Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion peptide site

Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion peptide site

The HIV-1 fusion peptide (FP) represents a promising vaccine target, but global FP sequence diversity among circulating strains has limited anti-FP antibodies to ~60% neutralization breadth. Here we evolve the FP-targeting antibody VRC34.01 in vitro to enhance FP-neutralization using site saturation...

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Bibliographic Details
Main Authors: Banach, Bailey B, Pletnev, Sergei, Olia, Adam S, Xu, Kai, Zhang, Baoshan, Rawi, Reda, Bylund, Tatsiana, Doria-Rose, Nicole A, Nguyen, Thuy Duong, Fahad, Ahmed S, Lee, Myungjin, Lin, Bob C, Liu, Tracy, Louder, Mark K, Madan, Bharat, McKee, Krisha, O’Dell, Sijy, Sastry, Mallika, Schön, Arne, Bui, Natalie, Shen, Chen-Hsiang, Wolfe, Jacy R, Chuang, Gwo-Yu, Mascola, John R, Kwong, Peter D, DeKosky, Brandon J
Other Authors: Massachusetts Institute of Technology. Department of Chemical Engineering
Format: Article
Language:English
Published: Springer Science and Business Media LLC 2025
Online Access:https://hdl.handle.net/1721.1/158240

Internet

https://hdl.handle.net/1721.1/158240

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