Efficient Multiplication of Human Metapneumovirus in Vero Cells Expressing the Transmembrane Serine Protease TMPRSS2

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Published inJournal of Virology Vol. 82; no. 17; pp. 8942 - 8946
Main Authors Shirogane, Yuta, Takeda, Makoto, Iwasaki, Masaharu, Ishiguro, Nobuhisa, Takeuchi, Hiroki, Nakatsu, Yuichiro, Tahara, Maino, Kikuta, Hideaki, Yanagi, Yusuke
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.09.2008
American Society for Microbiology (ASM)
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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 Human metapneumovirus (HMPV) is a major causative agent of severe bronchiolitis and pneumonia. Its fusion (F) protein must be cleaved by host proteases to cause membrane fusion, a critical step for virus infection. By generating Vero cells constitutively expressing the transmembrane serine protease TMPRSS2 and green fluorescent protein-expressing recombinant HMPV, we show that TMPRSS2, which is expressed in the human lung epithelium, cleaves the HMPV F protein efficiently and supports HMPV multiplication. The results indicate that TMPRSS2 is a possible candidate protease involved in the development of lower respiratory tract illness in HMPV-infected patients.
Human metapneumovirus (HMPV) is a major causative agent of severe bronchiolitis and pneumonia. Its fusion (F) protein must be cleaved by host proteases to cause membrane fusion, a critical step for virus infection. By generating Vero cells constitutively expressing the transmembrane serine protease TMPRSS2 and green fluorescent protein-expressing recombinant HMPV, we show that TMPRSS2, which is expressed in the human lung epithelium, cleaves the HMPV F protein efficiently and supports HMPV multiplication. The results indicate that TMPRSS2 is a possible candidate protease involved in the development of lower respiratory tract illness in HMPV-infected patients.Human metapneumovirus (HMPV) is a major causative agent of severe bronchiolitis and pneumonia. Its fusion (F) protein must be cleaved by host proteases to cause membrane fusion, a critical step for virus infection. By generating Vero cells constitutively expressing the transmembrane serine protease TMPRSS2 and green fluorescent protein-expressing recombinant HMPV, we show that TMPRSS2, which is expressed in the human lung epithelium, cleaves the HMPV F protein efficiently and supports HMPV multiplication. The results indicate that TMPRSS2 is a possible candidate protease involved in the development of lower respiratory tract illness in HMPV-infected patients.
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       
Author Makoto Takeda
Yuta Shirogane
Hiroki Takeuchi
Nobuhisa Ishiguro
Yusuke Yanagi
Maino Tahara
Hideaki Kikuta
Yuichiro Nakatsu
Masaharu Iwasaki
AuthorAffiliation Department of Virology, Faculty of Medicine, Kyushu University, Fukuoka 812-8582, 1 Department of Pediatrics, Hokkaido University Graduate School of Medicine, Sapporo 060-8638, 2 Pediatric Clinic, Touei Hospital, Kita-41, Higashi-6, Higashi-ku, Sapporo 007-0841, Japan 3
AuthorAffiliation_xml – name: Department of Virology, Faculty of Medicine, Kyushu University, Fukuoka 812-8582, 1 Department of Pediatrics, Hokkaido University Graduate School of Medicine, Sapporo 060-8638, 2 Pediatric Clinic, Touei Hospital, Kita-41, Higashi-6, Higashi-ku, Sapporo 007-0841, Japan 3
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  fullname: Iwasaki, Masaharu
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  givenname: Maino
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  surname: Yanagi
  fullname: Yanagi, Yusuke
  organization: Department of Virology, Faculty of Medicine, Kyushu University, Fukuoka 812-8582
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Corresponding author. Mailing address: Department of Virology, Faculty of Medicine, Kyushu University, Fukuoka 812-8582, Japan. Phone: 81-92-642-6138. Fax: 81-92-642-6140. E-mail: mtakeda@virology.med.kyushu-u.ac.jp
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Human metapneumovirus (HMPV) is a major causative agent of severe bronchiolitis and pneumonia. Its fusion (F) protein must be cleaved by host proteases to...
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StartPage 8942
SubjectTerms Animals
Biological and medical sciences
Cercopithecus aethiops
Epithelium - metabolism
Fundamental and applied biological sciences. Psychology
Gene Expression
Green Fluorescent Proteins - metabolism
Lung - cytology
Membrane Fusion
Metapneumovirus - growth & development
Microbiology
Miscellaneous
Serine Endopeptidases - genetics
Serine Endopeptidases - metabolism
Vero Cells
Viral Fusion Proteins - metabolism
Virology
Virus-Cell Interactions
Title Efficient Multiplication of Human Metapneumovirus in Vero Cells Expressing the Transmembrane Serine Protease TMPRSS2
URI http://jvi.asm.org/content/82/17/8942.abstract
https://www.ncbi.nlm.nih.gov/pubmed/18562527
https://www.proquest.com/docview/69426193
https://pubmed.ncbi.nlm.nih.gov/PMC2519639
Volume 82
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