Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus

Journal of Virology

Volumn 70, Issue 11, 1996, Pages 8142-8147

  Stiasny, Karin ^a   Allison, Steven L ^a   Marchler Bauer, Aron ^b   Kunz, Christian ^a   Heinz, Franz X ^a  

^a UNIVERSITY OF VIENNA   (Austria)

^b RESEARCH INSTITUTE OF MOLECULAR PATHOLOGY   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; OLIGOMER; VIRUS ENVELOPE PROTEIN;

ARTICLE; FLAVIVIRUS; MEMBRANE FUSION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; TICK BORNE ENCEPHALITIS; VIRUS ENVELOPE;

EID: 0029795282     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.11.8142-8147.1996     Document Type: Article

References (34)

1. Allison, S. L., J. Schalich, K. Stiasny, C. W. Mandl, C. Kunz, and F. X. Heinz. 1995. Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. J. Virol. 69:695-700.
2. Buckland, R., and F. Wild. 1989. Leucine zipper motif extends. Nature (London) 338:547.
3. Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature (London) 371:37-43.
4. Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832.
5. Chambers, P., C. R. Pringle, and A. J. Easton. 1990. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71:3075-3080.
6. de Groot, R. J., W. Luytjes, M. C. Horzinek, B. A. M. van der Zeijst, W. J. M. Spaan, and J. A. Lenstra. 1987. Evidence for a coiled-coil structure in the spike proteins of coronaviruses. J. Mol. Biol. 196:963-966.
7. Fuller, S. D., et al. Unpublished results.
8. Gallagher, T. M., C. Escarmis, and M. J. Buchmeier. 1991. Alteration of the pH dependence of coronavirus-induced cell fusion: effect of mutations in the spike glycoprotein. J. Virol. 65:1916-1928.
9. Gallaher, W. R., J. M. Ball, R. F. Garry, M. C. Griffin, and R. C. Montelaro. 1989. A general model for the transmembrane proteins of HIV and other retroviruses. AIDS Res. Hum. Retroviruses 5:431-440.
10. Gaudin, Y., R. W. H. Ruigrok, and J. Brunner. 1995. Low-pH induced conformational changes in viral fusion proteins: implications for the fusion mechanism. J. Gen. Virol. 76:1541-1556.
11. Guirakhoo, F., F. X. Heinz, and C. Kunz. 1989. Epitope model of tick-borne encephalitis virus envelope glycoprotein E: analysis of structural properties, role of carbohydrate side chain, and conformational changes occurring at acidic pH. Virology 169:90-99.
12. Heinz, F. X., S. L. Allison, K. Stiasny, J. Schalich, H. Holzmann, C. W. Mandl, and C. Kunz. 1995. Recombinant and virion derived soluble and particulate immunogens for vaccination against tick-borne encephalitis. Vaccine 13:1636-1642.
13. Heinz, F. X., and C. Kunz. 1980. Chemical crosslinking of tick-borne encephalitis virus and its subunits. J. Gen. Virol. 46:301-309.
14. Heinz, F. X., and C. Kunz. 1980. Isolation of dimeric glycoprotein subunits from tick-borne encephalitis virus. Intervirology 13:169-177.
15. Heinz, F. X., and C. Kunz. 1980. Formation of polymeric glycoprotein complexes from a flavivirus: tick-borne encephalitis virus. J. Gen. Virol. 49:125-132.
16. Heinz, F. X., and C. Kunz. 1981. Homogencity of the structural glycoprotein from European isolates of tick-borne encephalitis virus: comparison with other flaviviruses. J. Gen. Virol. 57:263-274.
17. Heinz, F. X., C. W. Mandl, H. Holzmann, C. Kunz, B. A. Harris, F. Key, and S. C. Harrison. 1991. The flavivirus envelope protein E: isolation of a soluble form from tick-borne encephalitis virus and its crystallization. J. Virol. 65: 5579-5583.
18. Heinz, F. X., K. Stiasny, G. Püschner-Auer, H. Holzmann, S. L. Allison, C. W. Mandl, and C. Kunz. 1994. Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM. Virology 198:109-117.
19. Heinz, F. X., W. Tuma, F. Guirakhoo, and C. Kunz. 1986. A model study of the use of monoclonal antibodies in capture enzyme immunoassays for antigen quantification exploiting the epitope map of tick-borne encephalitis virus. J. Biol. Stand. 14:133-141.
20. Helenius, A. 1995. Alphavirus and flavivirus glycoproteins: structures and functions. Cell 81:651-653.
21. Hofmann, K., and W. Stoffel. 1993. TMbase - a database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler 347:166.
22. Holzmann, H., K. Stiasny, H. York, F. Dorner, C. Kunz, and F. X. Heinz. 1995. Tick-borne encephalitis virus envelope protein E-specific monoclonal antibodies for the study of low pH-induced conformational changes and immature virions. Arch. Virol. 140:213-221.
23. Kielian, M., and S. Jungerwirth. 1990. Mechanism of enveloped virus entry into cells. Mol. Biol. Med. 7:17-31.
24. Lamb, R. A. 1993. Paramyxovirus fusion: a hypothesis for changes. Virology 197:1-11.
25. Lu, M., S. C. Blacklow, and P. S. Kim. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2:1075-1082.
26. Mandl, C. W., F. X. Heinz, and C. Kunz. 1988. Sequence of the structural proteins of tick-borne encephalitis virus (Western subtype) and comparative analysis with other flaviviruses. Virology 166:197-205.
27. Marsh, M., and A. Helenius. 1989. Virus entry into animal cells. Adv. Virus Res. 36:107-151.
28. Rey, F. A., F. X. Heinz, C. Mandl, C. Kunz, and S. C. Harrison. 1995. The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature (London) 375:291-298.
29. Rey, F. A., et al. Unpublished results.
30. Roehrig, J. T., A. R. Hunt, A. J. Johnson, and R. A. Hawkes. 1989. Synthetic peptides derived from the deduced amino acid sequence of the E glycoprotein of Murray valley encephalitis virus elicit antiviral antibody. Virology 171:49-60.
31. Roehrig, J. T., A. J. Johnson, A. R. Hunt, R. A. Bolin, and M. C. Chu. 1990. Antibodies to dengue 2 virus E-glycoprotein synthetic peptides identify antigenic conformation. Virology 177:668-675.
32. Rost, B., and C. Sander. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-72.
33. White, J. M. 1990. Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52:675-697.
34. Wilson, I. A., J. J. Skehel, and D. C. Wiley. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature (London) 289:366-373.