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- W3004840451 abstract "Broadly neutralizing antibodies (bNAbs) isolated from HIV-1 infected individuals inform vaccine design and are potential therapeutic agents. However, developing bNAbs with increased efficacy requires understanding how antibodies interact with the native oligomannose and complex-type N-glycan shield that hides most protein epitopes on HIV-1 envelope (Env). We present single-particle cryoEM structures of natively-glycosylated Env trimers complexed with newly identified bNAbs that target distinct epitopes on the surface of Env. A 3.3Å cryoEM structure of Env bound to SF12, an antibody that recognizes a glycan-dominated epitope on Env's silent face, revealed distinct N-glycan conformations across Env protomers, demonstrating intra-Env glycan heterogeneity. Insights from these antibody-Env complex structures have facilitated our understanding of bNAb-glycan interactions critical for their potential use in HIV-1 prevention, therapy, and vaccine development." @default.
- W3004840451 created "2020-02-14" @default.
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- W3004840451 date "2020-02-01" @default.
- W3004840451 modified "2023-09-30" @default.
- W3004840451 title "Structures of Natively-Glycosylated HIV-1 Envelope Trimers Define Antibody-Mediated Neutralization of HIV-1" @default.
- W3004840451 doi "https://doi.org/10.1016/j.bpj.2019.11.211" @default.
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