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Viral Protein 1 (VP1), also known as Major Capsid Protein VP1, is the main component of the polyomavirus capsid. 360 VP1 molecules are organized in 72 pentamers to form the capsid. This protein also contains large unique regions that might be responsible for the characteristic properties observed in the Reoviridae family (such as rotavirus). Polyomaviruses have from five to seven proteins, including three capsid proteins, VP1, VP2, and VP3, and two proteins, T and t, which are involved in DNA replication. ==History== Dr. Sarah Stewart and Dr. Bernice E. Eddy were the first ones to describe the polyoma virus. "Polyoma" is a word derived from the Greek roots "poly-", meaning many or much, and "-oma", meaning tumors. Until 2000 d.C, polyomaviruses were taxonomically classified as a genus in the family papovaviridae. With the publication of the Seventh Report of the International Committee on Taxonomy of Viruses, papovaviridae was split into two new families, papillomaviridae and polyomaviridae. Here we see some differences between them.〔(Polyomaviridae )〕 The major polyoma virus capsid protein,VP1, has been cloned in ''Escherichia coli''. Under the inducible control of the hybrid tac promoter, VP1 constituted between 2 and 3% of the total host cell protein. The expressed VP, was purified to near homogeneity with initial yields to 10%. Optimal expression was temperature-dependent, and significant intracellular degradation could be demonstrated. The final product was obtained as one predominant isoelectric focusing species, without the pattern of post-translational modification seen in virus-infected eukaryotic cells. The purified VP1 from E. coli will be useful as a substrate for the purification of VP1 modification enzymes and in the study of inter-VP1 oligomerization. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Polyomavirus capsid protein (VP1)」の詳細全文を読む スポンサード リンク
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