Dissociation of gp120 from HIV-1 virions induced by soluble CD4.
The CD4 antigen is the high affinity cellular receptor for the human immunodeficiency virus type-1 (HIV-1). Binding of recombinant soluble CD4 (sCD4) or the purified V1 domain of sCD4 to the surface glycoprotein gp120 on virions resulted in rapid dissociation of gp120 from its complex with the transmembrane glycoprotein gp41. This may represent the initial stage in virus-cell and cell-cell fusion. Shedding of gp120 from virions induced by sCD4 may also contribute to the mechanism by which these soluble receptor molecules neutralize HIV-1.
Moore
J P
JP
Chester Beatty Laboratories, Institute of Cancer Research, London, United Kingdom.
McKeating
J A
JA
Weiss
R A
RA
Sattentau
Q J
QJ
D000818:Animals; D000911:Antibodies, Monoclonal / Q000494:pharmacology; D001665:Binding Sites; D001667:Binding, Competitive; D015704:CD4 Antigens / Q000276:immunology / Q000378:metabolism*; D002460:Cell Line; D006224:Cricetinae; D015699:HIV Envelope Protein gp120 / Q000378:metabolism*; D015700:HIV Envelope Protein gp41 / Q000378:metabolism; D015497:HIV-1 / Q000378:metabolism*; D014771:Virion / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120; D015700:HIV Envelope Protein gp41