Involvement of ATP synthase β subunit in chikungunya virus entry into insect cells

Chikungunya virus (CHIKV), the virus responsible for the disease chikungunya fever in humans, is transmitted by Aedes mosquitoes. While significant progress has been made in understanding the process by which CHIKV enters into mammalian cells, far less progress has been made in understanding the CHI...

Full description

Saved in:
Bibliographic Details
Published inArchives of virology Vol. 159; no. 12; pp. 3353 - 3364
Main Authors Fongsaran, Chanida, Jirakanwisal, Krit, Kuadkitkan, Atichat, Wikan, Nitwara, Wintachai, Phitchayapak, Thepparit, Chutima, Ubol, Sukathida, Phaonakrop, Narumon, Roytrakul, Sittiruk, Smith, Duncan R
Format Journal Article
LanguageEnglish
Published Vienna Springer-Verlag 01.12.2014
Springer Vienna
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Chikungunya virus (CHIKV), the virus responsible for the disease chikungunya fever in humans, is transmitted by Aedes mosquitoes. While significant progress has been made in understanding the process by which CHIKV enters into mammalian cells, far less progress has been made in understanding the CHIKV entry process in insect cells. This study sought to identify mosquito-cell-expressed CHIKV-binding proteins through a combination of virus overlay protein binding assays (VOPBA) and mass spectroscopy. A 50-kDa CHIKV-binding protein was identified as the ATP synthase β subunit (ATPSβ). Co-immunoprecipitation studies confirmed the interaction, and colocalization analysis showed cell-surface and intracellular co-localization between CHIKV and ATPSβ. Both antibody inhibition and siRNA-mediated downregulation experiments targeted to ATPSβ showed a significant reduction in viral entry and virus production. These results suggest that ATPSβ is a CHIKV-binding protein capable of mediating the entry of CHIKV into insect cells.
Bibliography:http://dx.doi.org/10.1007/s00705-014-2210-4
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0304-8608
1432-8798
DOI:10.1007/s00705-014-2210-4