αVβ3-Integrin Relocalizes nectin1 and Routes Herpes Simplex Virus to Lipid Rafts

被引：42

作者：

Gianni, Tatiana ^{[1
]}

Campadelli-Fiume, Gabriella ^{[1
]}

机构：

[1] Alma Mater Studiorum Univ Bologna, Dept Expt Pathol, Sect Microbiol & Virol, Bologna, Italy

来源：

JOURNAL OF VIROLOGY | 2012年 / 86卷 / 05期

关键词：

EPSTEIN-BARR-VIRUS; POLIOVIRUS RECEPTOR; ENDOCYTIC ENTRY; GLYCOPROTEIN-D; LOW-PH; CELLS; TYPE-1; EXPRESSION; INFECTION; PATHWAY;

D O I：

10.1128/JVI.06689-11

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Herpes simplex virus (HSV) enters cells by fusion at plasma membranes or endosomes. Cellular factors route the virus to different pathways. alpha V beta 3-integrin directs HSV to a lipid raft and acidic endosome pathway. We report that infection mediated by nectin1 plus alpha V beta 3-integrin exhibits the same characteristics as entry mediated by raft-located forms of nectin. alpha V beta 3-integrin relocalizes nectin1 to lipid rafts, independently of virus. Thus, HSV routing to the lipid raft-dependent pathway is consequent to the integrin-induced relocalization of nectin1. Inhibition by the Na+/H+ exchanger 5-(N-ethyl-N-isopropyl)amirolide suggests that alpha V beta 3-integrin overexpression favors HSV macropinocytic uptake in some cells but not in others.

引用

页码：2850 / 2855

页数：6

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