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PMID: 2991572 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Poliovirus protease 3C (P3-7c) does not cleave P220 of the eucaryotic mRNA cap-binding protein complex.

Journal of virology ·Vol. 55 ·No. 2 ·1985-08-00 ·Pages 489-93

Lee KA, Edery I, Hanecak R, Wimmer E, Sonenberg N

Abstract

Infection of HeLa cells by poliovirus results in proteolysis of the large subunit (P220) of the cap-binding protein complex. This is believed to cause the rapid shut-off of host protein synthesis during poliovirus infection. In this communication we examined the possible involvement of poliovirus proteins 3C (a proteinase) and 2C in cleavage of P220. Using antisera against these two viral polypeptides, we were unable to inhibit proteolysis of P220 in an in vitro assay. These results indicate that viral proteins 3C and 2C are not directly involved in cleaving P220 and hence do not cause shut-off of cellular protein synthesis.

MeSH Terms
Carrier Proteins/metabolism HeLa Cells Humans Immune Sera Peptide Hydrolases/immunology,metabolism Poliovirus/enzymology Protein Biosynthesis RNA Cap-Binding Proteins RNA Caps/metabolism
Chemicals
Carrier Proteins Immune Sera RNA Cap-Binding Proteins RNA Caps Peptide Hydrolases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Lee K A
Edery I
Hanecak R
Wimmer E
Sonenberg N
References (14)
14 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1985-08-00
Pages
489-93
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC254958
Subset
IM
Grants
NIAID NIH HHS · AI-15122 · United States
NCI NIH HHS · CA-28146 · United States
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