MISC

査読有り
1993年11月

PROTEOLYTIC PROCESSING AND MEMBRANE ASSOCIATION OF PUTATIVE NONSTRUCTURAL PROTEINS OF HEPATITIS-C VIRUS

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
  • M HIJIKATA
  • ,
  • H MIZUSHIMA
  • ,
  • Y TANJI
  • ,
  • Y KOMODA
  • ,
  • Y HIROWATARI
  • ,
  • T AKAGI
  • ,
  • N KATO
  • ,
  • K KIMURA
  • ,
  • K SHIMOTOHNO

90
22
開始ページ
10773
終了ページ
10777
記述言語
英語
掲載種別
DOI
10.1073/pnas.90.22.10773
出版者・発行元
NATL ACAD SCIENCES

By using a plasmid-based transient protein expression system in cultured cells and an in vitro transcription/translation system, we analyzed the proteolytic processing of the putative nonstructural protein region of the precursor polyprotein from a Japanese type of hepatitis C virus. In addition to the previously reported viral proteins, p21 and p70, we identified products of 4 kDa (p4), 27 kDa (p27), 56 kDa (p56), 58 kDa (p58), and 66 kDa (p66). These products were produced in a viral serine proteinase (proteinase 2)-dependent manner from the region downstream of p70 in the precursor polyprotein and were arranged as NH2-p70-p4-p27-p58(p56)-p66-COOH as determined with region-specific antibodies. We showed that p56 was an N-terminally truncated form of p58, which suggested that a small polypeptide of 2 kDa (p2) was produced from the N-terminal part of p58. Cleavage between p4 and p27 was inefficient in vitro and we saw the 31-kDa precursor polypeptide (p31) accumulate. Furthermore, efficient cleavage at this site in vivo required the presence of p58/p56. Immunoprecipitation analysis in vitro also suggested the mutual interaction of those nonstructural protein products. An especially close association of p4 with p70 may contribute to association of p70 with microsomal membranes.

リンク情報
DOI
https://doi.org/10.1073/pnas.90.22.10773
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:A1993MH32200075&DestApp=WOS_CPL
ID情報
  • DOI : 10.1073/pnas.90.22.10773
  • ISSN : 0027-8424
  • Web of Science ID : WOS:A1993MH32200075

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