Gregory Effantin
  • Université Grenoble Alpes, France
Research focus
  • Immunology
Personal information


Ph.D in Physic for Life Science at the Joseph Fourier University of Grenoble (France), 2005

Current position

Post doctoral fellow at IBS (Institut de Biologie Structurale ), Grenoble, France


  1. Effantin, G., Estrozi, L. F., Aschman, N., Renesto, P., Stanke, N., Lindemann, D., Schoehn, G. and Weissenhorn, W. (2016). Cryo-electron Microscopy Structure of the Native Prototype Foamy Virus Glycoprotein and Virus Architecture. PLoS Pathog 12(7): e1005721.

  2. Hutin, S., Ling, W. L., Round, A., Effantin, G., Reich, S., Iseni, F., Tarbouriech, N., Schoehn, G. and Burmeister, W. P. (2016). Domain Organization of Vaccinia Virus Helicase-Primase D5. J Virol 90(9): 4604-4613.

  3. Caillat, C., Macheboeuf, P., Wu, Y., McCarthy, A. A., Boeri-Erba, E., Effantin, G., Gottlinger, H. G., Weissenhorn, W. and Renesto, P. (2015). Asymmetric ring structure of Vps4 required for ESCRT-III disassembly. Nat Commun 6: 8781.

  4. Lopez, J., Bittame, A., Massera, C., Vasseur, V., Effantin, G., Valat, A., Buaillon, C., Allart, S., Fox, B. A., Rommereim, L. M., Bzik, D. J., Schoehn, G., Weissenhorn, W., Dubremetz, J. F., Gagnon, J., Mercier, C., Cesbron-Delauw, M. F. and Blanchard, N. (2015). Intravacuolar Membranes Regulate CD8 T Cell Recognition of Membrane-Bound Toxoplasma gondii Protective Antigen. Cell Rep 13(10): 2273-2286.

  5. Gutsche, I., Desfosses, A., Effantin, G., Ling, W. L., Haupt, M., Ruigrok, R. W., Sachse, C. and Schoehn, G. (2015). Structural virology. Near-atomic cryo-EM structure of the helical measles virus nucleocapsid. Science 348(6235): 704-707.

  6. Bittame, A., Effantin, G., Petre, G., Ruffiot, P., Travier, L., Schoehn, G., Weissenhorn, W., Cesbron-Delauw, M. F., Gagnon, J. and Mercier, C. (2015). Toxoplasma gondii: biochemical and biophysical characterization of recombinant soluble dense granule proteins GRA2 and GRA6. Biochem Biophys Res Commun 459(1): 107-112.

  7. Hamann, M. V., Mullers, E., Reh, J., Stanke, N., Effantin, G., Weissenhorn, W. and Lindemann, D. (2014). The cooperative function of arginine residues in the Prototype Foamy Virus Gag C-terminus mediates viral and cellular RNA encapsidation. Retrovirology 11: 87.

  8. Lai, R. P., Hock, M., Radzimanowski, J., Tonks, P., Hulsik, D. L., Effantin, G., Seilly, D. J., Dreja, H., Kliche, A., Wagner, R., Barnett, S. W., Tumba, N., Morris, L., LaBranche, C. C., Montefiori, D. C., Seaman, M. S., Heeney, J. L. and Weissenhorn, W. (2014). A fusion intermediate gp41 immunogen elicits neutralizing antibodies to HIV-1. J Biol Chem 289(43): 29912-29926.

  9. Radzimanowski, J., Effantin, G. and Weissenhorn, W. (2014). Conformational plasticity of the Ebola virus matrix protein. Protein Sci 23(11): 1519-1527.

  10. Malet, H., Liu, K., El Bakkouri, M., Chan, S. W., Effantin, G., Bacia, M., Houry, W. A. and Gutsche, I. (2014). Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins. Elife 3: e03653.

  11. Weissenhorn, W., Poudevigne, E., Effantin, G. and Bassereau, P. (2013). How to get out: ssRNA enveloped viruses and membrane fission. Curr Opin Virol 3(2): 159-167.

  12. Effantin, G., Hamasaki, R., Kawasaki, T., Bacia, M., Moriscot, C., Weissenhorn, W., Yamada, T. and Schoehn, G. (2013). Cryo-electron microscopy three-dimensional structure of the jumbo phage PhiRSL1 infecting the phytopathogen Ralstonia solanacearum. Structure 21(2): 298-305.

  13. Effantin, G., Dordor, A., Sandrin, V., Martinelli, N., Sundquist, W. I., Schoehn, G. and Weissenhorn, W. (2013). ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. Cell Microbiol 15(2): 213-226.

  14. Derrien, B., Majeran, W., Effantin, G., Ebenezer, J., Friso, G., van Wijk, K. J., Steven, A. C., Maurizi, M. R. and Vallon, O. (2012). The purification of the Chlamydomonas reinhardtii chloroplast ClpP complex: additional subunits and structural features. Plant Mol Biol 80(2): 189-202.

  15. Germi, R., Effantin, G., Grossi, L., Ruigrok, R. W., Morand, P. and Schoehn, G. (2012). Three-dimensional structure of the Epstein-Barr virus capsid. J Gen Virol 93(Pt 8): 1769-1773.

  16. Bodon, G., Chassefeyre, R., Pernet-Gallay, K., Martinelli, N., Effantin, G., Hulsik, D. L., Belly, A., Goldberg, Y., Chatellard-Causse, C., Blot, B., Schoehn, G., Weissenhorn, W. and Sadoul, R. (2011). Charged multivesicular body protein 2B (CHMP2B) of the endosomal sorting complex required for transport-III (ESCRT-III) polymerizes into helical structures deforming the plasma membrane. J Biol Chem 286(46): 40276-40286.

  17. Effantin, G., Figueroa-Bossi, N., Schoehn, G., Bossi, L. and Conway, J. F. (2010). The tripartite capsid gene of Salmonella phage Gifsy-2 yields a capsid assembly pathway engaging features from HK97 and lambda. Virology 402(2): 355-365.

  18. Effantin, G., Ishikawa, T., De Donatis, G. M., Maurizi, M. R. and Steven, A. C. (2010). Local and global mobility in the ClpA AAA+ chaperone detected by cryo-electron microscopy: functional connotations. Structure 18(5): 553-562.

  19. Effantin, G., Maurizi, M. R. and Steven, A. C. (2010). Binding of the ClpA unfoldase opens the axial gate of ClpP peptidase. J Biol Chem 285(19): 14834-14840.

  20. Adams, P., Kandiah, E., Effantin, G., Steven, A. C. and Ehrenfeld, E. (2009). Poliovirus 2C protein forms homo-oligomeric structures required for ATPase activity. J Biol Chem 284(33): 22012-22021.

  21. Effantin, G., Rosenzweig, R., Glickman, M. H. and Steven, A. C. (2009). Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2. J Mol Biol 386(5): 1204-1211.

  22. Hierro, A., Rojas, A. L., Rojas, R., Murthy, N., Effantin, G., Kajava, A. V., Steven, A. C., Bonifacino, J. S. and Hurley, J. H. (2007). Functional architecture of the retromer cargo-recognition complex. Nature 449(7165): 1063-1067.

  23. Effantin, G., Boulanger, P., Neumann, E., Letellier, L. and Conway, J. F. (2006). Bacteriophage T5 structure reveals similarities with HK97 and T4 suggesting evolutionary relationships. J Mol Biol 361(5): 993-1002.

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