Structure of a high-affinity "mimotope" peptide bound to HIV-1-neutralizing antibody b12 explains its inability to elicit gp120 cross-reactive antibodies.

@article{Saphire2007StructureOA,
  title={Structure of a high-affinity "mimotope" peptide bound to HIV-1-neutralizing antibody b12 explains its inability to elicit gp120 cross-reactive antibodies.},
  author={Erica Ollmann Saphire and Marinieve Montero and Alfredo Menendez and Nienke E van Houten and Melita B Irving and Ralph Pantophlet and Michael B. Zwick and Paul W H I Parren and Dennis R. Burton and Jamie K. Scott and Ian A. Wilson},
  journal={Journal of molecular biology},
  year={2007},
  volume={369 3},
  pages={696-709}
}
The human antibody b12 recognizes a discontinuous epitope on gp120 and is one of the rare monoclonal antibodies that neutralize a broad range of primary human immunodeficiency virus type 1 (HIV-1) isolates. We previously reported the isolation of B2.1, a dimeric peptide that binds with high specificity to b12 and competes with gp120 for b12 antibody binding. Here, we show that the affinity of B2.1 was improved 60-fold over its synthetic-peptide counterpart by fusing it to the N terminus of a… CONTINUE READING

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