Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer

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Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer

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Title: Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer
Author: Mao, Youdong; Wang, Liping; Gu, Christopher H.; Herschhorn, Alon Menachem; Xiang, Shi-Hua; Haim, Hillel; Yang, Xinzhen; Sodroski, Joseph Gerard

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Citation: Mao, Youdong, Liping Wang, Christopher Gu, Alon Herschhorn, Shi-Hua Xiang, Hillel Haim, Xinzhen Yang, and Joseph Sodroski. 2012. Subunit organization of the membrane-bound hiv-1 envelope glycoprotein trimer. Nature structural & molecular biology 19(9): 893-899.
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Abstract: The trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) spike is a molecular machine that mediates virus entry into host cells and is the sole target for virus-neutralizing antibodies. The mature Env spike results from cleavage of a trimeric gp160 precursor into three gp120 and three gp41 subunits. Here we describe an ~11-Å cryo-EM structure of the trimeric HIV-1 Env precursor in its unliganded state. The three gp120 and three gp41 subunits form a cage-like structure with an interior void surrounding the trimer axis. Interprotomer contacts are limited to the gp41 transmembrane region, the torus-like gp41 ectodomain, and a gp120 trimer association domain composed of the V1/V2 and V3 variable regions. The cage-like architecture, which is unique among characterized viral envelope proteins, restricts antibody access, reflecting requirements imposed by HIV-1 persistence in the host.
Published Version: doi:10.1038/nsmb.2351
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3443289/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:10646780
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