The inability of vaccinia virus A33R protein to form intermolecular disulfide-bonded homodimers does not affect the production of infectious extracellular virus

Abstract The orthopoxvirus protein A33 forms a disulfide-bonded high molecular weight species that could be either a homodimer or a heteromultimer. The protein is a major target for neutralizing antibodies and the majority of antibodies raised against A33 only recognize the disulfide-bonded form. He...

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Veröffentlicht in:	Virology (New York, N.Y.) N.Y.), 2010-12, Vol.408 (1), p.109-118
Hauptverfasser:	Chan, Winnie M, Kalkanoglu, Aja E, Ward, Brian M
Format:	Artikel
Sprache:	eng
Schlagworte:	A33R Amino acids Antibodies Cysteine Cysteine - genetics Cysteine - metabolism Disulfides - metabolism HeLa Cells Humans Infection Infectious Disease Intermolecular disulfide bond Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Morphogenesis Mutagenesis, Site-Directed Orthopoxvirus Protein Multimerization Serine Serine - genetics Serine - metabolism Vaccinia virus Vaccinia virus - growth & development Vaccinia virus - pathogenicity Vaccinia virus - physiology Viral Envelope Proteins - genetics Viral Envelope Proteins - metabolism Viral Load Viral Plaque Assay Virus Assembly Virus Replication
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