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

Youdong Mao, Liping Wang, Christopher Gu, Alon Herschhorn, Shi Hua Xiang, Hillel Haim, Xinzhen Yang, Joseph Sodroski

Research output: Contribution to journalArticle

119 Scopus citations

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 glycoprotein precursor, gp160, 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 trimer-association domain of gp120 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.

Original languageEnglish (US)
Pages (from-to)893-899
Number of pages7
JournalNature Structural and Molecular Biology
Volume19
Issue number9
DOIs
StatePublished - Sep 2012

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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