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PMID: 1720631 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

N-terminal residues 105-117 of HIV-1 gp120 are not involved in CD4 binding.

AIDS research and human retroviruses ·Vol. 7 ·No. 10 ·1991-10-00 ·Pages 855-8

el Ahmar W, Poumbourios P, McPhee DA, Kemp BE

Abstract

Syu et al. recently reported that deletion of residues Ile-108 to Leu-116 from the amino terminus of gp120 abolished CD4 binding. The authors have investigated the role of this region using a monospecific antipeptide antibody. As assessed by a microtiter plate-based radioimmunoassay, the antibody, raised in sheep against a synthetic peptide encompassing this deleted region, does not inhibit the gp120-CD4 association. The reported loss of CD4 binding ability, resulting from the deletion in this region of gp120, is likely to be due to indirect structural changes in gp120 rather than representing an integral part of the CD4 binding domain.

MeSH Terms
Amino Acid Sequence Animals Binding Sites CD4 Antigens/metabolism Epitopes HIV Antibodies HIV Envelope Protein gp120/genetics,immunology,metabolism HIV-1/genetics,immunology,metabolism Humans Molecular Sequence Data Peptides/genetics,immunology,metabolism Sheep
Chemicals
CD4 Antigens Epitopes HIV Antibodies HIV Envelope Protein gp120 Peptides
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
el Ahmar W
St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Poumbourios P
McPhee D A
Kemp B E
Article Info
Journal
AIDS research and human retroviruses
Abbr.
AIDS Res Hum Retroviruses
ISSN
0889-2229
Published
1991-10-00
Pages
855-8
Language
English
Region
United States
NLM ID
8709376
Subset
IM
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