Human immunodeficiency virus type 1 envelope glycoprotein molecules containing membrane fusion-impairing mutations in the V3 region efficiently undergo soluble CD4-stimulated gp120 release

E A Berger; J R Sisler; P L Earl

doi:10.1128/JVI.66.10.6208-6212.1992

Human immunodeficiency virus type 1 envelope glycoprotein molecules containing membrane fusion-impairing mutations in the V3 region efficiently undergo soluble CD4-stimulated gp120 release

J Virol. 1992 Oct;66(10):6208-12. doi: 10.1128/JVI.66.10.6208-6212.1992.

Authors

E A Berger¹, J R Sisler, P L Earl

Affiliation

¹ Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892.

Abstract

The ability of soluble forms of CD4 to induce gp120 release from the human immunodeficiency virus type 1 envelope glycoprotein complex may reflect molecular events associated with membrane fusion. The third hypervariable (V3) region of gp120 appears to play a role in fusion independent of CD4 binding. We demonstrate herein that envelope glycoprotein molecules rendered fusion defective by mutations in conserved residues within the V3 region nevertheless undergo efficient soluble CD4-induced gp120 release.

Publication types

Research Support, U.S. Gov't, P.H.S.

MeSH terms

Animals
Blotting, Western
CD4 Antigens / metabolism*
Cell Line
Genes, Viral
Giant Cells
HIV Envelope Protein gp120 / genetics
HIV Envelope Protein gp120 / metabolism*
HIV Envelope Protein gp120 / physiology*
HIV-1 / genetics
HIV-1 / metabolism*
Membrane Fusion / genetics*
Mutation*
Peptide Fragments / genetics
Peptide Fragments / physiology*
Plasmids
Protein Processing, Post-Translational
Vaccinia virus / genetics

Substances

CD4 Antigens
HIV Envelope Protein gp120
HIV envelope protein gp120 (305-321)
Peptide Fragments