posted on 2017-02-24, 19:50authored byDavid Easterhoff, M. Anthony Moody, Daniela Fera, Hao Cheng, Margaret Ackerman, Kevin Wiehe, Kevin O. Saunders, Justin Pollara, Nathan Vandergrift, Rob Parks, Jerome Kim, Nelson L. Michael, Robert J. O’Connell, Jean-Louis Excler, Merlin L. Robb, Sandhya Vasan, Supachai Rerks-Ngarm, Jaranit Kaewkungwal, Punnee Pitisuttithum, Sorachai Nitayaphan, Faruk Sinangil, James Tartaglia, Sanjay Phogat, Thomas B. Kepler, S. Munir Alam, Hua-Xin Liao, Guido Ferrari, Michael S. Seaman, David C. Montefiori, Georgia D. Tomaras, Stephen C. Harrison, Barton F. Haynes
Purified recombinant monoclonal antibodies (mAbs) were assayed by ELISA for (A) blocking the binding of soluble CD4 to AE.A244gp120, and (B) sensitivity to the CD4 binding site mutations Δ371I/P363N, D368R, N276A, and T278A in the AE.A244gp120 protein. (C) Epitope mapping of mAbs on yeast displayed YU2gp120 with point mutations within the inner domain, outer domain and CD4 binding site. (D) Assaying the long HCDR3 CD4 bs antibodies for HIV-1 neutralization in the TZM-bl neutralization assay.