Picornavirus Modification of a Host mRNA Decay Protein

ABSTRACT Due to the limited coding capacity of picornavirus genomic RNAs, host RNA binding proteins play essential roles during viral translation and RNA replication. Here we describe experiments suggesting that AUF1, a host RNA binding protein involved in mRNA decay, plays a role in the infectious...

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Autores principales:	Janet M. Rozovics, Amanda J. Chase, Andrea L. Cathcart, Wayne Chou, Paul D. Gershon, Saiprasad Palusa, Jeffrey Wilusz, Bert L. Semler
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2012
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/ae4060ea75f54179a289bd9da8e1c5b5
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spelling	oai:doaj.org-article:ae4060ea75f54179a289bd9da8e1c5b52021-11-15T15:39:11ZPicornavirus Modification of a Host mRNA Decay Protein10.1128/mBio.00431-122150-7511https://doaj.org/article/ae4060ea75f54179a289bd9da8e1c5b52012-12-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00431-12https://doaj.org/toc/2150-7511ABSTRACT Due to the limited coding capacity of picornavirus genomic RNAs, host RNA binding proteins play essential roles during viral translation and RNA replication. Here we describe experiments suggesting that AUF1, a host RNA binding protein involved in mRNA decay, plays a role in the infectious cycle of picornaviruses such as poliovirus and human rhinovirus. We observed cleavage of AUF1 during poliovirus or human rhinovirus infection, as well as interaction of this protein with the 5′ noncoding regions of these viral genomes. Additionally, the picornavirus proteinase 3CD, encoded by poliovirus or human rhinovirus genomic RNAs, was shown to cleave all four isoforms of recombinant AUF1 at a specific N-terminal site in vitro. Finally, endogenous AUF1 was found to relocalize from the nucleus to the cytoplasm in poliovirus-infected HeLa cells to sites adjacent to (but distinct from) putative viral RNA replication complexes. IMPORTANCE This study derives its significance from reporting how picornaviruses like poliovirus and human rhinovirus proteolytically cleave a key player (AUF1) in host mRNA decay pathways during viral infection. Beyond cleavage of AUF1 by the major viral proteinase encoded in picornavirus genomes, infection by poliovirus results in the relocalization of this host cell RNA binding protein from the nucleus to the cytoplasm. The alteration of both the physical state of AUF1 and its cellular location illuminates how small RNA viruses manipulate the activities of host cell RNA binding proteins to ensure a faithful intracellular replication cycle.Janet M. RozovicsAmanda J. ChaseAndrea L. CathcartWayne ChouPaul D. GershonSaiprasad PalusaJeffrey WiluszBert L. SemlerAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 3, Iss 6 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Janet M. Rozovics Amanda J. Chase Andrea L. Cathcart Wayne Chou Paul D. Gershon Saiprasad Palusa Jeffrey Wilusz Bert L. Semler Picornavirus Modification of a Host mRNA Decay Protein
description	ABSTRACT Due to the limited coding capacity of picornavirus genomic RNAs, host RNA binding proteins play essential roles during viral translation and RNA replication. Here we describe experiments suggesting that AUF1, a host RNA binding protein involved in mRNA decay, plays a role in the infectious cycle of picornaviruses such as poliovirus and human rhinovirus. We observed cleavage of AUF1 during poliovirus or human rhinovirus infection, as well as interaction of this protein with the 5′ noncoding regions of these viral genomes. Additionally, the picornavirus proteinase 3CD, encoded by poliovirus or human rhinovirus genomic RNAs, was shown to cleave all four isoforms of recombinant AUF1 at a specific N-terminal site in vitro. Finally, endogenous AUF1 was found to relocalize from the nucleus to the cytoplasm in poliovirus-infected HeLa cells to sites adjacent to (but distinct from) putative viral RNA replication complexes. IMPORTANCE This study derives its significance from reporting how picornaviruses like poliovirus and human rhinovirus proteolytically cleave a key player (AUF1) in host mRNA decay pathways during viral infection. Beyond cleavage of AUF1 by the major viral proteinase encoded in picornavirus genomes, infection by poliovirus results in the relocalization of this host cell RNA binding protein from the nucleus to the cytoplasm. The alteration of both the physical state of AUF1 and its cellular location illuminates how small RNA viruses manipulate the activities of host cell RNA binding proteins to ensure a faithful intracellular replication cycle.
format	article
author	Janet M. Rozovics Amanda J. Chase Andrea L. Cathcart Wayne Chou Paul D. Gershon Saiprasad Palusa Jeffrey Wilusz Bert L. Semler
author_facet	Janet M. Rozovics Amanda J. Chase Andrea L. Cathcart Wayne Chou Paul D. Gershon Saiprasad Palusa Jeffrey Wilusz Bert L. Semler
author_sort	Janet M. Rozovics
title	Picornavirus Modification of a Host mRNA Decay Protein
title_short	Picornavirus Modification of a Host mRNA Decay Protein
title_full	Picornavirus Modification of a Host mRNA Decay Protein
title_fullStr	Picornavirus Modification of a Host mRNA Decay Protein
title_full_unstemmed	Picornavirus Modification of a Host mRNA Decay Protein
title_sort	picornavirus modification of a host mrna decay protein
publisher	American Society for Microbiology
publishDate	2012
url	https://doaj.org/article/ae4060ea75f54179a289bd9da8e1c5b5
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Picornavirus Modification of a Host mRNA Decay Protein

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