This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shirogane, Y.
Right arrow Articles by Yanagi, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shirogane, Y.
Right arrow Articles by Yanagi, Y.

 Previous Article  |  Next Article 

Journal of Virology, September 2008, p. 8942-8946, Vol. 82, No. 17
0022-538X/08/$08.00+0     doi:10.1128/JVI.00676-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

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

Yuta Shirogane,1 Makoto Takeda,1* Masaharu Iwasaki,1 Nobuhisa Ishiguro,2 Hiroki Takeuchi,1 Yuichiro Nakatsu,1 Maino Tahara,1 Hideaki Kikuta,3 and Yusuke Yanagi1

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, Japan3

Received 27 March 2008/ Accepted 10 June 2008

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.

* 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{at}virology.med.kyushu-u.ac.jp

{triangledown} Published ahead of print on 18 June 2008.

Journal of Virology, September 2008, p. 8942-8946, Vol. 82, No. 17
0022-538X/08/$08.00+0     doi:10.1128/JVI.00676-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chaipan, C., Kobasa, D., Bertram, S., Glowacka, I., Steffen, I., Solomon Tsegaye, T., Takeda, M., Bugge, T. H., Kim, S., Park, Y., Marzi, A., Pohlmann, S. (2009). Proteolytic Activation of the 1918 Influenza Virus Hemagglutinin. J. Virol. 83: 3200-3211 [Abstract] [Full Text]  
  • Schowalter, R. M., Chang, A., Robach, J. G., Buchholz, U. J., Dutch, R. E. (2009). Low-pH Triggering of Human Metapneumovirus Fusion: Essential Residues and Importance in Entry. J. Virol. 83: 1511-1522 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»