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Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer.
- Source :
-
Nature structural & molecular biology [Nat Struct Mol Biol] 2012 Sep; Vol. 19 (9), pp. 893-9. Date of Electronic Publication: 2012 Aug 05. - Publication Year :
- 2012
-
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.
- Subjects :
- Cell Line
Cryoelectron Microscopy
HIV Envelope Protein gp120 metabolism
HIV Envelope Protein gp160 metabolism
HIV Envelope Protein gp41 metabolism
HIV-1 metabolism
Humans
Models, Molecular
Protein Conformation
Protein Multimerization
Protein Structure, Tertiary
Protein Subunits chemistry
Protein Subunits metabolism
HIV Envelope Protein gp120 chemistry
HIV Envelope Protein gp41 chemistry
HIV Infections virology
HIV-1 chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1545-9985
- Volume :
- 19
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Nature structural & molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 22864288
- Full Text :
- https://doi.org/10.1038/nsmb.2351