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PMID: 2214033 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Oligomeric organization of gp120 on infectious human immunodeficiency virus type 1 particles.

Journal of virology ·Vol. 64 ·No. 11 ·1990-11-00 ·Pages 5674-7

Weiss CD, Levy JA, White JM

Abstract

The oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein (gp120) was examined by treating infectious virions with chemical cross-linking agents and subjecting the protein to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and velocity centrifugation. Immunoblots of cross-linked samples revealed three gp120 bands and an approximately threefold shift in gp120 sedimentation. Our finding of cross-linking solely between gp120 suggests that the gp120 subunits are closely associated in the native envelope structure.

MeSH Terms
Centrifugation, Density Gradient Cross-Linking Reagents Electrophoresis, Polyacrylamide Gel HIV Envelope Protein gp120/ultrastructure HIV-1/ultrastructure Macromolecular Substances Protein Binding
Chemicals
Cross-Linking Reagents HIV Envelope Protein gp120 Macromolecular Substances
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Weiss C D
Cancer Research Institute, School of Medicine, University of California 94143-0450.
Levy J A
White J M
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.64.11.5674-5677.1990
Published
1990-11-00
Pages
5674-7
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC248628
Subset
IM
Grants
NIAID NIH HHS · AI-26471 · United States
NIAID NIH HHS · AI22470 · United States
NIAID NIH HHS · R01-AI24499 · United States
External Links
PubMed source DOI: 10.1128/JVI.64.11.5674-5677.1990 PMC Full Text View journal details
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