Association between RABV G Proteins Transported from the Perinuclear Space to the Cell Surface Membrane and N-Glycosylation of the Sequon Asn²⁰⁴

• Hamamoto Noriko

  Department of Veterinary Science, National Institute of Infectious Diseases United Graduate School of Veterinary Science, Gifu University

• Uda Akihiko

  Department of Veterinary Science, National Institute of Infectious Diseases

• Tobiume Minoru

  Department of Pathology, National Institute of Infectious Diseases

• 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

書誌事項

タイトル別名

• Association between RABV G Proteins Transported from the Perinuclear Space to the Cell Surface Membrane and N-Glycosylation of the Sequon Asn²⁰⁴

抄録

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 Asn²⁰⁴ 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 Asn²⁰⁴ 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.

収録刊行物

• Japanese Journal of Infectious Diseases

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

  国立感染症研究所 Japanese Journal of Infectious Diseases 編集委員会

キーワード

• rabies virus
• G protein
• N-glycosylation
• street virus
• fixed virus

詳細情報

• CRID: 1390001206240907264
• NII論文ID: 130005098925
• NII書誌ID: AA1132885X
• DOI: 10.7883/yoken.jjid.2014.533
• ISSN: 18842836
• ISSN: 13446304
• NDL書誌ID: 026764280
• PubMed: 25766612
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I026764280
• Web Site: https://www.jstage.jst.go.jp/article/yoken/68/5/68_JJID.2014.533/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2016248578
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可