JC virus agnoprotein colocalizes with tubulin

Shuichi Endo, Yuki Okada, Yasuko Orba, Hiroshi Nishihara, Shinya Tanaka, Kazuo Nagashima, Hirofumi Sawa

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)


The human polyomavirus JC (JCV) encodes an agnoprotein that consists of 71 amino acid residues, with a molecular weight of approximately 8 kDa, from the late protein coding region. The agnoprotein of JCV shares 50% to 60% homology with those of simian virus 40 (SV40) and BK virus (BKV), and the carboxyl-terminal region of JCV agnoprotein is relatively unique. By using specific antibody to the carboxyl-terminal region of JCV agnoprotein, the authors have demonstrated that JCV agnoprotein expressed in the JCV-infected cells, where it localized predominantly in the perinuclear region of the cytoplasm, and colocalizes with the cellular cytoskeletal protein, tubulin. The results suggest that JCV agnoprotein may play a role in the stability of microtubules and the preservation of JCV infected cells via an interaction with tubulin.

Original languageEnglish
Pages (from-to)10-14
Number of pages5
JournalJournal of NeuroVirology
Issue numberSUPPL. 1
Publication statusPublished - 2003
Externally publishedYes


  • Agnoprotein
  • JC virus
  • Tubulin

ASJC Scopus subject areas

  • Neurology
  • Clinical Neurology
  • Cellular and Molecular Neuroscience
  • Virology


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