Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles.
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.
Gorny
Miroslaw K
MK
Department of Pathology, New York University School of Medicine, New York, NY 10010, USA.
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
D000911:Antibodies, Monoclonal; D002460:Cell Line; D045744:Cell Line, Tumor; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000737:chemistry*; D015699:HIV Envelope Protein gp120 / Q000737:chemistry / Q000276:immunology*; D015497:HIV-1 / Q000276:immunology*; D006801:Humans; D009500:Neutralization Tests; D020836:Protein Structure, Quaternary; D014771:Virion / Q000276:immunology / Q000502:physiology
D000911:Antibodies, Monoclonal; D000939:Epitopes; D015699:HIV Envelope Protein gp120