Association between RABV G Proteins Transported from the Perinuclear Space to the Cell Surface Membrane and N-Glycosylation of the Sequon Asn²⁰⁴ Association between RABV G Proteins Transported from the Perinuclear Space to the Cell Surface Membrane and N-Glycosylation of the Sequon Asn<sup>204</sup>

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Author(s)

    • Hamamoto Noriko Hamamoto Noriko
    • Department of Veterinary Science, National Institute of Infectious Diseases|United Graduate School of Veterinary Science, Gifu University
    • Park Chun-Ho
    • Department of Veterinary Pathology, School of Veterinary Medicine, Kitasato University
    • Noguchi Akira
    • Department of Veterinary Science, National Institute of Infectious Diseases
    • Kaku Yoshihiro
    • Department of Veterinary Science, National Institute of Infectious Diseases
    • Okutani Akiko
    • Department of Veterinary Science, National Institute of Infectious Diseases
    • Morikawa Shigeru
    • Department of Veterinary Science, National Institute of Infectious Diseases|United Graduate School of Veterinary Science, Gifu University
    • Inoue Satoshi
    • Department of Veterinary Science, National Institute of Infectious Diseases|United Graduate School of Veterinary Science, Gifu University

Abstract

In this study, G proteins of the rabies virus (RABV) Kyoto strain were detected in the cytoplasm but not distributed at the cell membrane of mouse neuroblastoma (MNA) cells. G proteins of CVS-26 were detected in both the cell membrane and perinuclear space of MNA cells. We found that N-glycosylation of street RABV G protein by the insertion of the sequon Asn<sup>204</sup> induced the transfer of RABV G proteins to the cell surface membrane. Fixed RABV budding from the plasma membrane has been found to depend not only on G protein but also on other structural proteins such as M protein. However, the differing N-glycosylation of G protein could be associated with the distinct budding and antigenic features of RABV in street and fixed viruses. Our study of the association of N-glycan of G protein at Asn<sup>204</sup> with the transport of RABV G protein to the cell surface membrane contributes to the understanding of the evolution of fixed virus from street virus, which in turn would help for determine the mechanism underlying RABV budding and enhanced host immune responses.

Journal

  • Japanese Journal of Infectious Diseases

    Japanese Journal of Infectious Diseases 68(5), 387-393, 2015

    National Institute of Infectious Diseases, Japanese Journal of Infectious Diseases Editorial Committee

Codes

  • NII Article ID (NAID)
    130005098925
  • NII NACSIS-CAT ID (NCID)
    AA1132885X
  • Text Lang
    ENG
  • ISSN
    1344-6304
  • NDL Article ID
    026764280
  • NDL Call No.
    Z53-C450
  • Data Source
    NDL  J-STAGE 
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