Sequence-Conserved and Antibody-Accessible Sites in the V1V2 Domain of HIV-1 gp120 Envelope Protein
Copyright policy )Sequence-Conserved and Antibody-Accessible Sites in the V1V2 Domain of HIV-1 gp120 Envelope Protein
The immune-correlates analysis of the RV144 trial suggested that epitopes targeted by protective antibodies (Abs) reside in the V1V2 domain of gp120. We mapped V1V2 positional sequence variation onto the conserved V1V2 structural fold and showed that while most of the solvent-accessible V1V2 amino acids vary between strains, there are two accessible molecular surface regions that are conserved and also naturally antigenic. These sites may contain epitopes targeted by broadly cross-reactive anti-V1V2 antibodies.
- University of California, San Francisco United States
- New York University United States
- University of California, San Diego United States
Biomedical and Clinical Sciences, Prevention, Immunology, Clinical Sciences, Molecular Sequence Data, Clinical sciences, HIV Antibodies, HIV Envelope Protein gp120, Good Health and Well Being, Medical Microbiology, Virology, HIV-1, HIV/AIDS, Amino Acid Sequence, Infection, Biotechnology
Biomedical and Clinical Sciences, Prevention, Immunology, Clinical Sciences, Molecular Sequence Data, Clinical sciences, HIV Antibodies, HIV Envelope Protein gp120, Good Health and Well Being, Medical Microbiology, Virology, HIV-1, HIV/AIDS, Amino Acid Sequence, Infection, Biotechnology
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