Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Primary isolates of human immunodeficiency virus type 1 (HIV-1) are much less sensitive to neutralization by soluble CD4 (sCD4) and sCD4-immunoglobulin (Ig) chimeras (CD4-IgG) than are HIV-1 strains adapted to growth in cell culture. We demonstrated that there are significant reductions (10- to 30-fold) in the binding of sCD4 and CD4-IgG to intact virions of five primary isolates compared with sCD4-sensitive, cell culture-adapted isolates RF and IIIB. However, soluble envelope glycoproteins (gp120) derived from the primary isolate virions, directly by detergent solubilization or indirectly by recombinant DNA technology, differed in affinity from RF and IIIB gp120 by only one- to threefold. The reduced binding of sCD4 to these primary isolate virions must therefore be a consequence of the tertiary or quaternary structure of the envelope glycoproteins in their native, oligomeric form on the viral surface. In addition, the rate and extent of sCD4-induced gp120 shedding from these primary isolates was lower than that from RF. We suggest that reduced sCD4 binding and increased gp120 retention together account for the relative resistance of these primary isolates to neutralization by sCD4 and CD4-IgG and that virions of different HIV-1 isolates vary both in the mechanism of sCD4 binding and in subsequent conformational changes in their envelope glycoproteins.

Original publication

DOI

10.1128/jvi.66.1.235-243.1992

Type

Journal article

Journal

Journal of virology

Publication Date

01/1992

Volume

66

Pages

235 - 243

Addresses

Chester Beatty Laboratories, Institute of Cancer Research, London, United Kingdom.

Keywords

Cell Line, Transformed, HIV-1, Virion, Immunoglobulin G, HIV Envelope Protein gp120, HIV Antibodies, Detergents, Enzyme-Linked Immunosorbent Assay, Neutralization Tests, Virus Cultivation, Sequence Alignment, Temperature, Species Specificity, Amino Acid Sequence, Kinetics, Solubility, Molecular Sequence Data, CD4 Antigens