Voss, James E.Andrabi, RaieesMcCoy, Laura E.de Val, NataliaFuller, Roberta P.Messmer, TerrenceSu, Ching-YaoSok, DevinKhan, Salar N.Garces, FernandoPritchard, Laura K.Wyatt, Richard T.Ward, Andrew B.Crispin, MaxWilson, Ian A.Burton, Dennis R.2017-12-062017Voss, J. E., R. Andrabi, L. E. McCoy, N. de Val, R. P. Fuller, T. Messmer, C. Su, et al. 2017. “Elicitation of Neutralizing Antibodies Targeting the V2 Apex of the HIV Envelope Trimer in a Wild-Type Animal Model.” Cell Reports 21 (1): 222-235. doi:10.1016/j.celrep.2017.09.024. http://dx.doi.org/10.1016/j.celrep.2017.09.024.http://nrs.harvard.edu/urn-3:HUL.InstRepos:34492154Summary Recent efforts toward HIV vaccine development include the design of immunogens that can engage B cell receptors with the potential to affinity mature into broadly neutralizing antibodies (bnAbs). V2-apex bnAbs, which bind a protein-glycan region on HIV envelope glycoprotein (Env) trimer, are among the most broad and potent described. We show here that a rare “glycan hole” at the V2 apex is enriched in HIV isolates neutralized by inferred precursors of prototype V2-apex bnAbs. To investigate whether this feature could focus neutralizing responses onto the apex bnAb region, we immunized wild-type rabbits with soluble trimers adapted from these Envs. Potent autologous tier 2 neutralizing responses targeting basic residues in strand C of the V2 region, which forms the core epitope for V2-apex bnAbs, were observed. Neutralizing monoclonal antibodies (mAbs) derived from these animals display features promising for subsequent broadening of the response.en-USHIVvaccinegermline targetingSOSIP trimerV2 apeximmunizationsrabbitneutralizing antibodiesbnAbsglycan holeJournal Article2017-12-0610.1016/j.celrep.2017.09.024