CCR5 mimicry by sulfated human anti-HIV-1 antibodies.
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.
Lin
George
G
Department of Medicine, Hematology-Oncology Division, University of Pennsylvania, Philadelphia, PA 19104, USA.
Hoxie
James A
JA
D000911:Antibodies, Monoclonal / Q000378:metabolism; D015704:CD4 Antigens / Q000378:metabolism; D015483:HIV Antibodies / Q000378:metabolism*; D015699:HIV Envelope Protein gp120 / Q000378:metabolism; D015497:HIV-1 / Q000276:immunology*; D006801:Humans; D018716:Molecular Mimicry; D010455:Peptides / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D019713:Receptors, CCR5 / Q000737:chemistry / Q000378:metabolism*; D013431:Sulfates / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism
D000911:Antibodies, Monoclonal; D015704:CD4 Antigens; D015483:HIV Antibodies; D015699:HIV Envelope Protein gp120; D010455:Peptides; D019713:Receptors, CCR5; D013431:Sulfates; D014443:Tyrosine