Single point mutation in tick-borne encephalitis virus prM protein induces a reduction of virus particle secretion

1 Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo 060-0818, Japan 2 Laboratory of Anatomy, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo 060-0818, Japan 3 Department of Pathology...

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Published in:Journal of general virology 2004-10, Vol.85 (10), p.3049-3058
Main Authors: Yoshii, Kentarou, Konno, Akihiro, Goto, Akiko, Nio, Junko, Obara, Mayumi, Ueki, Tomotaka, Hayasaka, Daisuke, Mizutani, Tetsuya, Kariwa, Hiroaki, Takashima, Ikuo
Format: Article
Language:English
Subjects:
Animals
Arboviral encephalitis
Arboviroses
Biological and medical sciences
Cell Line
Cricetinae
Encephalitis Viruses, Tick-Borne - physiology
Fundamental and applied biological sciences. Psychology
Human viral diseases
Infectious diseases
Medical sciences
Microbiology
Microscopy, Electron
Miscellaneous
Point Mutation
Tick-borne encephalitis virus
Tropical viral diseases
Viral diseases
Viral Envelope Proteins - genetics
Viral Envelope Proteins - physiology
Virion - physiology
Virology
Virus Assembly
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Summary:1 Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo 060-0818, Japan 2 Laboratory of Anatomy, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo 060-0818, Japan 3 Department of Pathology, Institute of Tropical Medicine, Nagasaki University, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan Correspondence Ikuo Takashima takasima{at}vetmed.hokudai.ac.jp Flaviviruses are assembled to bud into the lumen of the endoplasmic reticulum (ER) and are secreted through the vesicle transport pathway. Virus envelope proteins play important roles in this process. In this study, the effect of mutations in the envelope proteins of tick-borne encephalitis (TBE) virus on secretion of virus-like particles (VLPs), using a recombinant plasmid expression system was analysed. It was found that a single point mutation at position 63 in prM induces a reduction in secretion of VLPs. The mutation in prM did not affect the folding of the envelope proteins, and chaperone-like activity of prM was maintained. As observed by immunofluorescence microscopy, viral envelope proteins with the mutation in prM were scarce in the Golgi complex, and accumulated in the ER. Electron microscopic analysis of cells expressing the mutated prM revealed that many tubular structures were present in the lumen. The insertion of the prM mutation at aa 63 into the viral genome reduced the production of infectious virus particles. This data suggest that prM plays a crucial role in the virus budding process.
ISSN:0022-1317
1465-2099
DOI:10.1099/vir.0.80169-0