Vaccination against human immunodeficiency virus type 1 (HIV-1) requir
es an immunogen which will elicit a protective immunity against viruse
s that show a high degree of genetic polymorphism. Therefore, the iden
tification of neutralizing epitopes which are shared by many strains w
ould be useful. In previous studies, we established a human monoclonal
antibody (2F5) that neutralizes a variety of laboratory strains and c
linical isolates of HIV-1. In the present report, we define the amino
acid sequence Glu-Leu-Asp-Lys-Trp-Ala (ELDKWA) on the ectodomain of gp
41 as the epitope recognized by this antibody. The sequence was found
to be conserved in 72% of otherwise highly variable HIV-1 isolates. Es
cape mutants were not detected in cells infected with HIV-1 isolates M
N and RF in the presence of antibody 2F5. Since sequence variability o
f neutralizing epitopes is considered to be a major obstacle to HIV-1
vaccine development, the conserved B-cell epitope described here is a
promising candidate for inclusion in a vaccine against AIDS.