摘要：

Alanine scanning mutagenesis was performed on monomeric gpl20 of human immunodeficiency virus type 1 to systematically identify residues important for gpl20 recognition by neutralizing and nonneutralizing monoclonai antibodies (MAbs) to the CD4 binding site (CD4bs). Substitutions that affected the binding of broadly neutralizing antir monomeric gpl20 can be engineered to preferentially bind MAb b12, recombinant gpl20s were generated containing combinations of alanine substitutions shown to uniquely enhance b12 binding. Whereas b12 binding was maintained or increased, binding by five nonneutralizing anti-CD4bs MAbs (b3, b6, Fl05, 15e, and F91) was reduced or completely abolished. These reengineered gpl20s are prospective immunogens that may prove capable of eliciting broadly neutralizing antibodies.

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