Severe Acute Respiratory Syndrome Coronavirus Nonstructural Protein 2 Interacts with a Host Protein Complex Involved in Mitochondrial Biogenesis and Intracellular Signaling

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Published inJournal of Virology Vol. 83; no. 19; pp. 10314 - 10318
Main Authors Cornillez-Ty, Cromwell T., Liao, Lujian, Yates, John R., Kuhn, Peter, Buchmeier, Michael J.
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.10.2009
American Society for Microbiology (ASM)
Subjects
Online AccessGet full text
ISSN0022-538X
1098-5514
1098-5514
DOI10.1128/JVI.00842-09

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Abstract Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
AbstractList The severe acute respiratory syndrome coronavirus (SARS-CoV) generates 16 nonstructural proteins (nsp's) through proteolytic cleavage of a large precursor protein. Although several nsp's exhibit catalytic activities that are important for viral replication and transcription, other nsp's have less clearly defined roles during an infection. In order to gain a better understanding of their functions, we attempted to identify host proteins that interact with nsp's during SARS-CoV infections. For nsp2, we identified an interaction with two host proteins, prohibitin 1 (PHB1) and PHB2. Our results suggest that nsp2 may be involved in the disruption of intracellular host signaling during SARS-CoV infections.The severe acute respiratory syndrome coronavirus (SARS-CoV) generates 16 nonstructural proteins (nsp's) through proteolytic cleavage of a large precursor protein. Although several nsp's exhibit catalytic activities that are important for viral replication and transcription, other nsp's have less clearly defined roles during an infection. In order to gain a better understanding of their functions, we attempted to identify host proteins that interact with nsp's during SARS-CoV infections. For nsp2, we identified an interaction with two host proteins, prohibitin 1 (PHB1) and PHB2. Our results suggest that nsp2 may be involved in the disruption of intracellular host signaling during SARS-CoV infections.
The severe acute respiratory syndrome coronavirus (SARS-CoV) generates 16 nonstructural proteins (nsp's) through proteolytic cleavage of a large precursor protein. Although several nsp's exhibit catalytic activities that are important for viral replication and transcription, other nsp's have less clearly defined roles during an infection. In order to gain a better understanding of their functions, we attempted to identify host proteins that interact with nsp's during SARS-CoV infections. For nsp2, we identified an interaction with two host proteins, prohibitin 1 (PHB1) and PHB2. Our results suggest that nsp2 may be involved in the disruption of intracellular host signaling during SARS-CoV infections.
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
Author John R. Yates III
Lujian Liao
Michael J. Buchmeier
Cromwell T. Cornillez-Ty
Peter Kuhn
AuthorAffiliation Molecular and Integrative Neurosciences Department, 1 Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, 2 Department of Molecular Biology and Biochemistry, 3 Division of Infectious Disease, Department of Medicine, University of California, Irvine, 3205 McGaugh Hall, Irvine, California 92697-3900 4
AuthorAffiliation_xml – name: Molecular and Integrative Neurosciences Department, 1 Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, 2 Department of Molecular Biology and Biochemistry, 3 Division of Infectious Disease, Department of Medicine, University of California, Irvine, 3205 McGaugh Hall, Irvine, California 92697-3900 4
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  surname: Cornillez-Ty
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  surname: Buchmeier
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  organization: Molecular and Integrative Neurosciences Department, Department of Molecular Biology and Biochemistry, Division of Infectious Disease, Department of Medicine, University of California, Irvine, 3205 McGaugh Hall, Irvine, California 92697-3900
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Issue 19
Keywords Infection
Virus
Lung disease
Mitochondria
Coronavirus
Respiratory disease
Viral disease
Severe acute respiratory syndrome
Intracellular
Coronaviridae
Nidovirales
Protein
Language English
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Corresponding author. Mailing address: Department of Molecular Biology and Biochemistry and Division of Infectious Disease, Department of Medicine, University of California, Irvine, 3205 McGaugh Hall, Irvine, CA 92697-3900. Phone: (949) 824-5781. Fax: (949) 824-9437. E-mail: m.buchmeier@uci.edu
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Snippet Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
The severe acute respiratory syndrome coronavirus (SARS-CoV) generates 16 nonstructural proteins (nsp's) through proteolytic cleavage of a large precursor...
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StartPage 10314
SubjectTerms Amino Acid Sequence
Biological and medical sciences
Blotting, Western
Catalysis
Cell Line
Fundamental and applied biological sciences. Psychology
Humans
Microbiology
Miscellaneous
Mitochondria - metabolism
Molecular Sequence Data
Protein Binding
Protein Structure, Tertiary
Repressor Proteins - chemistry
SARS Virus - metabolism
Signal Transduction
Transcription, Genetic
Viral Nonstructural Proteins - genetics
Viral Nonstructural Proteins - metabolism
Virology
Virus-Cell Interactions
Title Severe Acute Respiratory Syndrome Coronavirus Nonstructural Protein 2 Interacts with a Host Protein Complex Involved in Mitochondrial Biogenesis and Intracellular Signaling
URI http://jvi.asm.org/content/83/19/10314.abstract
https://www.ncbi.nlm.nih.gov/pubmed/19640993
https://www.proquest.com/docview/67638157
https://pubmed.ncbi.nlm.nih.gov/PMC2748024
Volume 83
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