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H211: To examine sequence and conformational differences between subtypes B and C, several experiments were performed with 11 MAbs regarding binding and neutralization. Both binding and neutralization studies revealed that the 11 MAbs could be divided in three different groups, and that the most differences between the subtypes were located in the stem and turn regions of V3. H211 belonged to the group 2 MAbs, which are able to bind subtype B but not subtype C gp120, and are able to bind both V3 peptides. For subtype B, H211 required an R18 residue in order to bind, but the binding was not significantly affected by the H13R change. For subtype C, Q18R mutation did not restore binding to gp120, but the R13H-Q18R double mutation did. Peptide binding was affected only by the R13H mutation, indicating that the poor binding of Q18R gp120 mutant has a structural basis. H211 was not able to neutralize JR-FL isolate, but neutralized SF162. A chimeric SF162 variant with a JR-FL-like V3 sequence was hypersensitive to neutralization by this Ab.
Patel2008
(antibody binding site, neutralization, binding affinity, subtype comparisons)
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Patel2008
Milloni B Patel, Noah G. Hoffman, and Ronald Swanstrom. Subtype-Specific Conformational Differences within the V3 Region of Subtype B and Subtype C Human Immunodeficiency Virus Type 1 Env Proteins. J. Virol., 82(2):903-916, Jan 2008. PubMed ID: 18003735.
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