Tyrosine Sulfation of Human Antibodies Contributes to Recognition of the CCR5 Binding Region of HIV-1 gp120
| Autor: | Michael Farzan, Hyeryun Choe, Eric S. Rosenberg, Chih-chin Huang, Tatyana Dorfman, Michael B. Zwick, James E. Robinson, Dennis R. Burton, Miro Venturi, Liping Wang, Natalya Vasilieva, Peter D. Kwong, Christoph Grundner, Joseph Sodroski, Paulette L. Wright, Wenhui Li |
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| Jazyk: | angličtina |
| Předmět: |
Tyrosine sulfation
Receptors CCR5 viruses Molecular Sequence Data HIV Envelope Protein gp120 Models Biological General Biochemistry Genetics and Molecular Biology Cell Line Structure-Activity Relationship Sulfation Humans Amino Acid Sequence Tyrosine Binding site Peptide sequence B-Lymphocytes Binding Sites Hybridomas biology Sulfates Biochemistry Genetics and Molecular Biology(all) Antibodies Monoclonal virus diseases Envelope glycoprotein GP120 Molecular biology Primary and secondary antibodies CD4 Antigens HIV-1 biology.protein Antibody |
| Zdroj: | Cell. (2):161-170 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/S0092-8674(03)00508-7 |
| Popis: | Sulfated tyrosines at the amino terminus of the principal HIV-1 coreceptor CCR5 play a critical role in its ability to bind the HIV-1 envelope glycoprotein gp120 and mediate HIV-1 infection. Here, we show that a number of human antibodies directed against gp120 are tyrosine sulfated at their antigen binding sites. Like that of CCR5, antibody association with gp120 is dependent on sulfate moieties, enhanced by CD4, and inhibited by sulfated CCR5-derived peptides. Most of these antibodies preferentially associate with gp120 molecules of CCR5-utilizing (R5) isolates and neutralize primary R5 isolates more efficiently than laboratory-adapted isolates. These studies identify a distinct subset of CD4-induced HIV-1 neutralizing antibodies that closely emulate CCR5 and demonstrate that tyrosine sulfation can contribute to the potency and diversity of the human humoral response. |
| Databáze: | OpenAIRE |
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