Rat monoclonal antibodies to nonoverlapping epitopes of human immunodeficiency virus type 1 gp120 block CD4 binding in vitro.

Abstract:

:Monoclonal antibodies (MAbs) to a recombinant form of the envelope glycoprotein gp120 of human immunodeficiency virus type 1 (HIV-1 IIIB) were raised in rats and screened for their ability to block recombinant gp120 binding to recombinant, soluble CD4 (sCD4) in vitro. Four such MAbs were identified and characterised. Each MAb bound strongly to gp120 from eight widely divergent HIV-1 strains from the United States and Africa. Two MAbs were mapped to the fourth conserved (C4) region of gp120, whereas the other two recognised an as yet undefined, conformationally sensitive epitope. MAbs to the latter epitope were the more potent in blocking the gp120-sCD4 interaction. None of the MAbs, however, had potent neutralising activity.

journal_name

Virology

journal_title

Virology

authors

Cordell J,Moore JP,Dean CJ,Klasse PJ,Weiss RA,McKeating JA

doi

10.1016/0042-6822(91)90755-z

subject

Has Abstract

pub_date

1991-11-01 00:00:00

pages

72-9

issue

1

eissn

0042-6822

issn

1096-0341

pii

0042-6822(91)90755-Z

journal_volume

185

pub_type

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