Molecular genetic evidence that the hydrophobic anchors of glycoproteins E2 and E1 interact during assembly of alphaviruses

Journal of Virology

Volumn 76, Issue 20, 2002, Pages 10188-10194

  Strauss, Ellen G ^a   Lenches, Edith M ^a   Strauss, James H ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS GLYCOPROTEIN;

ALPHA VIRUS; AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; MOLECULAR GENETICS; NONHUMAN; PRIORITY JOURNAL; ROSS RIVER ALPHA VIRUS; SINDBIS VIRUS; SITE DIRECTED MUTAGENESIS; VIRION; VIROGENESIS; VIRUS ASSEMBLY;

ADAPTATION, PHYSIOLOGICAL; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BASE SEQUENCE; CAPSID; CAPSID PROTEINS; CELL LINE; CRICETINAE; DNA, VIRAL; HYDROPHOBICITY; ISOLEUCINE; MEMBRANE GLYCOPROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; ROSS RIVER VIRUS; SEQUENCE HOMOLOGY, AMINO ACID; SINDBIS VIRUS; VARIATION (GENETICS); VIRAL ENVELOPE PROTEINS; VIRUS ASSEMBLY;

EID: 0036785553     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.76.20.10188-10194.2002     Document Type: Article

References (26)

1. Cheng, R. H., R. J. Kuhn, N. H. Olson, M. G. Rossmann, H.-K. Choi, T. J. Smith, and T. S. Baker. 1995. Nucleocapsid and glycoprotein organization in an enveloped virus. Cell 80:621-630.
2. Forsell, K., L. Xing, T. Kozlovska, R. H. Cheng, and H. Garoff. 2000. Membrane proteins organize a symmetrical virus. EMBO J. 19:5081-5091.
3. Gaedigk-Nitschko, K., M. Ding, and M. J. Schlesinger. 1990. Site-directed mutations in the Sindbis virus 6K protein reveal sites for fatty acylation and the underacylated protein affects virus release and virion structure. Virology 175:282-291.
4. Gaedigk-Nitschko, K., and M. J. Schlesinger. 1990. The Sindbis virus 6K protein can be detected in virions and is acylated with fatty acid. Virology 175:274-281.
5. Hahn, C. S., S. Lustig, E. G. Strauss, and J. H. Strauss. 1988. Western equine encephalitis virus is a recombinant virus. Proc. Natl. Acad. Sci. USA 85:5997-6001.
6. Ivanova, L., S. Lustig, and M. J. Schlesinger. 1995. A pseudo-revertant of a Sindbis virus 6K protein mutant, which corrects for aberrant particle formation, contains two new mutations that map to the ectodomain of the E2 glycoprotein. Virology 206:1027-1034.
7. Kim, K. H., E. G. Strauss, and J. H. Strauss. 2000. Adaptive mutations in Sindbis virus E2 and Ross River virus E1 that allow efficient budding of chimeric viruses. J. Virol. 74:2663-2670.
8. Kuhn, R. J., D. E. Griffin, K. E. Owen, H. G. M. Niesters, and J. H. Strauss. 1996. Chimeric Sindbis-Ross River viruses to study interactions between alphavirus nonstructural and structural regions. J. Virol. 70:7900-7909.
9. Kunkel, T. A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488-492.
10. Lescar, J., A. Roussel, M. W. Wein, J. Navaza, S. D. Fuller, G. Wengler, G. Wengler, and F. A. Rey. 2001. The fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primer for fusogenic activation at endosomal pH. Cell 105:137-148.
11. Liljeström, P., S. Lusa, D. Huylebroeck, and H. Garoff. 1991. In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: the small 6,000-molecular-weight membrane protein modulates virus release J. Virol. 65:4107-4113.
12. Lopez, S., J.-S. Yao, R. J. Kuhn, E. G. Strauss, and J. H. Strauss. 1994. Nucleocapsid-glycoprotein interactions required for alphavirus assembly. J. Virol. 68:1316-1323.
13. Mancini, E. J., M. Clarke, B. E. Gowen, T. Rutten, and S. D. Fuller. 2000. Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus. Mol. Cell 5:255-266.
14. Paredes, A., K. Alwell-Warda, S. C. Weaver, W. I. Chiu, and S. J. Watowich. 2001. Venezuelan equine encephalomyelitis virus structure and its divergence from Old World alphaviruses. J. Virol. 75:9532-9537.
15. Paredes, A. M., D. T. Brown, R. B. Rothnagel, W. Chiu, R. J. Schoepp, R. E. Johnston, and B. V. V. Prasad. 1993. Three-dimensional structure of a membrane-containing virus. Proc. Natl. Acad. Sci. USA 90:9095-9099.
16. Paredes, A. M., H. Heidner, P. Thuman-Commike, B. V. V. Prasad, R. E. Johnson, and W. Chiu. 1998. Structural localization of the E3 glycoprotein in attenuated Sindbis virus mutants. J. Virol. 72:1534-1541.
17. Pletnev, S. V., W. Zhang, S. Mukhopadhyay, B. R. Fisher, R. Hernandez, D. T. Brown, T. S. Baker, M. G. Rossmann, and R. J. Kuhn. 2001. Locations of carbohydrate sites on alphavirus glycoproteins show that E1 forms an icosahedral scaffold. Cell 105:127-136.
18. Strauss, J. H., and E. G. Strauss. 1994. The alphaviruses: gene expression, replication, and evolution. Microbiol. Rev. 58:491-562.
19. Strauss, J. H., E. G. Strauss, and R. J. Kuhn. 1995. Budding of alphaviruses. Trends Microbiol. 3:346-350.
20. Vénien-Bryan, C., and S. D. Fuller. 1994. The organization of the spike complex of Semliki Forest virus. J. Mol. Biol. 236:572-583.
21. Weaver, S. C., W. Kang, Y. Shirako, T. Rümenapf, E. G. Strauss, and J. H. Strauss. 1997. Recombinational history and molecular evolution of Western equine encephalomyelitis complex alphaviruses. J. Virol. 71:613-623.
22. Yao, J., E. G. Strauss, and J. H. Strauss. 1998. Molecular genetic study of the interaction of Sindbis virus E2 with Ross River E1 for virus budding. J. Virol. 72:1418-1423.
23. Yao, J. S., E. G. Strauss, and J. H. Strauss. 1996. Interactions between PE2, E1, and 6K required for assembly of alphaviruses studied with chimeric viruses. J. Virol. 70:7910-7920.
24. Zhang, W., B. R. Fisher, N. H. Olson, J. H. Strauss, R. J. Kuhn, and T. S. Baker. 2002. Aura virus structure suggests that the T=4 organization is a fundamental property of viral structural proteins. J. Virol. 76:7239-7246.
25. Zhang, W., S. Mukhopadhyay, S. V. Pletnev, T. S. Baker, R. J. Kuhn, and M. G. Rossmann. Placement of the structural proteins in Sindbis virus. J. Virol., in press.
26. Zoller, M. J., and M. Smith. 1984. Oligonucleotide-directed mutagenesis: a simple method using two oligonucleotide primers and a single-stranded DNA template. DNA 3:479-488.