Phenotypes of vesicular stomatitis virus mutants with mutations in the PSAP motif of the matrix protein

Journal of General Virology

Volumn 93, Issue 4, 2012, Pages 857-865

  Obiang, Linda ^a   Raux, Hélène ^a   Ouldali, Malika ^a   Blondel, Danielle ^a   Gaudin, Yves ^a  

^a INSTITUTE FOR INTEGRATIVE BIOLOGY OF THE CELL I2BC   (France)

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX PROTEIN; TUMOR SUSCEPTIBILITY GENE 101 PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE NEDD4;

ANIMAL CELL; ARTICLE; CELL LINE; ELECTRON MICROSCOPY; GENE MUTATION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; VESICULAR STOMATITIS VIRUS; VIRUS PARTICLE;

ANIMALS; CELL LINE; CRICETINAE; DYNAMINS; ENDOSOMAL SORTING COMPLEXES REQUIRED FOR TRANSPORT; HUMANS; MICROSCOPY, ELECTRON; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHENOTYPE; UBIQUITIN-PROTEIN LIGASES; VESICULAR STOMATITIS; VESICULOVIRUS; VIRAL MATRIX PROTEINS; VIRUS ASSEMBLY;

CRICETINAE; VESICULAR STOMATITIS VIRUS;

EID: 84858216672     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.039800-0     Document Type: Article

References (35)

1. Barge, A., Gaudin, Y., Coulon, P. & Ruigrok, R. W. (1993). Vesicular stomatitis virus M protein may be inside the ribonucleocapsid coil. J Virol 67, 7246-7253.
2. Bergmann, J. E. & Fusco, P. J. (1988). The M protein of vesicular stomatitis virus associates specifically with the basolateral membranes of polarized epithelial cells independently of the G protein. J Cell Biol 107, 1707-1715.
3. Brun, G., Bao, X. & Prevec, L. (1995). The relationship of Piry virus to other vesiculoviruses: a re-evaluation based on the glycoprotein gene sequence. Intervirology 38, 274-282.
4. Chong, L. D. & Rose, J. K. (1993). Membrane association of functional vesicular stomatitis virus matrix protein in vivo. J Virol 67, 407-414.
5. Craven, R. C., Harty, R. N., Paragas, J., Palese, P. & Wills, J. W. (1999). Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras. J Virol 73, 3359-3365.
6. Dancho, B., McKenzie, M. O., Connor, J. H. & Lyles, D. S. (2009). Vesicular stomatitis virus matrix protein mutations that affect association with host membranes and viral nucleocapsids. J Biol Chem 284, 4500-4509.
7. Demirov, D. G., Orenstein, J. M. & Freed, E. O. (2002). The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner. J Virol 76, 105-117.
8. Flood, E. A. & Lyles, D. S. (1999). Assembly of nucleocapsids with cytosolic and membrane-derived matrix proteins of vesicular stomatitis virus. Virology 261, 295-308.
9. Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., Morham, S. G., Zavitz, K. H., Wang, H. E., Wettstein, D. A., Stray, K. M., Coté, M. & other authors (2001). Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell 107, 55-65.
10. Gaudier, M., Gaudin, Y. & Knossow, M. (2002). Crystal structure of vesicular stomatitis virus matrix protein. EMBO J 21, 2886-2892.
11. Gaudin, Y., Barge, A., Ebel, C. & Ruigrok, R. W. (1995). Aggregation of VSV M protein is reversible and mediated by nucleation sites: implications for viral assembly. Virology 206, 28-37.
12. Gaudin, Y., Sturgis, J., Doumith, M., Barge, A., Robert, B. & Ruigrok, R. W. (1997). Conformational flexibility and polymerization of vesicular stomatitis virus matrix protein. J Mol Biol 274, 816-825.
13. Ge, P., Tsao, J., Schein, S., Green, T. J., Luo, M. & Zhou, Z. H. (2010). Cryo-EM model of the bullet-shaped vesicular stomatitis virus. Science 327, 689-693.
14. Gö ttlinger, H. G., Dorfman, T., Sodroski, J. G. & Haseltine, W. A. (1991). Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. Proc Natl Acad Sci U S A 88, 3195-3199.
15. Graham, S. C., Assenberg, R., Delmas, O., Verma, A., Gholami, A., Talbi, C., Owens, R. J., Stuart, D. I., Grimes, J. M. & Bourhy, H. (2008). Rhabdovirus matrix protein structures reveal a novel mode of selfassociation. PLoS Pathog 4, e1000251.
16. Grigorov, B., Rabilloud, J., Lawrence, P. & Gerlier, D. (2011). Rapid titration of measles and other viruses: optimization with determination of replication cycle length. PLoS One 6, e24135.
17. Hackett, A. J., Zee, Y. C., Schaffer, F. L. & Talens, L. (1968). Electron microscopic study of the morphogenesis of vesicular stomatitis virus. J Virol 2, 1154-1162.
18. Harty, R. N., Paragas, J., Sudol, M. & Palese, P. (1999). A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: implications for viral budding. J Virol 73, 2921-2929.
19. Harty, R. N., Brown, M. E., McGettigan, J. P., Wang, G., Jayakar, H. R., Huibregtse, J. M., Whitt, M. A. & Schnell, M. J. (2001). Rhabdoviruses and the cellular ubiquitin-proteasome system: a budding interaction. J Virol 75, 10623-10629.
20. Irie, T. & Harty, R. N. (2005). L-domain flanking sequences are important for host interactions and efficient budding of vesicular stomatitis virus recombinants. J Virol 79, 12617-12622.
21. Irie, T., Licata, J. M., Jayakar, H. R., Whitt, M. A., Bell, P. & Harty, R. N. (2004). Functional analysis of late-budding domain activity associated with the PSAP motif within the vesicular stomatitis virus M protein. J Virol 78, 7823-7827.
22. Jayakar, H. R., Murti, K. G. & Whitt, M. A. (2000). Mutations in the PPPY motif of vesicular stomatitis virus matrix protein reduce virus budding by inhibiting a late step in virion release. J Virol 74, 9818-9827.
23. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
24. Lawson, N. D., Stillman, E. A., Whitt, M. A. & Rose, J. K. (1995). Recombinant vesicular stomatitis viruses from DNA. Proc Natl Acad Sci U S A 92, 4477-4481.
25. Libersou, S., Albertini, A. A., Ouldali, M., Maury, V., Maheu, C., Raux, H., de Haas, F., Roche, S., Gaudin, Y. & Lepault, J. (2010). Distinct structural rearrangements of the VSV glycoprotein drive membrane fusion. J Cell Biol 191, 199-210.
26. Luan, P. & Glaser, M. (1994). Formation of membrane domains by the envelope proteins of vesicular stomatitis virus. Biochemistry 33, 4483-4489.
27. Luan, P., Yang, L. & Glaser, M. (1995). Formation of membrane domains created during the budding of vesicular stomatitis virus. A model for selective lipid and protein sorting in biological membranes. Biochemistry 34, 9874-9883.
28. Lyles, D. S., McKenzie, M. O. & Hantgan, R. R. (1996). Stopped-flow, classical, and dynamic light scattering analysis of matrix protein binding to nucleocapsids of vesicular stomatitis virus. Biochemistry 35, 6508-6518.
29. Marriott, A. C. (2005). Complete genome sequences of Chandipura and Isfahan vesiculoviruses. Arch Virol 150, 671-680.
30. McCreedy, B. J., Jr, McKinnon, K. P. & Lyles, D. S. (1990). Solubility of vesicular stomatitis virus M protein in the cytosol of infected cells or isolated from virions. J Virol 64, 902-906.
31. Pauszek, S. J., Allende, R. & Rodriguez, L. L. (2008). Characterization of the full-length genomic sequences of vesicular stomatitis Cocal and Alagoas viruses. Arch Virol 153, 1353-1357.
32. Raux, H., Obiang, L., Richard, N., Harper, F., Blondel, D. & Gaudin, Y. (2010). The matrix protein of vesicular stomatitis virus binds dynamin for efficient viral assembly. J Virol 84, 12609-12618.
33. Schnell, M. J., Buonocore, L., Kretzschmar, E., Johnson, E. & Rose, J. K. (1996). Foreign glycoproteins expressed from recombinant vesicular stomatitis viruses are incorporated efficiently into virus particles. Proc Natl Acad Sci U S A 93, 11359-11365.
34. Solon, J., Gareil, O., Bassereau, P. & Gaudin, Y. (2005). Membrane deformations induced by the matrix protein of vesicular stomatitis virus in a minimal system. J Gen Virol 86, 3357-3363.
35. Timmins, J., Schoehn, G., Ricard-Blum, S., Scianimanico, S., Vernet, T., Ruigrok, R. W. & Weissenhorn, W. (2003). Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4. J Mol Biol 326, 493-502.