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Conformational transitions in CD4 due to complexation with HIV envelope glycoprotein gp120.

Abstract:

The binding of the surface envelope glycoprotein gp120 to its receptor, CD4, has been well characterized and is the primary basis for the cell tropism of HIV. In this study, the interaction between recombinant soluble CD4 and native membrane-associated CD4 with gp120 is probed by the use of mAbs. Complexation of gp120 with both forms of CD4 induces conformational epitopes that can be defined with specific mAbs. CG1, CG7, and CG8 are three novel mAbs that have a distinct preference for CD4 com...

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Publication status:
Published

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Authors


Denisova, G More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School, Jenner Institute
Gershoni, JM More by this author
Journal:
Journal of immunology (Baltimore, Md. : 1950)
Volume:
158
Issue:
3
Pages:
1157-1164
Publication date:
1997-02-05
EISSN:
1550-6606
ISSN:
0022-1767
URN:
uuid:904de6db-1631-4f07-a24c-d3f18852bc3e
Source identifiers:
21394
Local pid:
pubs:21394

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