8gpk
Crystal structure of human anti-HIV-1 broadly neutralizing antibody F6 FabCrystal structure of human anti-HIV-1 broadly neutralizing antibody F6 Fab
Structural highlights
Publication Abstract from PubMedStructure-guided immunofocusing HIV-1 vaccine design entails a comprehensive understanding of Envs from diverse HIV-1 subtypes, including circulating recombinant forms (CRFs). Here, we present the cryo-EM structures of Envs from two Asia prevalent CRFs (CRF01_AE and CRF07_BC) at 3.0 and 3.5 A. We compare the structures and glycosylation patterns of Envs from different subtypes and perform cross-clade statistical analyses to reveal the unique features of CRF01_AE V1 region, which are associated with the resistance to certain bNAbs. We also solve a 4.1 A cryo-EM structure of CRF01_AE Env in complex with F6, the first bNAb from CRF01_AE-infected individuals. F6 recognizes a gp120-gp41 spanning epitope to allosterically destabilize the Env trimer apex and weaken inter-protomer packing, which in turn hinders the receptor binding and induces Env trimer disassembly, demonstrating a dual mechanism of neutralization. These findings broaden our understanding of CRF Envs and shed lights on immunofocusing HIV-1 vaccine design. Structures and immune recognition of Env trimers from two Asia prevalent HIV-1 CRFs.,Niu J, Wang Q, Zhao W, Meng B, Xu Y, Zhang X, Feng Y, Qi Q, Hao Y, Zhang X, Liu Y, Xiang J, Shao Y, Yang B Nat Commun. 2023 Aug 4;14(1):4676. doi: 10.1038/s41467-023-40321-x. PMID:37542068[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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