Structural basis of glycan276-dependent recognition by HIV-1 broadly neutralizing antibodies

Summary: Recognition of N-linked glycan at residue N276 (glycan276) at the periphery of the CD4-binding site (CD4bs) on the HIV-envelope trimer is a formidable challenge for many CD4bs-directed antibodies. To understand how this glycan can be recognized, here we isolate two lineages of glycan276-dep...

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Main Authors:	Christopher A. Cottrell, Kartik Manne, Rui Kong, Shuishu Wang, Tongqing Zhou, Gwo-Yu Chuang, Robert J. Edwards, Rory Henderson, Katarzyna Janowska, Megan Kopp, Bob C. Lin, Mark K. Louder, Adam S. Olia, Reda Rawi, Chen-Hsiang Shen, Justin D. Taft, Jonathan L. Torres, Nelson R. Wu, Baoshan Zhang, Nicole A. Doria-Rose, Myron S. Cohen, Barton F. Haynes, Lawrence Shapiro, Andrew B. Ward, Priyamvada Acharya, John R. Mascola, Peter D. Kwong
Format:	Article
Language:	English
Published:	Elsevier 2021-11-01
Series:	Cell Reports
Subjects:	antibody-antigen binding antibody approach angle CD4 binding site cryo-EM glycan conformation glycan276
Online Access:	http://www.sciencedirect.com/science/article/pii/S2211124721013954

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http://www.sciencedirect.com/science/article/pii/S2211124721013954

Structural basis of glycan276-dependent recognition by HIV-1 broadly neutralizing antibodies

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