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Journal of Virology, October 2009, p. 10314-10318, Vol. 83, No. 19
0022-538X/09/$08.00+0 doi:10.1128/JVI.00842-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

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 92697-39004
Received 24 April 2009/ Accepted 21 July 2009
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.
Published ahead of print on 29 July 2009.
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