Molecular Determinants for Subcellular Localization of Hepatitis C Virus Core Protein

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Published inJournal of Virology Vol. 79; no. 2; pp. 1271 - 1281
Main Authors SUZUKI, Ryosuke, SAKAMOTO, Shinichiro, MIYAMURA, Tatsuo, SUZUKI, Tetsuro, TSUTSUMI, Takeya, RIKIMARU, Akiko, TANAKA, Keiko, SHIMOIKE, Takashi, MORIISHI, Kohji, IWASAKI, Takuya, MIZUMOTO, Kiyohisa, MATSUURA, Yoshiharu
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.01.2005
Subjects
Amino Acid Sequence
Biological and medical sciences
Cell Line
Cell Nucleus - chemistry
Endoplasmic Reticulum - chemistry
Fundamental and applied biological sciences. Psychology
Hepacivirus - chemistry
Hepatitis C virus
Humans
Karyopherins - physiology
Microbiology
Miscellaneous
Mitochondria - chemistry
Molecular Sequence Data
Nuclear Localization Signals
Viral Core Proteins - analysis
Viral Core Proteins - chemistry
Virology
Virus
Microbiology
Flaviviridae
Localization
Hepatitis C virus
Hepacivirus
Protein
Virology
Online AccessGet full text

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Abstract Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
AbstractList Hepatitis C virus (HCV) core protein is a putative nucleocapsid protein with a number of regulatory functions. In tissue culture cells, HCV core protein is mainly located at the endoplasmic reticulum as well as mitochondria and lipid droplets within the cytoplasm. However, it is also detected in the nucleus in some cells. To elucidate the mechanisms by which cellular trafficking of the protein is controlled, we performed subcellular fractionation experiments and used confocal microscopy to examine the distribution of heterologously expressed fusion proteins involving various deletions and point mutations of the HCV core combined with green fluorescent proteins. We demonstrated that a region spanning amino acids 112 to 152 can mediate association of the core protein not only with the ER but also with the mitochondrial outer membrane. This region contains an 18-amino-acid motif which is predicted to form an amphipathic α-helix structure. With regard to the nuclear targeting of the core protein, we identified a novel bipartite nuclear localization signal, which requires two out of three basic-residue clusters for efficient nuclear translocation, possibly by occupying binding sites on importin-α. Differences in the cellular trafficking of HCV core protein, achieved and maintained by multiple targeting functions as mentioned above, may in part regulate the diverse range of biological roles of the core protein.
Hepatitis C virus (HCV) core protein is a putative nucleocapsid protein with a number of regulatory functions. In tissue culture cells, HCV core protein is mainly located at the endoplasmic reticulum as well as mitochondria and lipid droplets within the cytoplasm. However, it is also detected in the nucleus in some cells. To elucidate the mechanisms by which cellular trafficking of the protein is controlled, we performed subcellular fractionation experiments and used confocal microscopy to examine the distribution of heterologously expressed fusion proteins involving various deletions and point mutations of the HCV core combined with green fluorescent proteins. We demonstrated that a region spanning amino acids 112 to 152 can mediate association of the core protein not only with the ER but also with the mitochondrial outer membrane. This region contains an 18-amino-acid motif which is predicted to form an amphipathic alpha -helix structure. With regard to the nuclear targeting of the core protein, we identified a novel bipartite nuclear localization signal, which requires two out of three basic-residue clusters for efficient nuclear translocation, possibly by occupying binding sites on importin- alpha . Differences in the cellular trafficking of HCV core protein, achieved and maintained by multiple targeting functions as mentioned above, may in part regulate the diverse range of biological roles of the core protein.
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
ABSTRACT Hepatitis C virus (HCV) core protein is a putative nucleocapsid protein with a number of regulatory functions. In tissue culture cells, HCV core protein is mainly located at the endoplasmic reticulum as well as mitochondria and lipid droplets within the cytoplasm. However, it is also detected in the nucleus in some cells. To elucidate the mechanisms by which cellular trafficking of the protein is controlled, we performed subcellular fractionation experiments and used confocal microscopy to examine the distribution of heterologously expressed fusion proteins involving various deletions and point mutations of the HCV core combined with green fluorescent proteins. We demonstrated that a region spanning amino acids 112 to 152 can mediate association of the core protein not only with the ER but also with the mitochondrial outer membrane. This region contains an 18-amino-acid motif which is predicted to form an amphipathic α-helix structure. With regard to the nuclear targeting of the core protein, we identified a novel bipartite nuclear localization signal, which requires two out of three basic-residue clusters for efficient nuclear translocation, possibly by occupying binding sites on importin-α. Differences in the cellular trafficking of HCV core protein, achieved and maintained by multiple targeting functions as mentioned above, may in part regulate the diverse range of biological roles of the core protein.
Author Takuya Iwasaki
Akiko Rikimaru
Kohji Moriishi
Ryosuke Suzuki
Takeya Tsutsumi
Kiyohisa Mizumoto
Keiko Tanaka
Tatsuo Miyamura
Takashi Shimoike
Tetsuro Suzuki
Yoshiharu Matsuura
Shinichiro Sakamoto
AuthorAffiliation Department of Virology II, National Institute of Infectious Diseases, Shinjuku-ku, 1 Department of Biochemistry, School of Pharmaceutical Sciences, Kitasato University, Minato-ku, 2 Department of Pathology, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo, 3 Research Center for Emerging Infectious Diseases, Research Institute for Microbial Diseases, Osaka University, Suita-shi, Osaka, 4 Department of Pathology, Institute of Tropical Medicine, Nagasaki University, Nagasaki-shi, Nagasaki, Japan 5
AuthorAffiliation_xml – name: Department of Virology II, National Institute of Infectious Diseases, Shinjuku-ku, 1 Department of Biochemistry, School of Pharmaceutical Sciences, Kitasato University, Minato-ku, 2 Department of Pathology, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo, 3 Research Center for Emerging Infectious Diseases, Research Institute for Microbial Diseases, Osaka University, Suita-shi, Osaka, 4 Department of Pathology, Institute of Tropical Medicine, Nagasaki University, Nagasaki-shi, Nagasaki, Japan 5
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  givenname: Ryosuke
  surname: SUZUKI
  fullname: SUZUKI, Ryosuke
  organization: Department of Virology II, National Institute of Infectious Diseases, Shinjuku-ku, Japan
– sequence: 2
  givenname: Shinichiro
  surname: SAKAMOTO
  fullname: SAKAMOTO, Shinichiro
  organization: Department of Virology II, National Institute of Infectious Diseases, Shinjuku-ku, Japan
– sequence: 3
  givenname: Tatsuo
  surname: MIYAMURA
  fullname: MIYAMURA, Tatsuo
  organization: Department of Virology II, National Institute of Infectious Diseases, Shinjuku-ku, Japan
– sequence: 4
  givenname: Tetsuro
  surname: SUZUKI
  fullname: SUZUKI, Tetsuro
  organization: Department of Virology II, National Institute of Infectious Diseases, Shinjuku-ku, Japan
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  givenname: Takeya
  surname: TSUTSUMI
  fullname: TSUTSUMI, Takeya
  organization: Department of Virology II, National Institute of Infectious Diseases, Shinjuku-ku, Japan
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  givenname: Akiko
  surname: RIKIMARU
  fullname: RIKIMARU, Akiko
  organization: Department of Virology II, National Institute of Infectious Diseases, Shinjuku-ku, Japan
– sequence: 7
  givenname: Keiko
  surname: TANAKA
  fullname: TANAKA, Keiko
  organization: Department of Pathology, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo, Japan
– sequence: 8
  givenname: Takashi
  surname: SHIMOIKE
  fullname: SHIMOIKE, Takashi
  organization: Department of Virology II, National Institute of Infectious Diseases, Shinjuku-ku, Japan
– sequence: 9
  givenname: Kohji
  surname: MORIISHI
  fullname: MORIISHI, Kohji
  organization: Research Center for Emerging Infectious Diseases, Research Institute for Microbial Diseases, Osaka University, Suita-shi, Osaka, Japan
– sequence: 10
  givenname: Takuya
  surname: IWASAKI
  fullname: IWASAKI, Takuya
  organization: Department of Pathology, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo, Japan
– sequence: 11
  givenname: Kiyohisa
  surname: MIZUMOTO
  fullname: MIZUMOTO, Kiyohisa
  organization: Department of Biochemistry, School of Pharmaceutical Sciences, Kitasato University, Minato-ku, Japan
– sequence: 12
  givenname: Yoshiharu
  surname: MATSUURA
  fullname: MATSUURA, Yoshiharu
  organization: Research Center for Emerging Infectious Diseases, Research Institute for Microbial Diseases, Osaka University, Suita-shi, Osaka, Japan
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Keywords Virus
Microbiology
Flaviviridae
Localization
Hepatitis C virus
Hepacivirus
Protein
Virology
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Corresponding author. Mailing address: Department of Virology II, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo, Japan 162-8640. Phone: (81) 3-5285-1111. Fax: (81) 3-5285-1161. E-mail: tesuzuki@nih.go.jp.
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Snippet Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
Hepatitis C virus (HCV) core protein is a putative nucleocapsid protein with a number of regulatory functions. In tissue culture cells, HCV core protein is...
ABSTRACT Hepatitis C virus (HCV) core protein is a putative nucleocapsid protein with a number of regulatory functions. In tissue culture cells, HCV core...
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StartPage 1271
SubjectTerms Amino Acid Sequence
Biological and medical sciences
Cell Line
Cell Nucleus - chemistry
Endoplasmic Reticulum - chemistry
Fundamental and applied biological sciences. Psychology
Hepacivirus - chemistry
Hepatitis C virus
Humans
Karyopherins - physiology
Microbiology
Miscellaneous
Mitochondria - chemistry
Molecular Sequence Data
Nuclear Localization Signals
Viral Core Proteins - analysis
Viral Core Proteins - chemistry
Virology
Title Molecular Determinants for Subcellular Localization of Hepatitis C Virus Core Protein
URI http://jvi.asm.org/content/79/2/1271.abstract
https://www.ncbi.nlm.nih.gov/pubmed/15613354
https://search.proquest.com/docview/17802670
https://search.proquest.com/docview/67331038
https://pubmed.ncbi.nlm.nih.gov/PMC538550
Volume 79
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