J Gen Virol Email Content Delivery
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


Published online ahead of print on 2 September 2009 as doi:10.1099/vir.0.012112-0
Journal of General Virology 2009;90:3042.

A more recent version of this article appeared on December 1, 2009 J Gen Virol (2009), DOI 10.1099/vir.0.012112-0
© 2009 Society for General Microbiology

This Article
Right arrow Full Text (Papers in Press[PDF])
Right arrow All Versions of this Article:
vir.0.012112-0v1
90/12/3042    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Google Scholar
Right arrow Articles by Zhang, X.
Right arrow Articles by Wong, S.-M.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhang, X.
Right arrow Articles by Wong, S.-M.
Agricola
Right arrow Articles by Zhang, X.
Right arrow Articles by Wong, S.-M.

Hibiscus chlorotic ringspot virus upregulates plant sulfite oxidase transcripts and increases sulfate levels in kenaf (Hibiscus cannabinus L.)

Xin Zhang and Sek-Man Wong1

National University of Singapore

1 E-mail: dbswsm{at}nus.edu.sg

Hibiscus chlorotic ringspot virus (HCRSV) coat protein (CP) is required for encapsidation and viral systemic movement. To better understand the roles of HCRSV CP in viral infection and its interactions with host proteins, a cDNA library of kenaf (Hibiscus cannabinus L.) was constructed and screened using a yeast two-hybrid system (YTHS) to identify CP-interacting proteins. One protein identified was sulfite oxidase (SO) and the interaction was confirmed in vitro and in vivo. The interaction was found to be associated with peroxisomes by immunofluorescent labeling of peroxisomes by anti-SKL signal peptide antibody. Our results showed that only the P and S domains of CP interacted with SO from kenaf (HcSO) by YTHS. This is probably due to the exposure of these two domains on the outer surface of the capsid. Peroxisomes were observed to aggregate in HCRSV infected cells, and biochemical assays of the total protein from kenaf leaf extracts showed that SO activity and SO-dependent H2O2-generating activity in the HCRSV-infected leaves increased compared to the mock-inoculated kenaf plants.

Received 23 March 2009; accepted 1 September 2009.





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2009 by the Society for General Microbiology.