Browsing by Author "Jaeger, Frederick H."
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Item Antibody light-chain-restricted recognition of the site of immune pressure in the RV144 HIV-1 vaccine trial is phylogenetically conserved.(Cell Press., 2014) Wiehe, Kevin.; Easterhoff, David.; Luo, Kan.; Nicely, Nathan I.; Bradley, Todd.; Jaeger, Frederick H.; Dennison, Sally Moses.; Zhang, Ruijun.; Lloyd, Krissey E.; Stolarchuk, Christina.; Parks, Robert.; Sutherland, Laura L.; Scearce, Richard M.; Morris, Lynn.; Kaewkungwal, Jaranit.; Nitayaphan, Sorachai.; Pitisuttithum, Punnee.; Rerks-Ngarm, Supachai.; Sinangil, Faruk.; Phogat, Sanjay.; Michael, Nelson L.; Kim, Jerome H.; Kelsoe, Garnett.; Montefiori, David Charles.; Tomaras, Georgia D.; Bonsignori, Mattia.; Santra, Sampa.; Kepler, Thomas B.; Alam, Shabnam Munir.; Moody, Michael Anthony.; Liao, Hua-Xin.; Haynes, Barton F.Abstract available in pdf.Item Isolation of a human anti-HIV gp41 membrane proximal region neutralizing antibody by antigen-specific single B cell sorting.(Plos., 2011) Morris, Lynn.; Chen, Xi.; Alam, Shabnam Munir.; Tomaras, Georgia D.; Zhang, Ruijun.; Marshall, Dawn J.; Chen, Bing.; Parks, Robert J.; Foulger, Andrew.; Jaeger, Frederick H.; Donathan, Michele.; Bilska, Mira.; Gray, Elin Solomonovna.; Abdool Karim, Salim Safurdeen.; Kepler, Thomas B.; Whitesides, John.; Montefiori, David Charles.; Moody, Michael Anthony.; Liao, Hua-Xin.; Haynes, Barton F.Broadly neutralizing antibodies are not commonly produced in HIV-1 infected individuals nor by experimental HIV-1 vaccines. When these antibodies do occur, it is important to be able to isolate and characterize them to provide clues for vaccine design. CAP206 is a South African subtype C HIV-1-infected individual previously shown to have broadly neutralizing plasma antibodies targeting the envelope gp41 distal membrane proximal external region (MPER). We have now used a fluoresceinated peptide tetramer antigen with specific cell sorting to isolate a human neutralizing monoclonal antibody (mAb) against the HIV-1 envelope gp41 MPER. The isolated recombinant mAb, CAP206-CH12, utilized a portion of the distal MPER (HXB2 amino acid residues, 673–680) and neutralized a subset of HIV-1 pseudoviruses sensitive to CAP206 plasma antibodies. Interestingly, this mAb was polyreactive and used the same germ-line variable heavy (VH1-69) and variable kappa light chain (VK3-20) gene families as the prototype broadly neutralizing anti-MPER mAb, 4E10 (residues 672–680). These data indicate that there are multiple immunogenic targets in the C-terminus of the MPER of HIV-1 gp41 envelope and suggests that gp41 neutralizing epitopes may interact with a restricted set of naive B cells during HIV-1 infection.