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JC virus agnoprotein colocalizes with tubulin
Authors:Endo  Shuichi  Okada  Yuki  Orba  Yasuko  Nishihara  Hiroshi  Tanaka  Shinya  Nagashima  Kazuo  Sawa  Hirofumi
Affiliation:1.Laboratory of Molecular and Cellular Pathology,Hokkaido University School of Medicine,Sapporo,Japan;2.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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