Covalent modifications of the Ebola virus glycoprotein

Journal of Virology

Volumn 76, Issue 24, 2002, Pages 12463-12472

  Jeffers, Scott A ^a   Sanders, David Avram ^a   Sanchez, Anthony ^b  

^a PURDUE UNIVERSITY   (United States)

^b NATL CENTER FOR INFECTIOUS DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS GLYCOPROTEIN;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; EBOLA VIRUS; FILOVIRUS; GENE DELETION; GENE MUTATION; GENETIC TRANSDUCTION; GLYCOSYLATION; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN MODIFICATION; PROTEIN SECRETION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

3T3 CELLS; ANIMALS; CELL LINE; GLYCOSYLATION; HUMANS; MICE; MUTAGENESIS, SITE-DIRECTED; STRUCTURE-ACTIVITY RELATIONSHIP; VIRAL ENVELOPE PROTEINS;

EID: 0036893140     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.76.24.12463-12472.2002     Document Type: Article

References (41)

1. Chan, S. Y., R. F. Speck, M. C. Ma, and M. A. Goldsmith. 2000. Distinct mechanisms of entry by envelope glycoproteins of Marburg and Ebola (Zaire) viruses. J. Virol. 74:4933-4937.
2. Chepurnov, A. A., M. N. Tuzova, V. A. Ternovoy, and I. V. Chernukhin. 1999. Suppressive effect of Ebola virus on T cell proliferation in vitro is provided by a 125-kDa GP viral protein. Immunol. Lett. 68:257-261.
3. Delos, S. E., and J. M. White. 2000. Critical role for the cysteines flanking the internal fusion peptide of avian sarcoma/leukosis virus envelope glycoprotein. J. Virol. 74:9738-9741.
4. Ellgaard, L., M. Molinari, and A. Helenius. 1999. Setting the standards: quality control in the secretory pathway. Science 286:1882-1888.
5. Elroy-Stein, O., T. R. Fuerst, and B. Moss. 1989. Cap-independent translation of mRNA conferred by encephalomyocarditis virus 5′ sequence improves the performance of the vaccinia virus/bacteriophage T7 hybrid expression system. Proc. Natl. Acad. Sci. USA 86:6126-6130.
6. Fass, D., S. C. Harrison, and P. S. Kim. 1996. Retrovirus envelope domain at 1.7 angstrom resolution. Nat. Struct. Biol. 3:465-469.
7. Feldmann, H., S. T. Nichol, H. D. Klenk, C. J. Peters, and A. Sanchez. 1994. Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein. Virology 199:469-473.
8. Feldmann, H., V. E. Volchkov, V. A. Volchkova, and H. D. Klenk. 1999. The glycoproteins of Marburg and Ebola virus and their potential roles in pathogenesis. Arch. Virol. Suppl. 15:159-169.
9. Felkner, R. H., and M. J. Roth. 1992. Mutational analysis of the N-linked glycosylation sites of the SU envelope protein of Moloney murine leukemia virus. J. Virol. 66:4258-4264.
10. Gallaher, W. R. 1996. Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses. Cell 85:477-478.
11. Grignani, F., T. Kinsella, A. Mencarelli, M. Valtieri, D. Riganelli, F. Grignani, L. Lanfrancone, C. Peschle, G. P. Nolan, and P. G. Pelicci. 1998. High-efficiency gene transfer and selection of human hematopoietic progenitor cells with a hybrid EBV/retroviral vector expressing the green fluorescence protein. Cancer Res. 58:14-19.
12. Ito, H., S. Watanabe, A. Sanchez, M. A. Whitt, and Y. Kawaoka. 1999. Mutational analysis of the putative fusion domain of Ebola virus glycoprotein. J. Virol. 73:8907-8912.
13. Ito, H., S. Watanabe, A. Takada, and Y. Kawaoka. 2001. Ebola virus glycoprotein: Proteolytic processing, acylation, cell tropism, and detection of neutralizing antibodies. J. Virol. 75:1576-1580.
14. Kayman, S. C., R. Kopelman, S. Projan, D. M. Kinney, and A. Pinter. 1991. Mutational analysis of N-linked glycosylation sites of Friend murine leukemia virus envelope protein. J. Virol. 65:5323-5332.
15. Li, Z., A. Pinter, and S. C. Kayman. 1997. The critical N-linked glycan of murine leukemia virus envelope protein promotes both folding of the C-terminal domains of the precursor polyprotein and stability of the postcleavage envelope complex. J. Virol. 71:7012-7019.
16. Malashkevich, V. N., B. J. Schneider, M. L. McNally, M. A. Milhollen, J. X. Pang, and P. S. Kim. 1999. Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution. Proc. Natl. Acad. Sci. USA 96:2662-2667.
17. Oliver, J. D., H. L. Roderick, D. H. Llewellyn, and S. High. 1999. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol. Biol. Cell 10:2573-2582.
18. Pear, W. S., G. P. Nolan, M. L. Scott, and D. Baltimore. 1993. Production of high-titer helper-free retroviruses by transient transfection. Proc. Natl. Acad. Sci. USA 90:8392-8396.
19. Pinter, A., R. Kopelman, Z. Li, S. C. Kayman, and D. A. Sanders. 1997. Localization of the labile disulfide bond between SU and TM of the murine leukemia virus envelope protein complex to a highly conserved CWLC motif in SU that resembles the active-site sequence of thiol-disulfide exchange enzymes. J. Virol. 71:8073-8077.
20. Ruiz-Arguello, M. B., F. M. Goni, F. B. Pereira, and J. L. Nieva. 1998. Phosphatidylinositol-dependent membrane fusion induced by a putative fusogenic sequence of Ebola virus. J. Virol. 72:1775-1781.
21. Sanchez, A., M. P. Kiley, B. P. Holloway, and D. D. Auperin. 1993. Sequence analysis of the Ebola virus genome: Organization, genetic elements, and comparison with the genome of Marburg virus. Virus Res. 29:215-240.
22. Sanchez, A., S. G. Trappier, B. W. Mahy, C. J. Peters, and S. T. Nichol. 1996. The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing. Proc. Natl. Acad. Sci. USA 93:3602-3607.
23. Sanchez, A., Z. Y. Yang, L. Xu, G. J. Nabel, T. Crews, and C. J. Peters. 1998. Biochemical analysis of the secreted and virion glycoproteins of Ebola virus. J. Virol. 72:6442-6447.
24. Sanders, D. A. 2000. Sulfhydryl involvement in fusion mechanisms, p. 483-514. In H. Hilderson and S. Fuller (ed.), Fusion of Biological Membranes and Related Problems. Kluwer Academic/Plenum Publishers, New York, N.Y.
25. Sharkey, C. M., C. L. North, R. J. Kuhn, and D. A. Sanders. 2001. Ross River virus glycoprotein-pseudotyped retroviruses and stable cell lines for their production. J. Virol. 75:2653-2659.
26. Simmons, G., R. J. Wool-Lewis, F. Baribaud, R. C. Netter, and P. Bates. 2002. Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence. J. Virol. 76:2518-2528.
27. Swift, S., J. Lorens, P. Achacoso, and G. P. Nolan. 1999. Rapid production of retroviruses for efficient gene delivery to mammalian cells using 293T cell-based systems, p. 10.17.14-10.17.29. In R. Coico (ed.), Current Protocols in Immunology, Suppl. 31. John Wiley & Sons, Inc., New York, N.Y.
28. Takada, A., C. Robison, H. Goto, A. Sanchez, K. G. Murti, M. A. Whitt, and Y. Kawaoka. 1997. A system for functional analysis of Ebola virus glycoprotein. Proc. Natl. Acad. Sci. USA 94:14764-14769.
29. Thomas, A., and M. J. Roth. 1995. Analysis of cysteine mutations on the transmembrane protein of Moloney murine leukemia virus. Virology 211: 285-289.
30. Volchkov, V. E., S. Becker, V. A. Volchkova, V. A. Ternovoj, A. N. Kotov, S. V. Netesov, and H. D. Kienk. 1995. GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases. Virology 214:421-430.
31. Volchkov, V. E., V. M. Blinov, and S. V. Netesov. 1992. The envelope glycoprotein of Ebola virus contains an immunosuppressive-like domain similar to oncogenic retroviruses. FEBS Lett. 305:181-184.
32. Volchkov, V. E., H. Feldmann, V. A. Volchkova, and H. D. Klenk. 1998. Processing of the Ebola virus glycoprotein by the proprotein convertase furin. Proc. Natl. Acad. Sci. USA 95:5762-5767.
33. Volchkov, V. E., V. A. Volchkova, E. Muhlberger, L. V. Kolesnikova, M. Weik, O. Dolnik, and H. D. Klenk. 2001. Recovery of infectious Ebola virus from complementary DNA: RNA editing of the GP gene and viral cytotoxicity. Science 291:1965-1969.
34. Volchkova, V. A., H. Feldmann, H. D. Klenk, and V. E. Volchkov. 1998. The nonstructural small glycoprotein sGP of Ebola virus is secreted as an antiparallel-orientated homodimer. Virology 250:408-414.
35. Volchkova, V. A., H. D. Klenk, and V. E. Volchkov. 1999. Delta-peptide is the carboxy-terminal cleavage fragment of the nonstructural small glycoprotein sGP of Ebola virus. Virology 265:164-171.
36. Weissenhorn, W., A. Carfi, K. H. Lee, J. J. Skehel, and D. C. Wiley. 1998. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol. Cell 2:605-616.
37. Wilson, J. A., M. Hevey, R. Bakken, S. Guest, M. Bray, A. L. Schmaljohn, and M. K. Hart. 2000. Epitopes involved in antibody-mediated protection from Ebola virus. Science 287:1664-1666.
38. Wool-Lewis, R. J., and P. Bates. 1998. Characterization of Ebola virus entry by using pseudotyped viruses: Identification of receptor-deficient cell lines. J. Virol. 72:3155-3160.
39. Wool-Lewis, R. J., and P. Bates. 1999. Endoproteolytic processing of the Ebola virus envelope glycoprotein: Cleavage is not required for function. J. Virol. 73:1419-1426.
40. Yang, Z., R. Delgado, L. Xu, R. F. Todd, E. G. Nabel, A. Sanchez, and G. J. Nabel. 1998. Distinct cellular interactions of secreted and transmembrane Ebola virus glycoproteins. Science 279:1034-1037.
41. Yang, Z. Y., H. J. Duckers, N. J. Sullivan, A. Sanchez, E. G. Nabel, and G. J. Nabel. 2000. Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury. Nat. Med. 6:886-889.