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 Celljournal_title
Molecular cellauthors
Magnuson B,Rainey EK,Benjamin T,Baryshev M,Mkrtchian S,Tsai Bdoi
10.1016/j.molcel.2005.08.034subject
Has Abstractpub_date
2005-10-28 00:00:00pages
289-300issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(05)01600-Xjournal_volume
20pub_type
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