Influence of deletions in N or C terminus of HIV-1 glycoprotein 120 on binding of infectivity-enhancing antibody.
Human monoclonal antibody 2.3a was previously shown to enhance human immunodeficiency virus type 1 (HIV-1) infection in vitro. This enhancing antibody recognizes a conserved epitope of envelope glycoprotein gp120. We report here that binding of the 2.3a antibody to gp120 is significantly affected by deletions of certain N- or C-terminal residues of gp120. However, not all such deletions affect the epitope recognized by a broadly neutralizing human monoclonal antibody, 1.5e. These findings suggest the feasibility of designing a gp120 antigen that is free of 2.3a epitope while retaining the conformation of the 1.5e epitope.
Lee
C N
CN
Department of Cancer Biology, Harvard School of Public Health, Boston, Massachusetts 02115.
Robinson
J
J
Cheng
Y L
YL
Essex
M
M
Lee
T H
TH
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D001483:Base Sequence; D001666:Binding Sites, Antibody; D000939:Epitopes / Q000032:analysis / Q000737:chemistry / Q000276:immunology; D015699:HIV Envelope Protein gp120 / Q000096:biosynthesis / Q000737:chemistry / Q000276:immunology*; D015497:HIV-1 / Q000472:pathogenicity / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000276:immunology; D017384:Sequence Deletion
D000911:Antibodies, Monoclonal; D000939:Epitopes; D015699:HIV Envelope Protein gp120; D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins