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Journal of Virology, July 2009, p. 6952-6956, Vol. 83, No. 13
0022-538X/09/$08.00+0 doi:10.1128/JVI.00480-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
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Mayumi Matsuoka,2,3,
Tsung-Hsien Chang,3
Mike Bray,4
Steven Jones,5
Masato Tashiro,1
Atsushi Kato,1 and
Keiko Ozato3
Department of Virology III,1 Department of Bacterial Pathogenesis and Infection Control, National Institute of Infectious Diseases, Tokyo 208-0011, Japan,2 Laboratory of Molecular Growth Regulation, Genomics of Differentiation Program, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-2753,3 Integrated Research Facility, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892,4 Population and Public Health Branch, National Microbiology Laboratory, Canadian Science Centre for Human and Animal Health, Manitoba R3E 3R2, Canada5
Received 6 March 2009/ Accepted 20 April 2009
The viral protein VP35 of ebolavirus (EBOV) is implicated to have diverse roles in the viral life cycle. We employed a yeast two-hybrid screen to search for VP35 binding partners and identified the cytoplasmic dynein light chain (DLC8) as a protein that interacts with VP35. Mapping analysis unraveled a consensus motif, SQTQT, within VP35 through which VP35 binds to DLC8. The disruption of DLC8 binding does not affect the ability of VP35 to inhibit type I IFN production. Given that VP35 from various EBOV species interacts with DLC8, this interaction may have a role in regulating the EBOV life cycle.
T.K. and M.M. contributed equally to this study.
Published ahead of print on 29 April 2009.
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