期刊
MICROBES AND INFECTION
卷 15, 期 4, 页码 310-318出版社
ELSEVIER
DOI: 10.1016/j.micinf.2013.01.004
关键词
Dengue virus; ECV304 cells; VOPBA; EDIII protein; Actin
资金
- National Natural Science Foundation of China [31070811, 31200133]
- New Drug Development Project of China [2012ZX09103301-038]
- Natural Science Foundation of Chongqing City (CSTC) [2009BB5015]
Characterization of the primary host factors associated with host-virus interaction is critical for understanding how a virus infects its host cell. In this study, a modified virus overlay protein binding assay was developed. Host factors with 34, 43, and 55 kDa proteins, which could interact with EDIII, a cell receptor-binding domain of Dengue virus (DENV)-enveloped E protein, were isolated from ECV304 cells. Mass spectrometry identified peptide masses of 43 kDa protein matched to actin, a cytoskeleton protein in eukaryotic cells. The interaction between 43 kDa actin and DENV-2 EDIII was further confirmed by competitive blocking and co-immunoprecipitation assays. Actin cytoskeleton rearrangement was observed within 1 h p.i. of DENV-2-infected ECV304 cells in the confocal immunofluorescent assay. The co-localization of DENV-2 E protein with the actin filaments occurred in the late stage of the DENV replication cycle. Finally, a docking complex was constructed, and the functional residues involved in the interaction of actin and DENV-2 EDIII protein were predicted. Our findings suggest that the direct contact of DENY E protein with 43 kDa actin protein may have a crucial function in DENY infection of ECV304 cells. (C) 2013 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.
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