Interaction of Tsg101 with Marburg Virus VP40 Depends on the PPPY Motif, but Not the PT/SAP Motif as in the Case of Ebola Virus, and Tsg101 Plays a Critical Role in the Budding of Marburg Virus-Like Particles Induced by VP40, NP, and GP

Author:

Urata Shuzo123,Noda Takeshi24,Kawaoka Yoshihiro245,Morikawa Shigeru6,Yokosawa Hideyoshi3,Yasuda Jiro12

Affiliation:

1. First Department of Forensic Science, National Research Institute of Police Science, Kashiwa 277-0882, Japan

2. CREST, Japan Science and Technology Agency, Saitama 332-0012, Japan

3. Department of Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan

4. International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan

5. Department of Pathological Sciences, School of Veterinary Medicine, University of Wisconsin—Madison, Madison, Wisconsin 53706

6. Special Pathogens Laboratory, Department of Virology 1, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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