Ultrastructural Microscopy  

  HEADPREVOST, Marie-Christine / mprevost@pasteur.fr
  MEMBERSDr. BONNE, Isabelle / CAYET, Nadège / GUADAGNINI, Stéphanie / Dr. LOUSSERT, Céline
MALLET, Adeline / PEHAU-ARNAUDET, Gérard / Dr. SACHSE, Martin / SCHMITT, Christine / VILEY, Christine

  Annual Report

The work in the platform for ultrastructural microscopy (PFMU) consists of high resolution ultrastructural analysis aimed at answering scientific questions in collaboration with departments of the Pasteur Institute and with other research establishments such as: INSERM, CNRS, laboratories from different Universities, Curie Institute, Necker Hospital, National Center of Reference and the International network of Pasteur Institutes.

Within these projects, new approaches and technologies are implemented or developed to obtain the best performances when answering to specific questions.

The morphological expertise of the platform lies in the following areas:

  • The study of the interactions between microorganisms and host cells

  • The morphological characterization of microorganisms (bacteria, viruses, parasites)

  • The analysis of the morphological organization of biofilms

  • The investigation of frozen hydrated specimen such as viruses, bacteria, proteins and liposomes and the study of proteins/liposomes interaction by cryo-electron microscopy.

Technological developments

  • Implementation of cryo preparation/new aspects of cryomicroscopy

  • “Cryo-scanning” in scanning electron microscopy

  • High pressure freezing (cryo-fixation), leading to an improvement of the sample structural preservation

  • Cryo-electron microscopy of vitreous sections (CEMOVIS)

In addition, the PFMU offers service activities for rapid diagnosis of agents responsible for new emerging diseases.

Within the institute, the PFMU offers training sessions for users to become autonomous in sample preparation as well as in the samples analysis.

Outside the institute, the PFMU participates in the organization of workshops for a wider audience as the CNRS training workshop « electron microscopy and AFM applied to DNA-protein complexes », co-organized with the UMR 8126 of the IGR (Villejuif) or theCEMOVIS course with the University of Paris-Sud within the multi-level program in the GDR « Structural analysis in Cryo-electron Microscopy ».

At the end of 2007 the PFMU, as part of the Imagopole, has obtained the ISO 9001 certification, issued by the French Association for the Improvement and Quality management (AFAQ).

Keywords: Microscopie Electronique à Transmission et à Balayage (MET et MEB), Ultrastructure, Immunomarquage, Cryocoupes, Cryofixation, Cryomicroscopy, CEMOVIS


Villi in the instestine of C. elegans
Adult worms were cryoimmobilized by high-pressure freezing,subsequently freeze substituted, and embedded in EPON. Bar: 500 nm. In co-laboration with Dr. Vincent Galy, Cell biology of the nucleus, Institute Pasteur.


West NP, Sansonetti P, Mounier J, Exley RM, Parsot C, Guadagnini S, Prévost MC, Prochnicka-Chalufour A, Delepierre M, Tanguy M, Tang CM. 25 february 2005. Optimization of virulence functions through glucosylation of Shigella LPS. Science, Vol 3071313-1317 PMID: 15731456

Dramsi S, Caliot E, Bonne I, Guadagnini S, Prévost MC, Kojadinovic M, Lalioui L, Poyart C, Trieu-Cuot P.2006 Jun. Assembly and role of pili in group B streptococci.  Molecular Microbiology, vol 60, No 6, pp 1401-1413. PMID: 16796677

Arhel NJ, Souquere-Besse S, Munier S, Souque P, Guadagnini S, Rutherford S, Prévost MC, Allen TD, Charneau P. 2007 Jun. HIV-1 DNA Flap formation promotes uncoating of the pre-integration complex at the nuclear pore. EMBO J. 20;26 (12):3025-37. PMID : 17557080

Beauvais A, Schmidt C, Guadagnini S, Roux P, Perret E, Henry C, Paris S, Mallet A, Prévost MC, Latgé JP.2007 Jun. An extracellular matrix glues together the aerial-grown hyphae of Aspergillus fumigatus.Cell Microbiol.; 9(6) :1588-600. PMID : 17371405

de Jonge MI, Pehau-Arnaudet G, Fretz MM, Romain F, Bottai D, Brodin P, Honoré N, Marchal G, Jiskoot W, England P, Cole ST, Brosch R. 2007 Aug. ESAT-6 from Mycobacterium tuberculosis dissociates from its putative chaperone CFP-10 under acidic conditions and exhibits membrane-lysing activity. J Bacteriol.;189(16):6028-34. PMID : 17557817

Activity Reports 2007 - Institut Pasteur
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