HIV Entry and Envelope Glycoprotein-mediated Fusion

被引：169

作者：

Blumenthal, Robert ^{[1
]}

Durell, Stewart ^{[2
]}

Viard, Mathias ^{[1
,3
]}

机构：

[1] NCI, Nanobiol Program, Ctr Canc Res, NIH, Frederick, MD 21702 USA

[2] NCI, Cell Biol Lab, Ctr Canc Res, NIH, Frederick, MD 21702 USA

[3] SAIC Frederick Inc, Basic Sci Program, CCRNP, Frederick Natl Lab, Frederick, MD 21702 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2012年 / 287卷 / 49期

基金：

美国国家卫生研究院;

关键词：

HUMAN-IMMUNODEFICIENCY-VIRUS; VIRAL MEMBRANE-FUSION; GP41 CYTOPLASMIC TAIL; INFLUENZA HEMAGGLUTININ; CELL-FUSION; T-CELLS; GP120; CORE; CONFORMATIONAL-CHANGES; TYPE-1; VIRIONS; PORE FORMATION;

D O I：

10.1074/jbc.R112.406272

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

HIV entry involves binding of the trimeric viral envelope glycoprotein (Env) gp120/gp41 to cell surface receptors, which triggers conformational changes in Env that drive the membrane fusion reaction. The conformational landscape that the lipids and Env navigate en route to fusion has been examined by biophysical measurements on the microscale, whereas electron tomography, x-rays, and NMR have provided insights into the process on the nanoscale and atomic scale. However, the coupling between the lipid and protein pathways that give rise to fusion has not been resolved. Here, we discuss the known and unknown about the overall HIV Env-mediated fusion process.

引用

页码：40841 / 40849

页数：9

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