the generation of transgenic mice expressing human E-cadherin as a new model for listeriosis (78) and were confirmed by the co-crystallisation studies performed by the group of D. Heinz (Schubert et al., Cell, 2002, 111:825-36, see below).
The dissection of the complex signaling pathways triggered during the InlB-mediated entryand the identification of two InlB receptors
InlB is a potent signaling molecule that triggers entry into a variety of cell types (37, 39, 99, 107). Its three dimensional structure was determined in collaboration with P. Ghosh (59, 68, 90). We identified, following pharmacological inhibition experiments, the PI3 kinase pathway as a key signaling cascade required for entry (25, 54). This led to the identification - by my ex post doc K. Ireton when he was back in Canada - of Met, the hepatocyte growth factor receptor as one of the three receptors for InlB. We identified the two other InlB ligands, gC1qR (61) and glycosaminoglycans (or GAGs) (76), and a series of key cytoskeleton molecules critical for entry (e.g. the small GTPases Rac and Cdc42, Arp2/3, Wave and N-WASP), and demonstrated the key role of cofilin as a regulator of entry (46, 75, 88, 121).
The elucidation of the role of rafts in the entry of <i>Listeria</i>
By using classical techniques to investigate if the presence of rafts in membranes affects Listeria entry, we could show that entry via the InlA pathway is affected at the step of adhesion and that the InlB mediated way of entry is affected not at the stage of adhesion but later in the process, at the level of Rac activation (114, 137).
Identification of the unexpected critical role of the endocytic machinery in bacterial entry
Guided by the fact that InlB interacts with a growth factor receptor (i.e. Met) which is known to be monoubiquitinated and degraded in lysosomes, we were able to demonstrate that inlB can induce the monoubiquitination of Met and that this event triggers its endocytosis (117, 127). We could then show that many 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.
The clarification of the mechanism used by <i>Listeria</i> to polymerize actin and move
Our discovery of the actA gene and of the ActA protein has been instrumental for the basic understanding of actin-based motility and contributed to the elucidation of the role of the Arp2/3 complex in this process (1, 5, 7, 10, 11, 13, 14, 20, 30, 33, 37, 40, 42, 43, 46, 51, 64, 119). Through a genetic study, we identified in ActA, the regions critical for movement and as also shown by other, demonstrated that ActA mimics cellular proteins of the WASp family and activates Arp2/3 (15, 27). We have also shown that ActA is able to bind PIP2, although the role of this phosphoinositide in the actin based motility of Listeria is still elusive (60). ActA-mediated motility is now cited as the best example of a strategy used by a pathogen to exploit mammalian cell functions during infection. It is also cited as a good example of a tool provided by a bacterium to unravel previously unknown cellular functions.
The discovery of the Vaccinia virus capacity to polymerize actin
Intrigued by an old study and amazing pictures, we investigated vaccinia virus intracellular behaviour and discovered that not only bacteria but also a virus could move by using actin-based motility. However, given the complexity of the vaccinia life cycle, we collaborated on this issue with M. Way (18). Vaccinia viruses are in fact not moving intracellularly by an actin-based mechanism but instead move on microtubules and it is only when they are present outside and on the plasma membrane, that they can induce protrusions that emerge through actin polymerisation that trigger viral dissemination.
The identification of a novel actin nucleator produced by <i>Rickettsia conorii</i>
By comparing Listeria, Shigella, and Rickettsia actin-based motilities, we have highlighted a novel type of actin-based movement. The actin tails of Rickettsia are made of long filaments and are thus 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.
Identification of the role of internalin in the crossing of the intestinal barrier : generation of a transgenic model for orally acquired listeriosis
By generating transgenic mice expressing human E-cadherin at the intestinal barrier level, in enterocytes (iFABP-hEcad transgenic mice) we could show that orally acquired listeriosis can be lethal and that internalin is a key factor in this process by mediating entry in enterocytes and translocation across the intestinal barrier (78). This model was the first transgenic model generated to overcome the species specificity of a bacterial virulence factor and to allow the demonstration of its key role in the infectious process (91).
The validation of the role of internalin in human listeriosis by an epidemiological survey of a large collection of food and clinical strains
We had noticed that one of the two strains that we had used for many years for our genetic studies, strain LO28, harbored a mutation in the inlA gene resulting in a truncated secreted internalin unable to promote entry into cells expressing E-cadherin (41). We have analyzed a large panel of strains (450 strains) of food origin or of clinical origin and have shown that most clinical strains (98%) express a full length internalin in contrast to food strains which contain a much higher proportion of truncated internalin (65% of full length internalin) (109). In addition, in serovar 4b strains, the most common serovar among epidemic strains, internalin has always its full length. This epidemiological survey thus establishes 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 or in the feces of pregnant women as a marker for potentially more virulent strains.
The identification of the role of internalin in targeting the placental barrier
While only 65% of food strains express a full length functional internalin, absolutely all strains associated with fetoplacental listeriosis listeriosis express a full length internalin, suggesting a role for internalin in the Listeria tropism for the materno-fetal barrier (109). By a combination of in vivo observations, in vitro infections of cell lines and ex vivo infections of healthy 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 (104). Such an interaction between a pathogen and its cellular ligand that mediates targeting and crossing of the placental barrier has never been observed.
The identification of the first <i>Rickettsia</i> receptor and its bacterial ligand
Rickettsia conorii, highjacks host cell signal transduction pathways to induce its entry into normally non-phagocytic target cells (115). Through various techniques, we have isolated and identified the first host cell receptor, Ku70, involved in the induced entry of a rickettsial species (131). 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. C. Kocks and P. Cossart (1994). Directional actin assembly by Listeria monocytogenes at the site of polar surface expression of the actA gene product involving the actin-bundling protein plastin (fimbrin). Infect. Agents Dis., 2 : 207-209.
2. M. Lebrun, A. Audurier and P. Cossart (1994). Plasmid-borne cadmium resistance genes in Listeria monocytogenes are similar to cadA and cadC genes of Staphylococcus. aureus and are induced by cadmium. J. Bacteriol., 176 : 3040-3048.
3. M. Lebrun, A. Audurier and P. Cossart (1994). Plasmid-borne cadmium resistance genes in Listeria monocytogenes are present on Tn5422, a transposon closely related to Tn917. J. Bacteriol., 176 : 3049-3061.
4. E. Gouin, J. Mengaud and P. Cossart (1994). The virulence gene cluster of Listeria monocytogenes is also present in Listeria ivanovii, an animal pathogen and Listeria seeligeri, a non pathogenic species. Infect. Immun., 62 : 3550-3553.
5. P. Cossart and C. Kocks (1994). The actin-based motility of the facultative intracellular pathogen Listeria monocytogenes. Mol. Microbiol., 13 : 395-403.
6. A. D. Klarsfeld, P.-L. Goossens and P. Cossart (1994). Five Listeria monocytogenes genes preferentially expressed in infected mammalian cells : plcA, purD, pyrE and an arginine ABC transporter gene, arpJ. Mol. Microbiol., 13 : 585-597.
7. P. Cossart (1995). Actin-based bacterial motility. Cur. Opin. Cell Biol., 7 : 4-101.
8. S. Dramsi, I. Biswas, E. Maguin, L. Braun, P. Mastroeni and P. Cossart (1995). Entry of Listeria monocytogenes into hepatocytes requires expression of InlB, a surface protein of the internalin multigene family. Mol. Microbiol., 16 : 251-261.
9. P. Dehoux and P. Cossart (1995). Homologies between salmolysin and some bacterial regulatory proteins. Mol. Microbiol., 15 : 591-591.
10. E. Gouin, P. Dehoux, J. Mengaud, C. Kocks and P. Cossart (1995). iactA of Listeria ivanovii although distantly related to Listeria monocytogenes actA restores actin tail formation in a Listeria monocytogenes actA mutant. Infect. Immun., 63 : 2729-2737.
11. E. Friedrich, E. Gouin, R. Hellio, C. Kocks, P. Cossart and D. Louvard (1995). Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function. Embo J., 14 : 2731-2744.
12. P.-L. Goossens, G. Milon, P. Cossart and M.-F. Saron (1995). Attenuated Listeria monocytogenes as a live vector for induction of CD8+T cells in vivo : a study with the nucleoprotein of the lymphocytic choriomeningitis virus. Int. Immunol., 7 : 797-805 .
13. J.-B. Marchand, P. Moreau, A. Paoletti, P. Cossart, M.-F. Carlier and D. Pantaloni (1995). Actin-based movement of Listeria monocytogenes : actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface. J. Cell Biol., 130 : 331-343.
14. C. Kocks, J.-B. Marchand, E. Gouin, H. d’Hauteville, P.-J. Sansonetti, M.-F. Carlier and P. Cossart (1995). The non-related surface proteins ActA of Listeria monocytogenes and IcsA of Shigella flexneri are sufficient to confer actin-based motility to Listeria innocua and Escherichia coli respectively. Mol. Microbiol., 18 : 413-423.
15. I. Lasa, V. David, E. Gouin, J.-B. Marchand and P. Cossart (1995). The amino-terminal part of ActA is critical for the actin-based motility of Listeria monocytogenes. Mol. Microbiol., 18 : 425-436.
16. M. Sanchez-Campillo, S. Dramsi, E. Michel, P. Dehoux, J.-M. Gomez-Gomez, P. Cossart, F. Baquero and J.-C. Perez-Diaz (1995). Modulation of DNA topology by flaR, a new gene from Listeria monocytogenes. Mol. Microbiol., 18 : 801-812.
17. B. Sheehan, A. Klarsfeld, T. Msadek and P. Cossart (1995). The differencial activation of virulence gene expression by PrfA, the Listeria monocytogenes virulence regulator. J. Bacteriol., 177 : 6469-6476.
18. S. Cudmore, P. Cossart, G. Griffiths and M. Way (1995). Actin-based motility of vaccinia virus. Nature, 378 : 636-638.
19. J. Mengaud, H. Ohayon, P. Gounon, R.-M. Mege and P. Cossart (1996). E-cadherin is the receptor for internalin, a surface protein required for entry of Listeria monocytogenes into epithelial cells. Cell, 84 : 923-932.
20. I. Lasa and P. Cossart (1996). Actin-based bacterial motility : towards a definition of the minimal requirements. Trends Cell Biol., 6 : 109-114.
21. B. Sheehan, A. Klarsfeld, R. Ebright and P. Cossart (1996). A single substitution in the putative helix-turn-helix motif of the pleiotropic activator prfA attenuates Listeria monocytogenes virulence. Mol. Microbiol.,20 : 785-797.
22. P. Cossart, P. Boquet, S. Normark and R. Rappuoli (1996). Cellular microbiology emerging. Science, 271 : 315-316.
23. M. Lebrun, J. Mengaud, H. Ohayon, F. Nato and P. Cossart (1996). Internalin must be on the bacterial surface to mediate entry of Listeria. monocytogenes into epithelial cells. Mol. Microbiol., 21 : 579-592.
24. P. Tang, I. Rosenshine, P. Cossart and B.-B. Finlay (1996). Listeriolysin O activates mitogen-activated protein kinase in eucaryotic cells. Infect. Immun., 64 : 2359-2361.
25. K. Ireton, B. Payrastre, H. Chap, W. Ogawa, H. Sakaue, M. Kasuga and P. Cossart (1996). A role for phosphoinositide 3-kinase in bacterial invasion. Science, 274 : 780-782.
26. J. Mengaud, M. Lecuit, M. Lebrun, F. Nato, J.-C. Mazie and P. Cossart (1996). Antibodies against the leucine-rich repeats region of internalin block entry of Listeria monocytogenes into cells expressing E-cadherin. Infect. Immun., 64 : 5430-5433.
27. I. Lasa, E. Gouin, M. Goethals, K. Vancompernolle, V. David, J. Vandekerckhove and P. Cossart (1997). Identification of two regions in the amino-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes. EMBO J., 16 : 1531-1540.
28. A. Renzoni, A. Klarsfeld, S. Dramsi and P. Cossart (1997). Evidence that PrfA, the pleiotropic activator of virulence genes in Listeria monocytogenes can be present but inactive. Infect. Immun., 65 : 1515-1518.
29. B.-B. Finlay, and P. Cossart (1997). Exploitation of mammalian host cell functions by bacterial pathogens. Science, 276 : 718-725.
30. P. Cossart (1997). Subversion of the mammalian cytoskeleton by invasive bacterial pathogens. J. Clin. Invest., 99 : 2307-2311.
31. S. Dramsi, P. Dehoux, M. Lebrun, P.-L. Goossens and P. Cossart (1997). Identification of four members of the internalin multigene family in Listeria monocytogenes strain EGD. Infect. Immun., 65 : 1615-1625.
32. L. Braun, S. Dramsi, P. Dehoux, H. Bierne, G. Lindahl and P. Cossart (1997). InlB: an invasion protein of Listeria monocytogenes with a novel type of surface association. Mol. Microbiol., 25 : 285-294.
33. P. Mourrain, I. Lasa, A. Gautreau, A. Pugsley and P. Cossart (1997). ActA is a dimer. Proc. Natl. Acad. Sci. USA, 94 : 10034-10039.
34. M. Lecuit, H. Ohayon, L. Braun, J. Mengaud and P. Cossart (1997). Internalin of Listeria monocytogenes with an intact leucine-rich repeat region is sufficient to promote internalization. Infect. Immun., 65 : 5309-5319.
35. D. Robichon, E. Gouin, M. Débarbouillé, P. Cossart, Y. Cenatiempo and Y. Hechard (1997). The rpoN (sigma 54) gene from Listeria monocytogenes is involved in resistance to mesentericin Y105, an antibacterial peptide from Leuconostoc mesenteroides. J. Bacteriol., 179 : 7591-7594.
36. P. Cossart (1997). Subversion of the mammalian cell cytoskeleton by invasive bacterial. J. Clin. Invest., 99 : 2307-2311.
37. K. Ireton and P. Cossart (1997). Host-pathogen interactions during entry and actin-based movement of Listeria monocytogenes. Annu. Rev. Genet., 31 : 113-138.
38. L. Braun, H. Ohayon and P. Cossart (1998). The InlB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells. Mol. Microbiol., 27 : 1077-1088.
39. K. Ireton and P. Cossart (1998). Interactions of invasive bacteria with host signaling pathways. Curr. Opin. Cell Biol., 10 : 276-283.
40. I. Lasa, P. Dehoux and P. Cossart (1998). Actin polymerization and bacterial movement. Biochim. Biophys. Acta., 1402 : 217-228.
41. R. Jonquieres, H. Bierne, J. Mengaud and P. Cossart (1998). The inlA gene of Listeria monocytogenes strain LO28 harbors a non-sense mutation resulting in release of internalin. Infect. Immun., 66 : 3420-3422.
42. S. Dramsi and P. Cossart (1998). Intracellular pathogens and the actin cytoskeleton. Annu. Rev. Cell Dev. Biol., 14 : 137-166.
43. P. Cossart and M. Lecuit (1998). Interactions of Listeria monocytogenes with mammalian cells during entry and actin-based movement : bacterial factors, cellular ligands and signaling. EMBO J., 17 : 3797-3806.
44. S. Dramsi, S. Levi, A. Triller and P. Cossart (1998). Entry of Listeria monocytogenes into neurons occurs by cell to cell spread : an in vitro study. Infect. Immun., 66 : 4461-4468.
45. S. Heffron, G. Moe, V. Sieber, J. Mengaud, P. Cossart, J. Vitali and F. Jurnak (1998). Sequence profile of the parallel b helix in the pectate lyase superfamily. J. Struct. Biol., 122 : 223-235.
46. V. David, E. Gouin, M. Van Troys, A. Grogan, A. Segal, C. Ampes and P. Cossart (1998). Identification of cofilin, coronin, Rac and capZ in actin tails using a Listeria affinity approach. J. Cell Sci., 111 : 2877-2884.
47. E. Michel, J. Mengaud, S. Galsworthy and P. Cossart (1998). Characterization of a large motility gene cluster containing the cheR, motAB genes of Listeria monocytogenes and evidence that PrfA downregulates motility genes. FEMS Microbiol. Lett., 169 : 341-347.
48. I. Callebaut, P. Cossart and P. Dehoux (1998). EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran binding domains of the Ran BP1 family. FEBS Lett., 441 : 181-185.
49. R. Jonquières, H. Bierne, F. Fiedler, P. Gopunon and P. Cossart (1999). Interactions between the protein InlB of Listeria monocytogenes and lipotechoic acid: a novel mechanism of association at the surface of gram positive bacteria. Mol. Microbiol., 34 : 902-914.
50. N. Promadej, F. Fiedler, P. Cossart, S. Dramsi and S. Kathariou (1999). Wall teichoic acid glycosylation in serotype 4b Listeria monocytogenes requires gtcA, a novel, serogroup-specific gene. J. Bacteriol., 181 : 418-425.
51. E. Gouin, H. Gantelet, C. Egile, I. Lasa, H. Ohayon, V. Villiers, P. Gounon, P.-J. Sansonetti andP. Cossart (1999). A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii. J. Cell Sci., 112 : 1697-1708
52. K. Dalet, E. Gouin, Y. Cenatiempo, P. Cossart and Y. Hechard (1999). Characterisation of a new operon encoding a Zur-kike protein and an associated ABC zinc permease in Listeria monocytogenes. FEMS Microbiol. Lett., 174 : 11-116.
53. F. Castellano, P. Montcourrier, J.-C. Guillemot, E. Gouin, L. Machesky, P. Cossart and P. Chavrier (1999). Inducible recruitment of Cdc42 or WASP to a cell-surface receptor triggers actin polymerization and filopodium formation. Curr. Biol., 9 : 351-360.
54. K. Ireton, B. Payrastre and P. Cossart (1999). The Listeria monocytogenes protein InlB is an agonist of mammalian PI 3-kinase. J. Biol. Chem., 274 : 17025-17032.
55. M. Lecuit, S. Dramsi, C. Gottardi, M. Fedor-Chaiken, B. Gumbiner and P. Cossart (1999). A single amino-acid in E-cadherin responsible for host-specificity towards the human pathogen Listeria monocytogenes. EMBO J., 18 : 3956-3963.
56. L. Braun, F. Nato, B. Payrastre, J.-C. Mazie and P. Cossart (1999). The 213-amino acid LRR region of the Listeria monocytogenes InlB protein is sufficient for entry into mammalian cells and stimulation of PI3-kinase. Mol. Microbiol., 34 : 10-23.
57. A. Renzoni, P. Cossart and S. Dramsi (1999). PrfA, the transcriptional activator of virulence genes in Listeria monocytogenes, is upregulated upon cell-contact and in cell extracts. Mol. Microbiol., 34 : 522-561.
58. B.-T. Edelson, P. Cossart and E. Unanue (1999). Paradigm revisited: antibody provides resistance to Listeria infection. J. Immunol., 163 : 4087-4090.
59. M. Marino, L. Braun, P. Cossart and P. Ghosh (1999). Structure of the InlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen. Mol. Cell., 4 : 1063-1072.
60. P. Steffen, D. A. Schafer, V. David, E. Gouin, J.-A. Cooper and P. Cossart (2000).The Listeria monocytogenes ActA protein interacts with phosphatidyl-inositol 4,5 biphosphate in vitro. Cell Motil. Cytoskeleton, 45 : 58-66.
61. L. Braun, B. Gebrehiwet and P. Cossart (2000). gC1q-R/p32, a C1q-binding protein, is a receptor for the InIB invasion protein of Listeria monocytogenes. EMBO J., 19 : 1458-1466.
62. A. Mansell, L. Braun, P. Cossart and L. O’Neill (2000). A novel function of InlB from Listeria monocytogenes : activation of NF-kB in J774 macrophages. Cell. Microbiol., 2 : 127-136.
63. P. Cossart and R. Jonquieres (2000). Sortase, a universal target for therapeutic agents against Gram-positive bacteria ? Proc. Natl. Acad. Sci. USA, 97 : 5013-5015.
64. P. Cossart (2000). Actin-based motility of pathogens : the Arp 2/3 complex is a central player. Cell. Microbiol., 2 : 195-205.
65. H. Bierne, S. Dramsi, M.-P. Gratacap, C. Randraimampita, G. Carpenter, B. Payrastre and P. Cossart (2000). The invasion protein InlB from Listeria monocytogenes activates PLC-gl downstream from PI 3-kinase. Cell. Microbiol., 20 : 1-13.
66. M. Lecuit, R. Hurme, J. Pizarro-Cerda, H. Ohayon, B. Geiger and P. Cossart (2000). A role for alpha and beta catenins in bacterial uptake. Proc. Natl. Acad. Sci. USA, 97 : 10008-10013.
67. P. Küssel-Andermann, A. El-Amraoui, S. Safieddine, S. Nouaille, I. Perfettini, M. Lecuit, P. Cossart, U. Wolfrum and C. Petit (2000). Vezatin, a novel transmembrane protein, bridges myosin VIIA to the cadherin-catenins complex. EMBO J., 19 : 6020-6029.
68. M. Marino, L. Braun, P. Cossart and P. Ghosh (2000). A framework for interpreting the leucine-rich repeats of Listeria internalins. Proc. Natl. Acad. Sci. USA, 97 : 8784-8788.
69. E. Milohanic, B. Pron, P. Berche, J.L. Gaillard and The European Listeria Genome Consortium (2000). Identification of new loci involved in adhesion of Listeria monocytogenes to eukaryotic cells. Microbiology, 46 : 731-9.
70. I. Dubail, P. Berche, A. Charbit and The European Listeria Genome Consortium (2000). Listeriolysin O as a reporter to identify constitutive and in vivo-inducible promoters in the pathogen Listeria monocytogenes. Infect. Immun., 68 : 3242-50.
71. E. Milohanic, R. Jonquieres, P. Cossart, P. Berche and J.-L. Gaillard (2001). The autolysin Ami mediates the adhesion of Listeria monocytogenes to eucaryotic cells via its cellwall anchor. Mol. Microbiol., 39 : 1212-1224.
72. P. Cossart and H. Bierne (2001). The use of host cell machinery in the pathogenesis of Listeria monocytogenes. Curr. Opin. Immunol., 13 : 96-103.
73. P. Cossart (2001). Met, the HGF-SF receptor : another receptor for Listeria monocytogenes.Trends Microbiol., 9 : 105-107.
74. R. Boujemaa-Paterski, E. Gouin, G. Hansen, S. Samarin, C. Le Clainche, D. Didry, P. Dehoux, P. Cossart, C. Kocks, M.-F. Carlier and D. Pantaloni (2001). The Listeria protein ActA mimics WASP family proteins : it activates filament branching by ARP 2/3 complex. Biochemistry, 40 : 11390-11404.
75. H. Bierne, E. Gouin, P. Roux, P. Caroni, H. Yin and P. Cossart (2001). A role for cofilin and LIM-kinase in bacterial induced phagocytosis. J. Cell Biol., 155 : 101-112.
76. R. Jonquières, J. Pizarro-Cerda and P. Cossart (2001). Synergy between the N and C-terminal domains of InlB for efficient invasion of non-phagocytic cells by Listeria monocytogenes. Mol. Microbiol., 42 : 955-965.
77. K. Dalet, Y. Cenatiempo, P. Cossart and The European Listeria Genome Consortium and Y. Héchard (2001). A s54-depedent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to the bacteriocin, mesentericin Y105. Microbiology, 147 : 3263-3269.
78. M. Lecuit, S. Vandormael-Pournin, J. Lefort, M. Huerre, P. Gounon, C. Dupuy, C. Babinet and P. Cossart (2001). A transgenic model for listeriosis : role of internalin in crossing the intestinal barrier. Science, 292 : 1722-1725.
79. H. Ogata, S. Audic, P. Renesto-Audiffren, P.-E. Fournier, V. Barbe, D. Samson, V. Roux, P. Cossart, J. Weissenbach, J.-M. Claverie and D. Raoult (2001). Mechanisms of evolution in Rickettsia conorii and Rickettsia prowaekii. Science, 293 : 2093-2098.
80. P. Glaser, L. Frangeul, C. Buchrieser, C. Rusniok, A. Amend, F. Baquero, P. Berche, H. Bloecker, P. Brandt, T. Chakraborty, A. Charbit, F. Chetouani, E. Couvé, A. de Daruvar, P. Dehoux, E. Domann, G. Dominguez-Bernal, E. Duchaud, L. Durant, O. Dussurget, K.-D. Entian, H. Fsihi, F. Garcia-Del Portillo, P. Garrido, L. Gautier, W. Goebel, N. Gomez-Lopez, T. Hain, J. Hauf, D. Jackson, L.-M. Jones, U. Kaerst, J. Kreft, M. Kuh,, F. Kunst, G. Kurapkat, E. Madueno, A. Maitournam, J.-M. Vicente, E. Ng, H. Nedjari, G. Nordsiek, S. Novella, B. de Pabols, J.-C. Perez-Diaz, R. Purcell, B. Remmel, M. Rose, T. Schlueter, N. Simoes, A. Tierrez, J.-A. Vasquez-Boland, H. Voss, J. Wehland and P. Cossart (2001). Comparative genomics of Listeria species. Science, 294 : 849-853.
81. A. Mansell, N. Khelef, P. Cossart and L. A.-J. O’Neill (2001). Internalin B activates NF-kB via Ras, PI-3 kinase and Akt. J. Biol. Chem., 276 : 43597-43603.
82. C. Jacquet, E. Gouin, D. Jeannel, P. Cossart and J. Rocourt (2002). Expression of ActA, Ami, InlB and LLO in Listeria monocytogenes of human and food origins. Appl. Environ. Microbiol., 68 : 616-622.
83. H. Bierne, S. Mazmanian, M. Trost, G. Pucciarelli, G. Liu, P. Dehoux, The European Listeria Genome consortium, L. Jânsch, F. Garcia del Portillo, O. Schneewind and P. Cossart (2002). Inactivation of the sortase srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affect virulence. Mol. Microbiol., 43 : 869-881.
84. J. Pizarro-Cerda, R. Jonquières, E. Gouin, J. Van de Kerkhove, J. Garin and P. Cossart (2002). Distinct protein patterns associated with Listeria monocytogenes InlA-and InlB-phagosomes. Cell. Microbiol., 4 : 101-115.
85. D. Cabanes, P. Dehoux, O. Dussurget, L. Frangeul and P. Cossart (2002). Surface proteins and pathogenic potential of Listeria monocytogenes. Trends Microbiol., 10 : 238-245.
86. S. Dramsi and P. Cossart (2002). Listeriolysin O : a genuine cytolysin optimized for an intracellular parasite. J. Cell Biol., 156 : 943-946.
87. O. Dussurget, D. Cabanes, P. Dehoux, M. Lecuit, The European Listeria Genome Consortium,C. Buchrieser, P. Glaser and P. Cossart (2002). Listeria monocytogenes bile salt hydrolase is a virulence factor involved in the intestinal and hepatic phases of listeriosis. Mol. Microbiol., 45 : 1095-1106.
88. H. Bierne and P. Cossart (2002). InlB, a surface protein of Listeria monocytogenes that behaves as an invasin and a growth factor. J. Cell Sci., 115 : 3357-3367.
89. J. Johansson, P. Mandin, A. Renzoni, C. Chiaruttini, M. Springer and P. Cossart (2002). An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes. Cell, 110 : 551-561.
90. M. Marino, M. Banerjee, T. Chapman, R. Jonquières, P. Cossart and P. Ghosh (2002). Structural mimics of SH3 domains in the Listeria monocytogenes invasion protein InlB mediate binding to host ligands. EMBO J., 21 : 5623-5634.
91. M. Lecuit and P. Cossart (2002). Genetically modified animal models for human infections : the Listeria paradigm. Trends Mol. Med., 8 : 537-542.
92. D. Merino, H. Reglier-Poupet, P. Berche, A. Charbit and The European Listeria Genome Consortium (2002). A hypermutator phenotype attenuates the virulence of Listeria monocytogenes in a mouse model. Mol. Microbiol., 44 : 877-87.
93. F. Tremoulet, O Duche, A. Namane, B. Martinie, J. Labadie , P. Cossart and The European Listeria Genome Consortium (2002). Comparison of protein patterns of Listeria monocytogenes grown in biofilm or in planktonic mode by proteomic analysis. FEMS Microbiol. Lett., 210 : 25-31.
94. O. Duche, F. Tremoulet, A. Namane, J. Labadie , P. Cossart and The European Listeria Genome Consortium (2002). A proteomic analysis of the salt stress response of Listeria monocytogenes. FEMS Microbiol. Lett., 215 : 183-8.
95. E. Milohanic, P. Glaser, J.-Y. Coppée, L. Frangeul, Y. Vega, J.-A. Vasquez-Boland, F. Kunst, P. Cossart and C. Buchrieser (2003). Transcriptome analysis of Listeria monocytogenes identifies three groups of genes differently regulated by PrfA. Mol. Microbiol., 47 : 1613-1625.
96. S. Dramsi and P. Cossart (2003). Listeriolysin O-mediated calcium influx potentiates entry of Listeria monocytogenes into the human Hep-2 epithelial cell line. Infect. Immun., 71 : 3614-3618.
97. R. Gardan, P. Cossart, J. Labadie and The European Listeria Genome Consortium (2003). Identification of Listeria monocytogenes genes involved in salt and alkaline-pH tolerance. Appl. Environ. Microbiol., 69 : 3137-3143.
98. P. Renesto, P. Dehoux, E. Gouin, L. Touqui, P. Cossart and D. Raoult (2003). Identification and characterization of a PLD-superfamily gene in Rickettsiae. J. Inf. Dis., 188 : 1276-83.
99. P. Cossart, J. Pizarro-Cerda and M. Lecuit (2003). Invasion of mammalian cells by Listeria monocytogenes : functional mimicry to subvert cellular functions. Trends Cell Biol., 13 : 23-31.
100. J. Johansson and P. Cossart (2003). RNA-mediated control of virulence gene expression in bacterial pathogens. Trends Microbiol., 11 : 280-285.
101. E. Gouin, 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 : 457-461.
102. M. Doumith, 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. Infect. Immun., 72 : 1072-1083.
103. P. Cossart (2004) Bacterial invasion : a new strategy to dominate cytoskeleton plasticity. Dev. Cell, 6 : 314-315.
104. M. Lecuit, 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 : 6152-6157.
105. H. Bierne, C. Garandeau, M.-G. Pucciarelli, C. Sabet, S. Newton, F. Garcia-del-Portillo, P. Cossart and A. Charbit. (2004). Sortase B, a new class of sortase in Listeria monocytogenes. J. Bacteriol., 186 :1972-1982.
106. D. Cabanes, 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 : 1601-1614.
107. P. Cossart and P.-J. Sansonetti. (2004). Bacterial invasion : the paradigms of enteroinvasive pathogens. Science., 304 : 242-248.
108. S. Sousa, D. Cabanes, A. El Amraoui, C. Petit, M. Lecuit and P. Cossart. (2004). Unconventional myosin VIIa and vezatin, two proteins critical in Listeria entry into epithelial cells. J. Cell Sci., 117 : 2121-2130.
109. C. Jacquet, M. Doumith, J.I. Gordon, P. Martin, P. Cossart and M. Lecuit. (2004). A molecular marker for evaluating the pathogenic potential of foodborne Listeria monocytogenes. J. Infect. Dis., 189 : 2094-2100.
110. S. Dramsi, F. Bourdichon, D. Cabanes, M. Lecuit, H. Fshihi and P. Cossart (2004). FbpA, a novel multifunctional Listeria monocytogenes virulence factor. Mol. Microbiol., 53 : 639-649.
111. M. Marino, 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 : 379-386.
112. O. Dussurget, J. Pizarro-Cerda and P. Cossart (2004). Molecular determinants of Listeria monocytogenes virulence. Ann. Rev. Microbiol., 58 : 587-610.
113. E. Milohanic, R. Jonquière, 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 : 4401-4409.
114. S. Seveau, S. Giroux, H. Bierne, M.-C. Prévost 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., 116 : 743-753.
115. J. Martinez and P. Cossart (2004). Early signaling events involved in the entry of Rickettsia conorii into mammalian cells. J. Cell Sci., 177 : 5097-5106.
116. J. Pizarro-Cerda and P. Cossart (2004). Subversion of phosphoinositide metabolism by intracellular bacterial pathogens. Nat. Cell Biol., 6 : 1026-1033.
117. E. Veiga and P. Cossart (2005). Ubiquitination of intracellular bacteria : a new bacteria-sensing system ? Trends Cell Biol., 15 : 2-5.
118. E. Calvo, 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 nano-liquid chromatography coupled to mass spectrometry. Proteomics, 5 :433-443.
119. E. Gouin, M.-D. Welch and P. Cossart.(2005) Actin-based motility of intracellular pathogens. Curr. Opin. Microbiol., 8 :35-45.
120. C. Archambaud, 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 :383-396.
121. H. Bierne, H. Miki, M.I nnocenti, G. Scita, F.-B. Gertler, T. Takenawa and P. Cossart. (2005) WAVE2, Abi1 and Ena/VASP proteins are involved in Met-induced cytoskeleton rearrangements induced by the Listeria invasion protein InlB. J. Cell Sci., 118 : 1537-1547.
122. V. Dellaretti Guimaraes, J. Eyre Gabriel, F. Lefebvre, D. Cabanes, A. Gruss, P. Cossart, V. Azevedo and P. Langella. (2005) Internalin expressing Lactococcus lactis are able to invade small intestine of guinea pigs and deliver DNA into mammalian cells. Microbes Infect., 7 : 836-844.
123. D. Cabanes, 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 : 2827-2838.
124. P. Mandin, 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 : 1367-1380.
125. O. Dussurget, E. Dumas, C. Archambaud, I. Chafsey, C. Chambon, M. Hébraud and P. Cossart. (2005) Listeria monocytogenes ferritin protects against multiple stresses and is required for virulence. FEMS Microbiol. Lett., 250 : 253-261.
126. S. Sousa, M. Lecuit and P. Cossart.(2005) Microbial strategies to target, cross or disrupt epithelia. Curr. Opin. Cell. Biol., 17 :1-10.
127. E.Veiga and P. Cossart. (2005) Listeria hijacks the clathrin-dependent endocytic machinery to invade mammalian cells. Nat. Cell. Biol., 7 : 894-900.
128. C. Sabet, 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 : 9312-6922.
129. S.-M. Roche, P. Gracieux, E. Milohanic, I. Albert, I. Virlogeux-Payant, S. Témoin, O. Grépinet, A. Kerouaton, C. Jacquet, P. Cossart and P. Velge. (2005) Investigation of specific substitutions in virulence genes characterizing phenotypical groups of low-virulence field strains of Listeria monocytogenes. Appl. Environ. Microbiol., 71 : 6039-48.
130. S. Sousa, D. Cabanes, F. Colland, M. Lecuit, P. Legrain and P. Cossart. (2005) ARHGAP10 is necessary for µ-catenin recruitment at adherens junctions and for Listeria invasion. Nat. Cell Biol., 7 : 954-960.
131. J.-J. Martinez, S. Seveau, E. Veiga-Chacon, S. Matsuyama and P. Cossart. (2005) Ku70, a component of DNA-dependent protein kinase, is a receptor involved in Rickettsia conorii invasion of mammalian cells. Cell, 123 : 1013-1023.
132. M.-G. Pucciarelli, 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 : 4808-4817.
133. N. Khelef, M. Lecuit, H. Bierne and P. Cossart. (2005) Species-specificity of the interaction between Listeria monocytogenes InlB and its receptor Met : Implications for the role of InlB in virulence. Cell. Microbiol. (on-line).
134. R. Herro, 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. (in press)
135. J. Pizarro-Cerda, Y.-J. Wang, B. Payrastre, H.-L. Yin and P. Cossart. Type II phosphatidylinositol 4-kinases a and b promote bacterial invasion. Nat. Cell Biol. (under revision)
136. S. Boisson-Dupuis, J. Pizarro-Cerda, C. Schmitt, M.-C. Prévost and P. Cossart. Septins control vacuolar escape of intracytosolic bacteria. Nat. Cell. Biol. (under revision)
137. S. Seveau, T.-N. Tam, B. Payrastre, A.-D. Hoppe, J.-A. Swanson and P. Cossart. Spatial distribution of PI(3,4)P2 and PI(3,4,5)P3 phosphoinositides is crucial for Rac1 activation in Met signalling pathway. EMBO J. (under revision)
138. J. Pizarro-Cerda and P. Cossart. Adhesion and invasion of mammalian cells. Cell (under reviewing)
139. M. Hamon, H. Bierne and P. Cossart. Listerial insights in genomics, cell biology, regulation and physiopathology. Nat. Rev. Microbiol. (under reviewing)
Non peer reviewed chapters and reviews
1. J.-L. Gaillard, S. Dramsi, P. Berche and P. Cossart (1994). Molecular cloning and expression of internalin in Listeria. Methods Enzymol., 236 : 551-565.
2. P. Cossart (1994). Listeria monocytogenes : Strategies for entry and survival in cells and tissues. Strategies for intracellular survival of microbes. Baillière’s Clinical Infectious diseases, 1 : 285-304. Edited by D. Russell.
3. A. Sheehan, C. Kocks, S. Dramsi, E. Gouin, A. Klarsfeld, J. Mengaud and P. Cossart (1994). Molecular and genetic determinants of the Listeria monocytogenes infectious process. Curr. Top. Microbiol. Immunol., 192 : 187-216.
4. S. Dramsi and P. Cossart (1995). Le pouvoir pathogène de Listeria monocytogenes. Ann. Inst. Pasteur (Paris), 5 : 202-211.
5. P. Cossart (1995). Bases génétiques et moléculaires du pouvoir pathogène de Listeria monocytogenes. Med. Mal.Infect., 25 : 210-218.
6. P. Cossart (1995). Actin polymerization by the intracellular bacterial pathogen, Listeria monocytogenes. The Cytoskeleton : 135-142. Springer-Verlag.
7. G. Milon and P. Cossart (1995). Live recombinant Listeria monocytogenes as vaccines and immunotherapeutic agents to prevent growth and to induce regression of experimental tumors ? Trends Microbiol., 3 : 451-452.
8. S. Dramsi, M. Lebrun and P. Cossart (1996). Molecular and genetic determinants involved in invasion of mammalian cells by Listeria monocytogenes. Curr. Top. Microbiol. Immunol., 209 : 61-77.
9. S. Dramsi and P. Cossart (1996) Listeria monocytogenes : molecular aspects of entry and spread into mammalian cells. Bacterial Protein Toxins. B. Witholt, J.-E. Alouf, G.-J. Boulnois, P. Cossart, B.-W. Dijstra, P. Falmagne, F.-J. Fehrenbach, J. Freer, H. Niemann, R. Rappuoli and T. Wadstrom, eds Gustav Fisher Verlag. Stuttgart. New-York.
10. V. David and P. Cossart (1996). Mécanismes physiopathologiques de l’infection à Listeria monocytogenes. La Lettre de l’Infectiologue, XI (5) : 102-105.
11. J. Rocourt and P. Cossart (1996). Listeria monocytogenes : virulence factors/mechanisms of pathogenicity. Fundamentals of Food Microbiology : 337-352, eds ASM.
12. A. Kocks and P. Cossart (1996). ActA (Listeria monocytogenes). Guidebook to protein toxins and their use in cell biology : 75-77. R. Rappuoli and C. Montecucco Editors.
13. K. Ireton and P. Cossart (1997). Mécanismes d’entrée de Listeria monocytogenes dans les cellules de mammifères : facteurs bactériens, ligands cellulaires, signalisation. Ann. Inst. Pasteur (Paris), 8 : 131-138.
14. I. Lasa C. Egile, P. Cossart and P. Sansonetti (1997). Motilité intracellulaire et polymérisation de l’actine par Listeria monocytogenes et Shigella flexneri. Ann. Inst. Pasteur (Paris), 8 : 163-172.
15. P. Cossart, E. Michel and B. Sheehan (1997). Listeria monocytogenes. Bacterial Genomes. : 679-680.Ed. by F. J. de Bruijn, J. R. Lupski and G. M. Weinstock.
16. P. Cossart (1998). Interactions of the bacterial pathogen Listeria monocytogenes with mammalian cells. Molecular Microbiology : 301-318. Ed. by S.J.W. Busby, C.M. Thomas and N.L. Brown, NATO ASI series, H 103.
17. P. Cossart (1998). Interactions of the bacterial pathogen Listeria monocytogenes with mammalian cells : bacterial factors, cellular ligands, and signaling. Folia Microbiol. (Praha), 43 : 291-303.
18. P. Cossart (1998). Listeria monocytogenes : strategies for entry and spread within cells and tissues. Recent advances in the pathogenesis of gastrointestinal bacterial infections : 111-124. P. Rampal and P. boquet. eds John Libbey Eurotext, Paris.
19. J. Miller and P. Cossart (1999). Before the post genomic era. Curr. Opin. Microbiol., 2: 15-17.
20. R. Hurme and P. Cossart (1999). Invasion of mammalian cells by Listeria monocytogenes. In Phagocytosis and pathogens. edited by S. Gordon. Advances in Cell and Molecular Biology of membranes and organelles, 6: 59-79. JAI Press.
21. L. Braun and P. Cossart (2000). Interactions between Listeria monocytogenes and host mammalian cells. Microbes Infect., 2 : 803-811.
22. P. Cossart and D. Portnoy (2000). The cell biology of invasion and intracellular growth by Listeria monocytogenes. Gram-Positive Pathogens : 507-515. Edited by V. Fischetti. ASM Press.
23. P. Cossart and M. Lecuit (2000). Microbial pathogens : an overview. Cellular Microbiology :1-27. Edited by P. Cossart, P. Boquet, S. Normark and R. Rappuoli. ASM Press.
24. Cellular Microbiology (2000). Edited by P. Cossart, P. Boquet, S. Normark and R. Rappuoli. ASM Press.
25. M. Lecuit and P. Cossart (2000). De cadhérine en cadhérine, la E-cadhérine porte d’entrée de Listeria monocytogenes. Med. Sci. (Paris), 16 : 128-130.
26. H. Fsihi, P. Steffen and P. Cossart (2001). Listeria monocytogenes. Molecular Mechanisms of Bacterial Pathogenesis : 751-803. Edited by E. Groisman. Academic Press, London.
27. M. Lecuit and P. Cossart (2001). Listeria monocytogenes. Molecular Medical Microbiology, 2 : 1437-1462. Edited by M. Sussman. Academic Press, London.
28. G. Tran Van Nhieu et P. Cossart (2001). Détournement de fonctions cellulaires clés par les bactéries pathogènes. Med. Sci. (Paris), 17 : 701-711.
38. M. Lecuit and P. Cossart (2001). Un modèle transgénique pour la listériose humaine : rôle de l’interaction entre l’internaline et la E-cadhérine dans la traversée de la barrière intestinale. Med. Sci. (Paris) 17 : 1333-1335.
39. J. Pizarro-Cerda, M. Lecuit et P. Cossart (2002). Measuring and analyzing invasion of mammalian cells by bacterial pathogens : the Listeria monocytogenes system. Meth. Cell. Microbiol., 31 : 161-177. Edited by P.-J. Sansonetti and A. Zychlinsky. Academic Press, London.
40. P. Cossart (2002). Molecular and cellular basis of the infection by Listeria monocytogenes : an overview. Int. J. Med. Microbiol., 291 : 1-9.
41. P. Cossart (2002). Listeria monocytogenes : une bactérie responsable d’infections graves mais adulée des biologistes cellulaires. Cah. Nutr. Diét. Médecine et Nutrition, 37 : 273-277.
42. C. Buchrieser, C. Rusniok, The European Listeria Consortium, F. Kunst, P. Cossart and P. Glaser (2003). Comparison of the genome sequences of Listeria monocytogenes and Listeria innocua: clues for evolution and pathogenicity. FEMS Immunol. Med. Microbiol., 35 : 207-213.
43. P. Cossart and H. Bierne (2003). Entry of Listeria monocytogenes into mammalian cells. Microbial subversion of host cells , 62nd Symposium of the Society for Microbiology., vol 62 : 53-67. Edited by C.D. O’Connor and D.G.E.Smith. Cambridge University Press, Cambridge.
44. J. Pizarro-Cerda, 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.
45. P. Cossart, J.Pizarro-Cerda & M. Lecuit. (2004) Microbiol pathogens : an overview. Cellular Microbiology, 2nd Edition. Edited by P. Cossart, P. Boquet, S. Normark and R. Rappuoli. ASM Press, Washington, DC.
46. M. Lecuit and P. Cossart (2005). Bases moléculaires du tropisme foetoplacentaire de Listeria monocytogenes. Med. Sci. (Paris), 21 : 17-19.
47. J.-E. Galan and P. Cossart. (2005) Host-pathogen interactions : a diversity of themes, a variety of molecular machines. Curr. Opin. Microbiol., 8 :1-3.
48. P. Cossart. (2005) Host specificity : the Listeria paradigm. Nova Acta Leopold., NF92, 344 : 163-166.
49. N. Khelef, M. Lecuit, C. Buchrieser, D. Cabanes, O. Dussurget and P. Cossart. « Listeria monocytogenes and the Genus Listeria ». 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
50. J. Pizarro-Cerda and P. Cossart. (2006). Listeria monocytogenes : Techniques to analyze bacterial infection in vitro. Cell biology : a laboratory handbook, 3rd Edition. Edited by J. E. Celis. Academic Press, London.
51. P. Cossart (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.
52. J. Pizarro-Cerda and P. Cossart. (2006). Subversion of cellular functions by Listeria monocytogenes. J. Pathol., 208 : 215-223.
53. J. Pizarro-Cerda and P. Cossart. (2005) The cell biology of invasion and intracellular growth by Listeria monocytogenes. Gram Positive Pathogens. Edited by V. Fischetti and D. Portnoy. ASM Press, Washington, DC. (in press)
2. P. Cossart (1994). Listeria monocytogenes : Strategies for entry and survival in cells and tissues. Strategies for intracellular survival of microbes. Baillière’s Clinical Infectious diseases, 1 : 285-304. Edited by D. Russell.
3. A. Sheehan, C. Kocks, S. Dramsi, E. Gouin, A. Klarsfeld, J. Mengaud and P. Cossart (1994). Molecular and genetic determinants of the Listeria monocytogenes infectious process. Curr. Top. Microbiol. Immunol., 192 : 187-216.
4. S. Dramsi and P. Cossart (1995). Le pouvoir pathogène de Listeria monocytogenes. Ann. Inst. Pasteur (Paris), 5 : 202-211.
5. P. Cossart (1995). Bases génétiques et moléculaires du pouvoir pathogène de Listeria monocytogenes. Med. Mal.Infect., 25 : 210-218.
6. P. Cossart (1995). Actin polymerization by the intracellular bacterial pathogen, Listeria monocytogenes. The Cytoskeleton : 135-142. Springer-Verlag.
7. G. Milon and P. Cossart (1995). Live recombinant Listeria monocytogenes as vaccines and immunotherapeutic agents to prevent growth and to induce regression of experimental tumors ? Trends Microbiol., 3 : 451-452.
8. S. Dramsi, M. Lebrun and P. Cossart (1996). Molecular and genetic determinants involved in invasion of mammalian cells by Listeria monocytogenes. Curr. Top. Microbiol. Immunol., 209 : 61-77.
9. S. Dramsi and P. Cossart (1996) Listeria monocytogenes : molecular aspects of entry and spread into mammalian cells. Bacterial Protein Toxins. B. Witholt, J.-E. Alouf, G.-J. Boulnois, P. Cossart, B.-W. Dijstra, P. Falmagne, F.-J. Fehrenbach, J. Freer, H. Niemann, R. Rappuoli and T. Wadstrom, eds Gustav Fisher Verlag. Stuttgart. New-York.
10. V. David and P. Cossart (1996). Mécanismes physiopathologiques de l’infection à Listeria monocytogenes. La Lettre de l’Infectiologue, XI (5) : 102-105.
11. J. Rocourt and P. Cossart (1996). Listeria monocytogenes : virulence factors/mechanisms of pathogenicity. Fundamentals of Food Microbiology : 337-352, eds ASM.
12. A. Kocks and P. Cossart (1996). ActA (Listeria monocytogenes). Guidebook to protein toxins and their use in cell biology : 75-77. R. Rappuoli and C. Montecucco Editors.
13. K. Ireton and P. Cossart (1997). Mécanismes d’entrée de Listeria monocytogenes dans les cellules de mammifères : facteurs bactériens, ligands cellulaires, signalisation. Ann. Inst. Pasteur (Paris), 8 : 131-138.
14. I. Lasa C. Egile, P. Cossart and P. Sansonetti (1997). Motilité intracellulaire et polymérisation de l’actine par Listeria monocytogenes et Shigella flexneri. Ann. Inst. Pasteur (Paris), 8 : 163-172.
15. P. Cossart, E. Michel and B. Sheehan (1997). Listeria monocytogenes. Bacterial Genomes. : 679-680.Ed. by F. J. de Bruijn, J. R. Lupski and G. M. Weinstock.
16. P. Cossart (1998). Interactions of the bacterial pathogen Listeria monocytogenes with mammalian cells. Molecular Microbiology : 301-318. Ed. by S.J.W. Busby, C.M. Thomas and N.L. Brown, NATO ASI series, H 103.
17. P. Cossart (1998). Interactions of the bacterial pathogen Listeria monocytogenes with mammalian cells : bacterial factors, cellular ligands, and signaling. Folia Microbiol. (Praha), 43 : 291-303.
18. P. Cossart (1998). Listeria monocytogenes : strategies for entry and spread within cells and tissues. Recent advances in the pathogenesis of gastrointestinal bacterial infections : 111-124. P. Rampal and P. boquet. eds John Libbey Eurotext, Paris.
19. J. Miller and P. Cossart (1999). Before the post genomic era. Curr. Opin. Microbiol., 2: 15-17.
20. R. Hurme and P. Cossart (1999). Invasion of mammalian cells by Listeria monocytogenes. In Phagocytosis and pathogens. edited by S. Gordon. Advances in Cell and Molecular Biology of membranes and organelles, 6: 59-79. JAI Press.
21. L. Braun and P. Cossart (2000). Interactions between Listeria monocytogenes and host mammalian cells. Microbes Infect., 2 : 803-811.
22. P. Cossart and D. Portnoy (2000). The cell biology of invasion and intracellular growth by Listeria monocytogenes. Gram-Positive Pathogens : 507-515. Edited by V. Fischetti. ASM Press.
23. P. Cossart and M. Lecuit (2000). Microbial pathogens : an overview. Cellular Microbiology :1-27. Edited by P. Cossart, P. Boquet, S. Normark and R. Rappuoli. ASM Press.
24. Cellular Microbiology (2000). Edited by P. Cossart, P. Boquet, S. Normark and R. Rappuoli. ASM Press.
25. M. Lecuit and P. Cossart (2000). De cadhérine en cadhérine, la E-cadhérine porte d’entrée de Listeria monocytogenes. Med. Sci. (Paris), 16 : 128-130.
26. H. Fsihi, P. Steffen and P. Cossart (2001). Listeria monocytogenes. Molecular Mechanisms of Bacterial Pathogenesis : 751-803. Edited by E. Groisman. Academic Press, London.
27. M. Lecuit and P. Cossart (2001). Listeria monocytogenes. Molecular Medical Microbiology, 2 : 1437-1462. Edited by M. Sussman. Academic Press, London.
28. G. Tran Van Nhieu et P. Cossart (2001). Détournement de fonctions cellulaires clés par les bactéries pathogènes. Med. Sci. (Paris), 17 : 701-711.
38. M. Lecuit and P. Cossart (2001). Un modèle transgénique pour la listériose humaine : rôle de l’interaction entre l’internaline et la E-cadhérine dans la traversée de la barrière intestinale. Med. Sci. (Paris) 17 : 1333-1335.
39. J. Pizarro-Cerda, M. Lecuit et P. Cossart (2002). Measuring and analyzing invasion of mammalian cells by bacterial pathogens : the Listeria monocytogenes system. Meth. Cell. Microbiol., 31 : 161-177. Edited by P.-J. Sansonetti and A. Zychlinsky. Academic Press, London.
40. P. Cossart (2002). Molecular and cellular basis of the infection by Listeria monocytogenes : an overview. Int. J. Med. Microbiol., 291 : 1-9.
41. P. Cossart (2002). Listeria monocytogenes : une bactérie responsable d’infections graves mais adulée des biologistes cellulaires. Cah. Nutr. Diét. Médecine et Nutrition, 37 : 273-277.
42. C. Buchrieser, C. Rusniok, The European Listeria Consortium, F. Kunst, P. Cossart and P. Glaser (2003). Comparison of the genome sequences of Listeria monocytogenes and Listeria innocua: clues for evolution and pathogenicity. FEMS Immunol. Med. Microbiol., 35 : 207-213.
43. P. Cossart and H. Bierne (2003). Entry of Listeria monocytogenes into mammalian cells. Microbial subversion of host cells , 62nd Symposium of the Society for Microbiology., vol 62 : 53-67. Edited by C.D. O’Connor and D.G.E.Smith. Cambridge University Press, Cambridge.
44. J. Pizarro-Cerda, 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.
45. P. Cossart, J.Pizarro-Cerda & M. Lecuit. (2004) Microbiol pathogens : an overview. Cellular Microbiology, 2nd Edition. Edited by P. Cossart, P. Boquet, S. Normark and R. Rappuoli. ASM Press, Washington, DC.
46. M. Lecuit and P. Cossart (2005). Bases moléculaires du tropisme foetoplacentaire de Listeria monocytogenes. Med. Sci. (Paris), 21 : 17-19.
47. J.-E. Galan and P. Cossart. (2005) Host-pathogen interactions : a diversity of themes, a variety of molecular machines. Curr. Opin. Microbiol., 8 :1-3.
48. P. Cossart. (2005) Host specificity : the Listeria paradigm. Nova Acta Leopold., NF92, 344 : 163-166.
49. N. Khelef, M. Lecuit, C. Buchrieser, D. Cabanes, O. Dussurget and P. Cossart. « Listeria monocytogenes and the Genus Listeria ». 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
50. J. Pizarro-Cerda and P. Cossart. (2006). Listeria monocytogenes : Techniques to analyze bacterial infection in vitro. Cell biology : a laboratory handbook, 3rd Edition. Edited by J. E. Celis. Academic Press, London.
51. P. Cossart (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.
52. J. Pizarro-Cerda and P. Cossart. (2006). Subversion of cellular functions by Listeria monocytogenes. J. Pathol., 208 : 215-223.
53. J. Pizarro-Cerda and P. Cossart. (2005) The cell biology of invasion and intracellular growth by Listeria monocytogenes. Gram Positive Pathogens. Edited by V. Fischetti and D. Portnoy. ASM Press, Washington, DC. (in press)
Book
Cellular Microbiology, 1st Edition. (2000) Edited by P. Cossart, P. Boquet, S. Normak and R. Rappuoli. ASM Press, Washington, DC.
Cellular Microbiology, 2nd Edition. (2005) Edited by P. Cossart, P. Boquet, S. Normak and R. Rappuoli. ASM Press, Washington, DC.
Cellular Microbiology, 2nd Edition. (2005) Edited by P. Cossart, P. Boquet, S. Normak and R. Rappuoli. ASM Press, Washington, DC.