Previous Article | Next Article ![]()
Journal of Virology, May 2007, p. 4895-4899, Vol. 81, No. 9
0022-538X/07/$08.00+0 doi:10.1128/JVI.02829-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

First Department of Forensic Science, National Research Institute of Police Science, Kashiwa 277-0882, Japan,1 CREST, Japan Science and Technology Agency, Saitama 332-0012, Japan,2 Department of Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan,3 International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan,4 Department of Pathological Sciences, School of Veterinary Medicine, University of WisconsinMadison, Madison, Wisconsin 53706,5 Special Pathogens Laboratory, Department of Virology 1, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan6
Received 21 December 2006/ Accepted 29 January 2007
Marburg virus (MARV) VP40 is a matrix protein that can be released from mammalian cells in the form of virus-like particles (VLPs) and contains the PPPY sequence, which is an L-domain motif. Here, we demonstrate that the PPPY motif is important for VP40-induced VLP budding and that VLP production is significantly enhanced by coexpression of NP and GP. We show that Tsg101 interacts with VP40 depending on the presence of the PPPY motif, but not the PT/SAP motif as in the case of Ebola virus, and plays an important role in VLP budding. These findings provide new insights into the mechanism of MARV budding.
Published ahead of print on 14 February 2007.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»