Differential cleavage of IRES trans-acting factors (ITAFs) in cells infected by human rhinovirus.

Abstract

Human rhinovirus (HRV) is a major causative agent of the common cold, and thus has several important health implications. As a member of the picornavirus family, HRV has a small genomic RNA that utilizes several host cell proteins for RNA replication. Host proteins poly(rC) binding protein 2 (PCBP2) and polypyrimidine tract binding protein (PTB) are cleaved by a viral proteinase during the course of infection by the related picornavirus, poliovirus. The cleavage of PCBP2 and PTB inhibits poliovirus translation and has been proposed to mediate a switch in poliovirus template usage from translation to RNA replication. HRV RNA replication also requires a switch in template usage from translation to RNA replication; however, the mechanism is not yet known. We demonstrate that PCBP2 and PTB are differentially cleaved during HRV infection in different cell lines, suggesting that HRV utilizes a mechanism distinct from PCBP2 or PTB cleavage to mediate a switch in template usage.

• Authors: Amanda J Chase, Bert L Semler
• Journal: Virology (Virology) Vol. 449 Pg. 35-44 (Jan 20 2014) ISSN: 1096-0341 [Electronic] United States
• PMID: 24418535 (Publication Type: Journal Article, Research Support, N.I.H., Extramural)
• Copyright: © 2013 Elsevier Inc. All rights reserved.

Chemical References

• PCBP2 protein, human
• RNA, Viral
• RNA-Binding Proteins
• Viral Proteins
• Polypyrimidine Tract-Binding Protein
• Peptide Hydrolases

Topics

• Gene Expression Regulation, Viral
• HeLa Cells
• Humans
• Peptide Hydrolases (genetics, metabolism)
• Picornaviridae Infections (genetics, metabolism, virology)
• Polypyrimidine Tract-Binding Protein (genetics, metabolism)
• Protein Biosynthesis
• Protein Processing, Post-Translational
• RNA, Viral (genetics, metabolism)
• RNA-Binding Proteins (genetics, metabolism)
• Rhinovirus (enzymology, genetics, metabolism)
• Viral Proteins (genetics, metabolism)