A 14,000-Mr envelope protein of vaccinia virus is involved in cell fusion and forms covalently linked trimers
- PMID: 3806791
- PMCID: PMC253962
- DOI: 10.1128/JVI.61.2.395-404.1987
A 14,000-Mr envelope protein of vaccinia virus is involved in cell fusion and forms covalently linked trimers
Abstract
A monoclonal antibody, MAbC3, that reacts with a 14,000-molecular-weight envelope protein (14K protein) of vaccinia virus completely inhibited virus-induced cell fusion during infection. Immunoblot and immunofluorescence studies revealed that the 14K protein was synthesized at about 6 to 7 h postinfection and transported from the cytoplasm to the cell surface. Synthesis and transport of the 14K protein during infection occurred in the presence of rifampin, an inhibitor of virus maturation. One- and two-dimensional gel electrophoretic analyses demonstrated that the 14K protein forms largely trimers (42K) that are covalently linked by disulfide bonds. The facts that MAbC3 prevents virus uncoating and blocks virus-induced cell fusion but does not prevent virus attachment to cells and the 14K envelope protein forms trimers all suggest that this protein plays major role in virus penetration.
Similar articles
-
A 14K envelope protein of vaccinia virus with an important role in virus-host cell interactions is altered during virus persistence and determines the plaque size phenotype of the virus.Virology. 1987 Aug;159(2):423-32. doi: 10.1016/0042-6822(87)90481-8. Virology. 1987. PMID: 2441522
-
Isolation and characterization of neutralizing monoclonal antibodies to vaccinia virus.J Virol. 1985 Nov;56(2):482-8. doi: 10.1128/JVI.56.2.482-488.1985. J Virol. 1985. PMID: 4057358 Free PMC article.
-
The vaccinia virus 14-kilodalton (A27L) fusion protein forms a triple coiled-coil structure and interacts with the 21-kilodalton (A17L) virus membrane protein through a C-terminal alpha-helix.J Virol. 1998 Dec;72(12):10126-37. doi: 10.1128/JVI.72.12.10126-10137.1998. J Virol. 1998. PMID: 9811753 Free PMC article.
-
Viral glycoprotein-mediated cell fusion assays using vaccinia virus vectors.Methods Mol Biol. 2004;269:309-32. doi: 10.1385/1-59259-789-0:309. Methods Mol Biol. 2004. PMID: 15114023 Review.
-
The exit of vaccinia virus from infected cells.Virus Res. 2004 Dec;106(2):189-97. doi: 10.1016/j.virusres.2004.08.015. Virus Res. 2004. PMID: 15567497 Review.
Cited by
-
Visualization and characterization of the intracellular movement of vaccinia virus intracellular mature virions.J Virol. 2005 Apr;79(8):4755-63. doi: 10.1128/JVI.79.8.4755-4763.2005. J Virol. 2005. PMID: 15795261 Free PMC article.
-
Vaccinia virus preferentially enters polarized epithelial cells through the basolateral surface.J Virol. 1991 Jan;65(1):494-8. doi: 10.1128/JVI.65.1.494-498.1991. J Virol. 1991. PMID: 1985212 Free PMC article.
-
Oligomerization of fusogenic peptides promotes membrane fusion by enhancing membrane destabilization.Biophys J. 2004 Jan;86(1 Pt 1):272-84. doi: 10.1016/S0006-3495(04)74103-X. Biophys J. 2004. PMID: 14695269 Free PMC article.
-
Disulfide bond formation at the C termini of vaccinia virus A26 and A27 proteins does not require viral redox enzymes and suppresses glycosaminoglycan-mediated cell fusion.J Virol. 2009 Jul;83(13):6464-76. doi: 10.1128/JVI.02295-08. Epub 2009 Apr 15. J Virol. 2009. PMID: 19369327 Free PMC article.
-
Plaque size phenotype as a selectable marker to generate vaccinia virus recombinants.J Virol. 1989 Feb;63(2):997-1001. doi: 10.1128/JVI.63.2.997-1001.1989. J Virol. 1989. PMID: 2911129 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources