Oligomerization of neutral peptides derived from the JC virus agnoprotein through a cysteine residue.
作者： Koushi Hidaka , Keiko Hojo , Shio Fujioka , Souichi Nukuzuma , Yuko Tsuda
DOI: 10.1007/S00726-015-2004-3
关键词:
摘要: The JC virus is the causative agent of progressive multifocal leukoencephalopathy. viral genome encodes a multifunctional protein known as agnoprotein which essential for proliferation and reported to possess oligomerization sequence. However, structural relationship with unclear. We synthesized 23 amino acid residue neutral peptides derived from agnoprotein, Lys22 Asp44. secondary structures these were β-sheet in aqueous buffer that converted helical structure hydrophobic environment. These interestingly formed dimers oligomers under oxidizing conditions. was facilitated by addition bismaleimides derivative without thiol group did not form such oligomers. results suggest Agno(22–44) could be transmembrane one disulfide bond between Cys40 triggers oligomerization.
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A. Sami Saribas, Buenafe T. Arachea, Martyn K. White, Ronald E. Viola, Mahmut Safak, Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function. Virology. ,vol. 420, pp. 51- 65 ,(2011) , 10.1016/J.VIROL.2011.08.015
A. Sami Saribas, Martyn K. White, Mahmut Safak, JC virus agnoprotein enhances large T antigen binding to the origin of viral DNA replication: evidence for its involvement in viral DNA replication. Virology. ,vol. 433, pp. 12- 26 ,(2012) , 10.1016/J.VIROL.2012.06.017
Onder Otlu, Francesca Isabella De Simone, Yolanda-Lopez Otalora, Kamel Khalili, Ilker Kudret Sariyer, The agnoprotein of polyomavirus JC is released by infected cells: Evidence for Its cellular uptake by uninfected neighboring cells Virology. ,vol. 468-470, pp. 88- 95 ,(2014) , 10.1016/J.VIROL.2014.07.054
Ambrish Roy, Alper Kucukural, Yang Zhang, I-TASSER: a unified platform for automated protein structure and function prediction Nature Protocols. ,vol. 5, pp. 725- 738 ,(2010) , 10.1038/NPROT.2010.5
P. Coric, A. S. Saribas, M. Abou-Gharbia, W. Childers, M. K. White, S. Bouaziz, M. Safak, Nuclear Magnetic Resonance Structure Revealed that the Human Polyomavirus JC Virus Agnoprotein Contains an α-Helix Encompassing the Leu/Ile/Phe-Rich Domain Journal of Virology. ,vol. 88, pp. 6556- 6575 ,(2014) , 10.1128/JVI.00146-14
Tamotsu Zako, Masafumi Sakono, Naomi Hashimoto, Masaki Ihara, Mizuo Maeda, Bovine Insulin Filaments Induced by Reducing Disulfide Bonds Show a Different Morphology, Secondary Structure, and Cell Toxicity from Intact Insulin Amyloid Fibrils Biophysical Journal. ,vol. 96, pp. 3331- 3340 ,(2009) , 10.1016/J.BPJ.2008.12.3957
Ilker K Sariyer, Abdullah S Saribas, Martyn K White, Mahmut Safak, None, Infection by agnoprotein-negative mutants of polyomavirus JC and SV40 results in the release of virions that are mostly deficient in DNA content Virology Journal. ,vol. 8, pp. 255- 255 ,(2011) , 10.1186/1743-422X-8-255
Gunhild Unterstab, Rainer Gosert, David Leuenberger, Pascal Lorentz, Christine H. Rinaldo, Hans H. Hirsch, The polyomavirus BK agnoprotein co-localizes with lipid droplets. Virology. ,vol. 399, pp. 322- 331 ,(2010) , 10.1016/J.VIROL.2010.01.011
Simona Tomaselli, Veronica Esposito, Paolo Vangone, Nico A. J. van Nuland, Alexandre M. J. J. Bonvin, Remo Guerrini, Teodorico Tancredi, Piero A. Temussi, Delia Picone, The α‐to‐β Conformational Transition of Alzheimer's Aβ‐(1–42) Peptide in Aqueous Media is Reversible: A Step by Step Conformational Analysis Suggests the Location of β Conformation Seeding ChemBioChem. ,vol. 7, pp. 257- 267 ,(2006) , 10.1002/CBIC.200500223
T. Suzuki, Y. Orba, Y. Makino, Y. Okada, Y. Sunden, H. Hasegawa, W. W. Hall, H. Sawa, Viroporin activity of the JC polyomavirus is regulated by interactions with the adaptor protein complex 3 Proceedings of the National Academy of Sciences of the United States of America. ,vol. 110, pp. 18668- 18673 ,(2013) , 10.1073/PNAS.1311457110