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Oligomerization of herpes simplex virus glycoprotein B
Journal of Virology
|November 1, 1986
Summary
Herpes simplex virus glycoprotein B (gB) forms stable homodimers rapidly after synthesis. These dimers exhibit variations in N-linked oligosaccharide processing, affecting their electrophoretic mobility.
Area of Science:
- Virology
- Molecular Biology
- Protein Chemistry
Background:
- Herpes simplex virus glycoprotein B (gB) is crucial for viral entry and infectivity.
- gB exists as detergent-stable, heat-dissociable oligomers in virions and infected cells.
Purpose of the Study:
- To investigate the composition and formation requirements of gB oligomers.
- To identify the specific oligomeric form of faster-migrating gB species.
Main Methods:
- Extraction of gB oligomers from virions and infected cells.
- Analysis of gB oligomer composition using electrophoretic techniques.
- Investigation of factors influencing gB dimerization, including glycosylation and viral protein expression.
Main Results:
- Faster-migrating forms of gB oligomers were identified as homodimers.
- gB dimerization occurs rapidly (within minutes) post-polypeptide synthesis.
- Dimerization is independent of glycosylation, other viral proteins, and virion assembly.
- Electrophoretic heterogeneity of gB dimers is attributed to differential N-linked oligosaccharide processing and other mobility-influencing modifications.
Conclusions:
- Herpes simplex virus glycoprotein B rapidly forms homodimers.
- Oligosaccharide processing variations contribute to the observed heterogeneity of gB dimers.