ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding.

Abstract:

:Membrane penetration of nonenveloped viruses is a poorly understood process. We have investigated early stages of this process by studying the conformational change experienced by polyomavirus (Py) in the lumen of the endoplasmic reticulum (ER), a step that precedes its transport into the cytosol. We show that a PDI-like protein, ERp29, exposes the C-terminal arm of Py's VP1 protein, leading to formation of a hydrophobic particle that binds to a lipid bilayer; this reaction likely mimics initiation of Py penetration across the ER membrane. Expression of a dominant-negative ERp29 decreases Py infection, indicating ERp29 facilitates viral infection. Interestingly, cholera toxin, another toxic agent that crosses the ER membrane into the cytosol, is unfolded by PDI in the ER. Our data thus identify an ER factor that mediates membrane penetration of a nonenveloped virus and suggest that PDI family members are generally involved in ER remodeling reactions.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Magnuson B,Rainey EK,Benjamin T,Baryshev M,Mkrtchian S,Tsai B

doi

10.1016/j.molcel.2005.08.034

subject

Has Abstract

pub_date

2005-10-28 00:00:00

pages

289-300

issue

2

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(05)01600-X

journal_volume

20

pub_type

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