Authors
Hua-Xin Liao, Rebecca Lynch, Tongqing Zhou, Feng Gao, S Munir Alam, Scott D Boyd, Andrew Z Fire, Krishna M Roskin, Chaim A Schramm, Zhenhai Zhang, Jiang Zhu, Lawrence Shapiro, James C Mullikin, S Gnanakaran, Peter Hraber, Kevin Wiehe, Garnett Kelsoe, Guang Yang, Shi-Mao Xia, David C Montefiori, Robert Parks, Krissey E Lloyd, Richard M Scearce, Kelly A Soderberg, Myron Cohen, Gift Kamanga, Mark K Louder, Lillian M Tran, Yue Chen, Fangping Cai, Sheri Chen, Stephanie Moquin, Xiulian Du, M Gordon Joyce, Sanjay Srivatsan, Baoshan Zhang, Anqi Zheng, George M Shaw, Beatrice H Hahn, Thomas B Kepler, Bette TM Korber, Peter D Kwong, John R Mascola, Barton F Haynes
Publication date
2013/4/25
Journal
Nature
Volume
496
Issue
7446
Pages
469-476
Publisher
Nature Publishing Group UK
Description
Current human immunodeficiency virus-1 (HIV-1) vaccines elicit strain-specific neutralizing antibodies. However, cross-reactive neutralizing antibodies arise in approximately 20% of HIV-1-infected individuals, and details of their generation could provide a blueprint for effective vaccination. Here we report the isolation, evolution and structure of a broadly neutralizing antibody from an African donor followed from the time of infection. The mature antibody, CH103, neutralized approximately 55% of HIV-1 isolates, and its co-crystal structure with the HIV-1 envelope protein gp120 revealed a new loop-based mechanism of CD4-binding-site recognition. Virus and antibody gene sequencing revealed concomitant virus evolution and antibody maturation. Notably, the unmutated common ancestor of the CH103 lineage avidly bound the transmitted/founder HIV-1 envelope glycoprotein, and evolution of antibody neutralization …
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Scholar articles
HX Liao, R Lynch, T Zhou, F Gao, SM Alam, SD Boyd… - Nature, 2013