HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Yoshii, K. Articles by Takashima, I. Search for Related Content PubMed PubMed Citation Articles by Yoshii, K. Articles by Takashima, I. Agricola Articles by Yoshii, K. Articles by Takashima, I.

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, 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.

This article has been cited by other articles:

				M. Panyasrivanit, A. Khakpoor, N. Wikan, and D. R. Smith Co-localization of constituents of the dengue virus translation and replication machinery with amphisomes J. Gen. Virol., February 1, 2009; 90(2): 448 - 456. [Abstract] [Full Text] [PDF]

				J. Junjhon, M. Lausumpao, S. Supasa, S. Noisakran, A. Songjaeng, P. Saraithong, K. Chaichoun, U. Utaipat, P. Keelapang, A. Kanjanahaluethai, et al. Differential Modulation of prM Cleavage, Extracellular Particle Distribution, and Virus Infectivity by Conserved Residues at Nonfurin Consensus Positions of the Dengue Virus pr-M Junction J. Virol., November 1, 2008; 82(21): 10776 - 10791. [Abstract] [Full Text] [PDF]

				K. Yoshii, A. Goto, K. Kawakami, H. Kariwa, and I. Takashima Construction and application of chimeric virus-like particles of tick-borne encephalitis virus and mosquito-borne Japanese encephalitis virus J. Gen. Virol., January 1, 2008; 89(1): 200 - 211. [Abstract] [Full Text] [PDF]

				Z. Zhao, T. Date, Y. Li, T. Kato, M. Miyamoto, K. Yasui, and T. Wakita Characterization of the E-138 (Glu/Lys) mutation in Japanese encephalitis virus by using a stable, full-length, infectious cDNA clone J. Gen. Virol., August 1, 2005; 86(8): 2209 - 2220. [Abstract] [Full Text] [PDF]