Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jprot.2012.05.047
Title: Molecular and enzymatic characterization of XMRV protease by a cell-free proteolytic analysis
Authors: Matsunaga, S.
Sawasaki, T.
Ode, H.
Morishita, R.
Furukawa, A.
Sakuma, R.
Sugiura, W.
Sato, H.
Katahira, M.
Takaori-Kondo, A.
Yamamoto, N. 
Ryo, A.
Keywords: AlphaSceen
Cell-free protein synthesis
Protease
XMRV
Issue Date: 3-Aug-2012
Citation: Matsunaga, S., Sawasaki, T., Ode, H., Morishita, R., Furukawa, A., Sakuma, R., Sugiura, W., Sato, H., Katahira, M., Takaori-Kondo, A., Yamamoto, N., Ryo, A. (2012-08-03). Molecular and enzymatic characterization of XMRV protease by a cell-free proteolytic analysis. Journal of Proteomics 75 (15) : 4863-4873. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jprot.2012.05.047
Abstract: Xenotropic murine leukemia virus-related virus (XMRV) is a virus generated under artificial conditions by the recombination of 2 murine leukemia virus (MLV) proviruses, PreXMRV-1 and PreXMRV-2, during the in vivo passage of human prostate cancer cells in athymic nude mice. The molecular etiology of XMRV infection has not been characterized and its implication in human prostate cancer progression remains equivocal. As a step toward resolving this issue we developed an in vitro enzymatic assay system to characterize XMRV protease (PR)-mediated cleavage of host-cell proteins. Enzymatically-active XMRV PR protein was synthesized using a wheat-germ cell-free system. By monitoring cleavage activity of XMRV PR by AlphaScreen and 2-color immunoblot analyses, we revealed that the catalytic activity of XMRV PR is selectively blocked by the HIV PR inhibitor, Amprenavir, and identified several human tumor suppressor proteins, including PTEN and BAX, to be substrates of XMRV PR. This system may provide an attractive means for analyzing the function of retrovirus proteases and provide a technology platform for drug screening. © 2012 Elsevier B.V.
Source Title: Journal of Proteomics
URI: http://scholarbank.nus.edu.sg/handle/10635/126737
ISSN: 18743919
DOI: 10.1016/j.jprot.2012.05.047
Appears in Collections:Staff Publications

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

SCOPUSTM   
Citations

2
checked on Jul 14, 2018

WEB OF SCIENCETM
Citations

1
checked on Jul 4, 2018

Page view(s)

10
checked on Jun 28, 2018

Google ScholarTM

Check

Altmetric


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