Journal article
Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer
Nature structural & molecular biology, Vol.19(9), pp.893-899
09/2012
DOI: 10.1038/nsmb.2351
PMCID: PMC3443289
PMID: 22864288
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.
Details
- Title: Subtitle
- Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer
- Creators
- Youdong Mao - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USALiping Wang - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USAChristopher Gu - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USAAlon Herschhorn - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USAShi-Hua Xiang - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USAHillel Haim - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USAXinzhen Yang - Division of Viral Pathogenesis, Beth Israel Deaconess Medical Center, Department of Medicine, Harvard Medical School, Boston, Massachusetts, USAJoseph Sodroski - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USA
- Resource Type
- Journal article
- Publication Details
- Nature structural & molecular biology, Vol.19(9), pp.893-899
- DOI
- 10.1038/nsmb.2351
- PMID
- 22864288
- PMCID
- PMC3443289
- NLM abbreviation
- Nat Struct Mol Biol
- ISSN
- 1545-9993
- eISSN
- 1545-9985
- Language
- English
- Date published
- 09/2012
- Academic Unit
- Microbiology and Immunology
- Record Identifier
- 9984083273802771
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