Studies of the conformation-dependent neutralizing epitopes of simian immunodeficiency virus envelope protein.

Journal Article (Journal Article)

It has been shown previously that the major neutralizing epitopes in simian immunodeficiency virus (SIV) are discontinuous and conformation dependent and that the V3 loop, in contrast to that of human immunodeficiency virus (HIV) type 1, does not by itself elicit neutralizing antibodies (K. Javaherian et al., Proc. Natl. Acad. Sci. USA 89:1418-1422, 1992). We now present data showing that on the basis of fractionation of infected macaque sera, protease digestion of the envelope, and binding properties of two neutralizing monoclonal antibodies to SIV and SIV-HIV chimeric envelope proteins, changes in V3 can disrupt the conformation-dependent neutralization region. The chimeric protein did not produce significant neutralizing antibodies against either SIV or HIV. We also report that neutralizing antibodies elicited by recombinant SIV envelope proteins of mac251 and B670 isolates cross-neutralize. Finally, we show that deglycosylation of the SIV envelope results in a molecule which binds neither soluble CD4 nor the neutralizing monoclonal antibodies being investigated here and does not elicit sera with a significant neutralizing titer.

Full Text

Duke Authors

Cited Authors

  • Javaherian, K; Langlois, AJ; Montefiori, DC; Kent, KA; Ryan, KA; Wyman, PD; Stott, J; Bolognesi, DP; Murphey-Corb, M; Larosa, GJ

Published Date

  • April 1994

Published In

Volume / Issue

  • 68 / 4

Start / End Page

  • 2624 - 2631

PubMed ID

  • 7511176

Pubmed Central ID

  • PMC236740

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/JVI.68.4.2624-2631.1994


  • eng

Conference Location

  • United States