Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Removal of the V1-V3 loops from IIIB gp120 results in a protein, PR12, with altered immunogenicity compared to the full-length protein. Polyclonal immune sera raised in rats using PR12 as immunogen recognizes envelope glycoproteins of clades A, B, C, E, F and G and can neutralize chimeric human immunodeficiency virus type 1 (HIV-1) HXB2 viruses expressing envelopes from primary HIV-1 clades B, C, E and F. These data suggest that the immune response to PR12 is directed toward conserved epitopes expressed by viral glycoproteins of diverse genotypes. Five monoclonal antibodies (mAb) derived from PR12-immunized rats were unable to neutralize virus infectivity; hence the epitopes responsible for the induction of this cross-clade neutralizing activity remain to be elucidated. However, PR12 immune sera were able to compete with the human neutralizing mAb 2G12 for gp120 binding, implying that this epitope may be immunogenic when expressed in the context of this truncated protein.

Original publication

DOI

10.1099/0022-1317-83-11-2723

Type

Journal article

Journal

J Gen Virol

Publication Date

11/2002

Volume

83

Pages

2723 - 2732

Keywords

Animals, CHO Cells, Cricetinae, HIV Antibodies, HIV Envelope Protein gp120, HIV-1, Humans, Mutagenesis, Neutralization Tests, Phylogeny