Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8751378 | Virology | 2018 | 6 Pages |
Abstract
Zika virus (ZIKV) has been identified as a cause of neurologic diseases in infants and Guillain-Barréâ¯Syndrome, and currently, no therapeutics or vaccines are approved. In this study, we sought to identify potential host proteins interacting with ZIKV particles to gain better insights into viral infectivity. Viral particles were purified through density-gradient centrifugation and subsequently, size-exclusion chromatography (SEC). Mass spectrometric analyses revealed viral envelope protein and HSP70 to comigrate in only one SEC fraction. Neither of these proteins were found in any other SEC fractions. We then performed neutralization assays and found that incubating viral particles with antibody against HSP70 indeed significantly reduced viral infectivity, while HSC70 antibody did not. Preincubating cells with recombinant HSP70 also decreased viral infectivity. Knockdown and inhibition of HSP70 also significantly diminished viral production. These results implicate HSP70 in the pathogenesis of ZIKV and identify HSP70 as a potential host therapeutic target against ZIKV infection.
Keywords
PBSZIKVMTaseNBDRdRpNCRaHIDGCHspSBDSAMDAASECTFAMOIRNA-dependent RNA polymeraseS-adenosyl-L-methionineTrifluoroacetic acidSize-exclusion chromatographysubstrate binding domainnucleotide binding domainDensity-gradient centrifugationnonstructuralMethyltransferasePhosphate-buffered salinedirect acting antiviralNon-coding regionHCVHepatitis C virusZika virusHeat shock proteinmultiplicity of infection
Related Topics
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Immunology and Microbiology
Virology
Authors
Ronik Khachatoorian, Whitaker Cohn, Anthony Buzzanco, Rana Riahi, Vaithilingaraja Arumugaswami, Asim Dasgupta, Julian P. Whitelegge, Samuel W. French,