Abstract
HIV-1 envelope glycoprotein interaction with a principal coreceptor, CCR5, requires sulfated tyrosines on the CCR5 amino terminus. In this issue of Cell, Choe et al. identified tyrosine-sulfated, neutralizing antibodies against HIV-1 that apparently mimic CCR5. The results demonstrate for the first time that a natural posttranslational modification of an antibody can contribute substantially to antigen recognition.
MeSH terms
-
Antibodies, Monoclonal / metabolism
-
CD4 Antigens / metabolism
-
HIV Antibodies / metabolism*
-
HIV Envelope Protein gp120 / metabolism
-
HIV-1 / immunology*
-
Humans
-
Molecular Mimicry*
-
Peptides / metabolism
-
Protein Processing, Post-Translational
-
Receptors, CCR5 / chemistry
-
Receptors, CCR5 / metabolism*
-
Sulfates / metabolism*
-
Tyrosine / metabolism
Substances
-
Antibodies, Monoclonal
-
CD4 Antigens
-
HIV Antibodies
-
HIV Envelope Protein gp120
-
Peptides
-
Receptors, CCR5
-
Sulfates
-
Tyrosine