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Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles.


ABSTRACT: The selection of human monoclonal antibodies (MAbs) specific for human immunodeficiency virus (HIV) type 1 by binding assays may fail to identify Abs to quaternary epitopes on the intact virions. The HIV neutralization assay was used for the selection of human MAb 2909, which potently neutralizes SF162 and recognizes an epitope on the virus surface but not on soluble proteins. Three regions of gp120, the V2 and V3 loops and the CD4 binding domain, contribute to the epitope recognized by MAb 2909. The existence of such a unique MAb, which defines a complex epitope formed by a quaternary structure, suggests that there may be other new neutralizing HIV epitopes to target with vaccines.

SUBMITTER: Gorny MK 

PROVIDER: S-EPMC1069558 | biostudies-literature | 2005 Apr

REPOSITORIES: biostudies-literature

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Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles.

Gorny Miroslaw K MK   Stamatatos Leonidas L   Volsky Barbara B   Revesz Kathy K   Williams Constance C   Wang Xiao-Hong XH   Cohen Sandra S   Staudinger Robert R   Zolla-Pazner Susan S  

Journal of virology 20050401 8


The selection of human monoclonal antibodies (MAbs) specific for human immunodeficiency virus (HIV) type 1 by binding assays may fail to identify Abs to quaternary epitopes on the intact virions. The HIV neutralization assay was used for the selection of human MAb 2909, which potently neutralizes SF162 and recognizes an epitope on the virus surface but not on soluble proteins. Three regions of gp120, the V2 and V3 loops and the CD4 binding domain, contribute to the epitope recognized by MAb 2909  ...[more]

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