A Non-enveloped Virus Hijacks Host Disaggregation Machinery to Translocate across the Endoplasmic Reticulum Membrane

被引：45

作者：

Ravindran, Madhu Sudhan ^{[1
]}

Bagchi, Parikshit ^{[1
]}

Inoue, Takamasa ^{[1
]}

Tsai, Billy ^{[1
]}

机构：

[1] Univ Michigan, Sch Med, Dept Cell & Dev Biol, Ann Arbor, MI 48109 USA

来源：

PLOS PATHOGENS | 2015年 / 11卷 / 08期

基金：

美国国家卫生研究院;

关键词：

NUCLEOTIDE EXCHANGE FACTORS; ER-ASSOCIATED DEGRADATION; QUALITY-CONTROL; MOLECULAR CHAPERONES; HSP110; CHAPERONES; CHOLERA-TOXIN; CAVEOLAR ENDOCYTOSIS; AAA-ATPASE; J-PROTEIN; SIMIAN-VIRUS-40;

D O I：

10.1371/journal.ppat.1005086

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Mammalian cytosolic Hsp110 family, in concert with the Hsc70:J-protein complex, functions as a disaggregation machinery to rectify protein misfolding problems. Here we uncover a novel role of this machinery in driving membrane translocation during viral entry. The nonenveloped virus SV40 penetrates the endoplasmic reticulum (ER) membrane to reach the cytosol, a critical infection step. Combining biochemical, cell-based, and imaging approaches, we find that the Hsp110 family member Hsp105 associates with the ER membrane J-protein B14. Here Hsp105 cooperates with Hsc70 and extracts the membrane-penetrating SV40 into the cytosol, potentially by disassembling the membrane-embedded virus. Hence the energy provided by the Hsc70-dependent Hsp105 disaggregation machinery can be harnessed to catalyze a membrane translocation event.

引用

页数：28