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Lai, Yen-Ting; Wang, Tao; O'Dell, Sijy; Louder, Mark K; Schön, Arne; Cheung, Crystal S F; Chuang, Gwo-Yu; Druz, Aliaksandr; Lin, Bob; McKee, Krisha; Peng, Dongjun; Yang, Yongping; Zhang, Baoshan; Herschhorn, Alon; Sodroski, Joseph; Bailer, Robert T; Doria-Rose, Nicole A; Mascola, John R; Langley, David R; Kwong, Peter D
Nature communications, 01/2019, Letnik: 10, Številka: 1Journal Article
Diverse entry inhibitors targeting the gp120 subunit of the HIV-1 envelope (Env) trimer have been developed including BMS-626529, also called temsavir, a prodrug version of which is currently in phase III clinical trials. Here we report the characterization of a panel of small-molecule inhibitors including BMS-818251, which we show to be >10-fold more potent than temsavir on a cross-clade panel of 208-HIV-1 strains, as well as the engineering of a crystal lattice to enable structure determination of the interaction between these inhibitors and the HIV-1 Env trimer at higher resolution. By altering crystallization lattice chaperones, we identify a lattice with both improved diffraction and robust co-crystallization of HIV-1 Env trimers from different clades complexed to entry inhibitors with a range of binding affinities. The improved diffraction reveals BMS-818251 to utilize functional groups that interact with gp120 residues from the conserved β20-β21 hairpin to improve potency.
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in: SICRIS
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