Cysteine Residues in the Major Capsid Protein, Vp1, of the JC Virus Are Important for Protein Stability and Oligomer Formation

Author:

Kobayashi Shintaro,Suzuki Tadaki,Igarashi Manabu,Orba Yasuko,Ohtake Noriko,Nagakawa Keita,Niikura Kenichi,Kimura Takashi,Kasamatsu Harumi,Sawa Hirofumi

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

Reference29 articles.

1. Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry;XS Chen;EMBO J,1998

2. Self-assembly of the JC virus major capsid protein, VP1, expressed in insect cells;D Chang;J Gen Virol 78 (Pt,1997

3. Disulfide bonds stabilize JC virus capsid-like structure by protecting calcium ions from chelation;PL Chen;FEBS Lett,2001

4. The major capsid protein, VP1, of human JC virus expressed in Escherichia coli is able to self-assemble into a capsid-like particle and deliver exogenous DNA into human kidney cells;WC Ou;J Gen Virol 80 (Pt,1999

5. Structure-function analysis of the human JC polyomavirus establishes the LSTc pentasaccharide as a functional receptor motif;U Neu;Cell Host Microbe,2010

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