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Severe acute respiratory syndrome coronavirus nonstructural protein 2 interacts with a host protein complex involved in mitochondrial biogenesis and intracellular signaling

Academic Article
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Overview

authors

  • Cornillez-Ty, C. T.
  • Liao, L. J.
  • Yates III, John
  • Kuhn, Peter
  • Buchmeier, M. J.

publication date

  • October 2009

journal

  • Journal of Virology  Journal

abstract

  • 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.

subject areas

  • Amino Acid Sequence
  • Blotting, Western
  • Catalysis
  • Cell Line
  • Humans
  • Mitochondria
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Tertiary
  • Repressor Proteins
  • SARS Virus
  • Signal Transduction
  • Transcription, Genetic
  • Viral Nonstructural Proteins
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Identity

PubMed Central ID

  • PMC2748024

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.00842-09

PubMed ID

  • 19640993
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Additional Document Info

start page

  • 10314

end page

  • 10318

volume

  • 83

issue

  • 19

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