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Updated: Aug 14, 2026

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly
Published on: March 1, 2012
JC virus agnoprotein colocalizes with tubulin
Shuichi Endo1, Yuki Okada, Yasuko Orba
1Laboratory of Molecular and Cellular Pathology, Hokkaido University School of Medicine, and CREST, Japan Science and Technology, Sapporo, Japan.
Abstract:
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.
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