title: Involvement of voltage-dependent anion channel (VDAC) in dengue infection.
abstract: During infection, dengue virus (DENV) proteins interact with host cellular constituents promoting the remodeling of the cell to facilitate virus production. While a number of interacting proteins have been identified for DENV non-structural proteins, far fewer interacting partners have been identified for the DENV structural proteins. One protein that has been identified as a DENV E protein interacting protein is the cellular chaperone GRP78. GRP78 has been shown to have a number of cellular interacting partners including the voltage-dependent anion channel (VDAC). In this study we confirmed the interactions between GRP78 and DENV E protein and between GRP78 and VDAC. VDAC was shown to be re-localized during DENV infection, with no change in levels of protein expression. VDAC is predominantly located on the outer membrane of mitochondria and our result is consistent with movement of the mitochondria towards the ER during DENV infection. Down regulation of VDAC through siRNA significantly reduced DENV protein expression, as well as the percentage infection and output virus titer. Our results suggest that VDAC plays an important role in DENV infection.
authors: Institute of Molecular Biosciences Mahidol University, Salaya Campus, 25/25 Phuttamonthon Sai 4, Salaya, Nakhon Pathom 73170, Thailand.
authors: Kunlakanya
authors: K
authors: Jitobaom
authors: Institute of Molecular Biosciences Mahidol University, Salaya Campus, 25/25 Phuttamonthon Sai 4, Salaya, Nakhon Pathom 73170, Thailand.
authors: Natthida
authors: N
authors: Tongluan
authors: Institute of Molecular Biosciences Mahidol University, Salaya Campus, 25/25 Phuttamonthon Sai 4, Salaya, Nakhon Pathom 73170, Thailand.|Center for Emerging and Neglected Infectious Diseases, Mahidol University, Salaya Campus, 25/25 Phuttamonthon Sai 4, Salaya, Nakhon Pathom 73170, Thailand.
authors: Duncan R
authors: DR
authors: Smith
mesh_terms: D003715:Dengue / Q000378:metabolism* / Q000821:virology; D003716:Dengue Virus / Q000378:metabolism / Q000472:pathogenicity*; D000091342:Endoplasmic Reticulum Chaperone BiP; D057809:HEK293 Cells; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D054884:Host-Pathogen Interactions; D006801:Humans; D034741:RNA, Small Interfering; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism; D050995:Voltage-Dependent Anion Channel 1 / Q000235:genetics / Q000378:metabolism; D050994:Voltage-Dependent Anion Channels / Q000235:genetics / Q000378:metabolism*
chemical_list: C051821:E-glycoprotein, Dengue virus type 2; D000091342:Endoplasmic Reticulum Chaperone BiP; C000717247:HSPA5 protein, human; D006360:Heat-Shock Proteins; D034741:RNA, Small Interfering; C494762:VDAC1 protein, human; D014759:Viral Envelope Proteins; D050994:Voltage-Dependent Anion Channels; C466981:glycoprotein E, dengue virus type 4; D050995:Voltage-Dependent Anion Channel 1