Human immunodeficiency virus type 1 envelope glycoprotein molecules containing membrane fusion-impairing mutations in the V3 region efficiently undergo soluble CD4-stimulated gp120 release.
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.
Berger
E A
EA
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892.
Sisler
J R
JR
Earl
P L
PL
D000818:Animals; D015153:Blotting, Western; D015704:CD4 Antigens / Q000378:metabolism*; D002460:Cell Line; D005814:Genes, Viral; D015726:Giant Cells; D015699:HIV Envelope Protein gp120 / Q000235:genetics / Q000378:metabolism* / Q000502:physiology*; D015497:HIV-1 / Q000235:genetics / Q000378:metabolism*; D008561:Membrane Fusion / Q000235:genetics*; D009154:Mutation; D010446:Peptide Fragments / Q000235:genetics / Q000502:physiology*; D010957:Plasmids; D011499:Protein Processing, Post-Translational; D014616:Vaccinia virus / Q000235:genetics
D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120; C059762:HIV envelope protein gp120 (305-321); D010446:Peptide Fragments