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Type: Journal article
Title: BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum are required for efficient simian virus 40 infection
Author: Goodwin, E.
Lipovsky, A.
Inoue, T.
Magaldi, T.
Edwards, A.
Van Goor, K.
Paton, A.
Paton, J.
Atwood, W.
Tsai, B.
DiMaio, D.
Citation: mBio, 2011; 2(3):e00101-1-e00101-9
Publisher: Amercian Society for Microbiology
Issue Date: 2011
ISSN: 2150-7511
Editor: Goff, S.P.
Statement of
Edward C. Goodwin, Alex Lipovsky, Takamasa Inoue, Thomas G. Magaldi, Anne P. B. Edwards, Kristin E. Y. Van Goor, Adrienne W. Paton, James C. Paton, Walter J. Atwood, Billy Tsai, and Daniel DiMaio
Abstract: Simian virus 40 (SV40) is a nonenveloped DNA virus that traffics through the endoplasmic reticulum (ER) en route to the nucleus, but the mechanisms of capsid disassembly and ER exit are poorly understood. We conducted an unbiased RNA interference screen to identify cellular genes required for SV40 infection. SV40 infection was specifically inhibited by up to 50-fold by knockdown of four different DNAJ molecular cochaperones or by inhibition of BiP, the Hsp70 partner of DNAJB11. These proteins were not required for the initiation of capsid disassembly, but knockdown markedly inhibited SV40 exit from the ER. In addition, BiP formed a complex with SV40 capsids in the ER in a DNAJB11-dependent fashion. These experiments identify five new cellular proteins required for SV40 infection and suggest that the binding of BiP to the capsid is required for ER exit. Further studies of these proteins will provide insight into the molecular mechanisms of polyomavirus infection and ER function.
Keywords: Cell Line
Endoplasmic Reticulum
Simian virus 40
Heat-Shock Proteins
Molecular Chaperones
HSP40 Heat-Shock Proteins
Host-Pathogen Interactions
Chlorocebus aethiops
Rights: Copyright © 2011 Goodwin et al.
DOI: 10.1128/mBio.00101-11
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Appears in Collections:Aurora harvest
Microbiology and Immunology publications

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