National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM103310
米国
Other private
SF349247
米国
引用
ジャーナル: Science / 年: 2021 タイトル: Recapitulation of HIV-1 Env-antibody coevolution in macaques leading to neutralization breadth. 著者: Ryan S Roark / Hui Li / Wilton B Williams / Hema Chug / Rosemarie D Mason / Jason Gorman / Shuyi Wang / Fang-Hua Lee / Juliette Rando / Mattia Bonsignori / Kwan-Ki Hwang / Kevin O Saunders / ...著者: Ryan S Roark / Hui Li / Wilton B Williams / Hema Chug / Rosemarie D Mason / Jason Gorman / Shuyi Wang / Fang-Hua Lee / Juliette Rando / Mattia Bonsignori / Kwan-Ki Hwang / Kevin O Saunders / Kevin Wiehe / M Anthony Moody / Peter T Hraber / Kshitij Wagh / Elena E Giorgi / Ronnie M Russell / Frederic Bibollet-Ruche / Weimin Liu / Jesse Connell / Andrew G Smith / Julia DeVoto / Alexander I Murphy / Jessica Smith / Wenge Ding / Chengyan Zhao / Neha Chohan / Maho Okumura / Christina Rosario / Yu Ding / Emily Lindemuth / Anya M Bauer / Katharine J Bar / David Ambrozak / Cara W Chao / Gwo-Yu Chuang / Hui Geng / Bob C Lin / Mark K Louder / Richard Nguyen / Baoshan Zhang / Mark G Lewis / Donald D Raymond / Nicole A Doria-Rose / Chaim A Schramm / Daniel C Douek / Mario Roederer / Thomas B Kepler / Garnett Kelsoe / John R Mascola / Peter D Kwong / Bette T Korber / Stephen C Harrison / Barton F Haynes / Beatrice H Hahn / George M Shaw / 要旨: Neutralizing antibodies elicited by HIV-1 coevolve with viral envelope proteins (Env) in distinctive patterns, in some cases acquiring substantial breadth. We report that primary HIV-1 envelope ...Neutralizing antibodies elicited by HIV-1 coevolve with viral envelope proteins (Env) in distinctive patterns, in some cases acquiring substantial breadth. We report that primary HIV-1 envelope proteins-when expressed by simian-human immunodeficiency viruses in rhesus macaques-elicited patterns of Env-antibody coevolution very similar to those in humans, including conserved immunogenetic, structural, and chemical solutions to epitope recognition and precise Env-amino acid substitutions, insertions, and deletions leading to virus persistence. The structure of one rhesus antibody, capable of neutralizing 49% of a 208-strain panel, revealed a V2 apex mode of recognition like that of human broadly neutralizing antibodies (bNAbs) PGT145 and PCT64-35S. Another rhesus antibody bound the CD4 binding site by CD4 mimicry, mirroring human bNAbs 8ANC131, CH235, and VRC01. Virus-antibody coevolution in macaques can thus recapitulate developmental features of human bNAbs, thereby guiding HIV-1 immunogen design.