Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein

被引：254

作者：

Mothes, W

Boerger, AL

Narayan, S

Cunningham, JM

Young, JAT ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Microbiol & Mol Genet, Boston, MA 02115 USA

[2] Brigham & Womens Hosp, Howard Hughes Med Inst, Boston, MA 02115 USA

[3] Brigham & Womens Hosp, Div Hematol & Oncol, Boston, MA 02115 USA

[4] Harvard Univ, Sch Med, Boston, MA 02115 USA

[5] Univ Wisconsin, McArdle Lab Canc Res, Madison, WI 53706 USA

来源：

CELL | 2000年 / 103卷 / 04期

关键词：

D O I：

10.1016/S0092-8674(00)00170-7

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：

Avian leukosis virus (ALV) has been used as a model system to understand the mechanism of pH-independent viral entry involving receptor-induced conformational changes in the viral envelope (Env) glycoprotein that lead to membrane fusion. Here, we report the unexpected finding that ALV entry depends on a critical low pH step that was overlooked when this virus was directly compared to the classical pH-dependent influenza A virus. In contrast to influenza A virus, receptor interaction plays an essential role in priming ALV Env for subsequent low pH triggering. Our results reveal a novel principle in viral entry, namely that receptor interaction can convert a pH-insensitive viral glycoprotein to a form that is responsive to low pH.

引用

页码：679 / 689

页数：11

共 38 条

[1] Identification and characterization of a shared TNFR-related receptor for subgroup B, D, and E avian leukosis viruses reveal cysteine residues required specifically for subgroup E viral entry [J].