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AIDS Res Hum Retroviruses. 1998 Feb 10;14(3):191-8.

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

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1
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.

PMID:
9491908
DOI:
10.1089/aid.1998.14.191
[Indexed for MEDLINE]
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