Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.virol.2009.11.028
DC FieldValue
dc.titlePorcine circovirus type 2 ORF3 protein competes with p53 in binding to Pirh2 and mediates the deregulation of p53 homeostasis
dc.contributor.authorKaruppannan, A.K.
dc.contributor.authorLiu, S.
dc.contributor.authorJia, Q.
dc.contributor.authorSelvaraj, M.
dc.contributor.authorKwang, J.
dc.date.accessioned2011-07-26T07:05:39Z
dc.date.available2011-07-26T07:05:39Z
dc.date.issued2010
dc.identifier.citationKaruppannan, A.K., Liu, S., Jia, Q., Selvaraj, M., Kwang, J. (2010). Porcine circovirus type 2 ORF3 protein competes with p53 in binding to Pirh2 and mediates the deregulation of p53 homeostasis. Virology 398 (1) : 1-11. ScholarBank@NUS Repository. https://doi.org/10.1016/j.virol.2009.11.028
dc.identifier.issn00426822
dc.identifier.issn10960341
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/24867
dc.description.abstractThe ORF3 protein of porcine circovirus type 2 (PCV2) causes apoptosis in virus-infected cells and is not essential for virus replication. The ORF3 protein plays an important role in the pathogenesis of the PCV2 infection in mouse models and SPF piglets. The ORF3 protein interacts with the porcine homologue of Pirh2 (pPirh2), a p53-induced ubiquitin-protein E3 ligase, which regulates p53 ubiquitination. Here, we present our study analyzing the details of the molecular interaction between these three factors. Our experiments, in vitro and in vivo, show that ORF3 protein competes with p53 in binding to pPirh2. The amino acid residues 20 to 65 of the ORF3 protein are essential in this competitive interaction of ORF3 protein with pPirh2 over p53. The interaction of ORF3 protein with pPirh2 also leads to an alteration in the physiological cellular localization of pPirh2 and a significant reduction in the stability of pPirh2. These events contribute to the deregulation of p53 by pPirh2, leading to increased p53 levels and apoptosis of the infected cells. © 2009 Elsevier Inc. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.virol.2009.11.028
dc.sourceScopus
dc.subjectCompetitive interaction
dc.subjectORF3
dc.subjectp53
dc.subjectPCV2
dc.subjectPirh2
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1016/j.virol.2009.11.028
dc.description.sourcetitleVirology
dc.description.volume398
dc.description.issue1
dc.description.page1-11
dc.identifier.isiut000274669100001
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

22
checked on Jul 12, 2019

WEB OF SCIENCETM
Citations

20
checked on Jul 12, 2019

Page view(s)

213
checked on Jul 5, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.