Analysis of the interaction of antibodies with a conserved enzymatically deglycosylated core of the HIV type 1 envelope glycoprotein 120.

Important note: Information in this article was accurate in 1998. The state of the art may have changed since the publication date.

Analysis of the interaction of antibodies with a conserved enzymatically deglycosylated core of the HIV type 1 envelope glycoprotein 120.

AIDS Res Hum Retroviruses. 1998 Feb 10;14(3):191-8. Unique Identifier : AIDSLINE MED/98150872
Binley JM; Wyatt R; Desjardins E; Kwong PD; Hendrickson W; Moore JP; Sodroski J; Aaron Diamond AIDS Research Center, The Rockefeller University, New; York, New York 10016, USA.

Abstract: The binding of a panel of monoclonal antibodies to V1, V2, and V3 loop-deleted HIV-1 gp120 was studied by competition analysis. Most of the previously defined relationships between gp120 epitopes were preserved on the variable loop-deleted protein, although interactions between some epitopes were dependent on the presence of the V1, V2, and V3 loops. Enzymatic deglycosylation of the variable loop-deleted protein only minimally altered the binding of most antibodies examined. Thus, a carbohydrate-deficient, conserved HIV-1 gp120 core can be produced that has a structure closely approximating that of the full-length, correctly folded gp120 monomer.

Keywords: *Antibodies, Monoclonal/IMMUNOLOGY *HIV Antibodies/IMMUNOLOGY *HIV Envelope Protein gp120/CHEMISTRY *HIV Envelope Protein gp120/IMMUNOLOGY *HIV-1/IMMUNOLOGY
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