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


     

J Gen Virol 87 (2006), 363-368; DOI 10.1099/vir.0.81456-0

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kaiser, W. J.
Right arrow Articles by Goodfellow, I. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kaiser, W. J.
Right arrow Articles by Goodfellow, I. G.
Agricola
Right arrow Articles by Kaiser, W. J.
Right arrow Articles by Goodfellow, I. G.
© 2006 Society for General Microbiology

Short Communication

Analysis of protein–protein interactions in the feline calicivirus replication complex

William J. Kaiser1, Yasmin Chaudhry1, Stanislav V. Sosnovtsev2 and Ian G. Goodfellow1,{dagger}

1 School of Biological Sciences, University of Reading, Whiteknights, Reading RG6 6AJ, UK
2 Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA

Correspondence
Ian G. Goodfellow
I.Goodfellow{at}ic.ac.uk

Caliciviruses are a major cause of gastroenteritis in humans and cause a wide variety of other diseases in animals. Here, the characterization of protein–protein interactions between the individual proteins of Feline calicivirus (FCV), a model system for other members of the family Caliciviridae, is reported. Using the yeast two-hybrid system combined with a number of other approaches, it is demonstrated that the p32 protein (the picornavirus 2B analogue) of FCV interacts with p39 (2C), p30 (3A) and p76 (3CD). The FCV protease/RNA polymerase (ProPol) p76 was found to form homo-oligomers, as well as to interact with VPg and ORF2, the region encoding the major capsid protein VP1. A weak interaction was also observed between p76 and the minor capsid protein encoded by ORF3 (VP2). ORF2 protein was found to interact with VPg, p76 and VP2. The potential roles of the interactions in calicivirus replication are discussed.

{dagger}Present address: Department of Virology, Faculty of Medicine, Imperial College London, St Mary's Campus, Norfolk Place, London W2 1PG, UK.




This article has been cited by other articles:


Home page
 J. Gen. Virol.Home page
M. Hogbom, K. Jager, I. Robel, T. Unge, and J. Rohayem
The active form of the norovirus RNA-dependent RNA polymerase is a homodimer with cooperative activity
J. Gen. Virol., February 1, 2009; 90(2): 281 - 291.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
G. Liu, Z. Ni, T. Yun, B. Yu, L. Chen, W. Zhao, J. Hua, and J. Chen
A DNA-launched reverse genetics system for rabbit hemorrhagic disease virus reveals that the VP2 protein is not essential for virus infectivity
J. Gen. Virol., December 1, 2008; 89(12): 3080 - 3085.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
S. V. Sosnovtsev, G. Belliot, K.-O. Chang, V. G. Prikhodko, L. B. Thackray, C. E. Wobus, S. M. Karst, H. W. Virgin, and K. Y. Green
Cleavage map and proteolytic processing of the murine norovirus nonstructural polyprotein in infected cells.
J. Virol., August 1, 2006; 80(16): 7816 - 7831.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2006 by the Society for General Microbiology.