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
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
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 Schwegmann-Wessels, C.
Right arrow Articles by Herrler, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schwegmann-Wessels, C.
Right arrow Articles by Herrler, G.

 Previous Article  |  Next Article 

Journal of Virology, November 2003, p. 11846-11848, Vol. 77, No. 21
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.21.11846-11848.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Binding of Transmissible Gastroenteritis Coronavirus to Brush Border Membrane Sialoglycoproteins

Christel Schwegmann-Wessels,1* Gert Zimmer,1 Bernd Schröder,2 Gerhard Breves,2 and Georg Herrler1

Institut für Virologie,1 Physiologisches Institut, Tierärztliche Hochschule Hannover, 30559 Hannover, Germany2

Received 2 May 2003/ Accepted 30 July 2003

Transmissible gastroenteritis coronavirus (TGEV) is a porcine pathogen causing enteric infections that are lethal for suckling piglets. The enterotropism of TGEV is connected with the sialic acid binding activity of the viral surface protein S. Here we show that, among porcine intestinal brush border membrane proteins, TGEV recognizes a mucin-type glycoprotein designated MGP in a sialic acid-dependent fashion. Virus binding assays with cryosections of the small intestine from a suckling piglet revealed the binding of TGEV to mucin-producing goblet cells. A nonenteropathogenic mutant virus that lacked a sialic acid binding activity was unable to bind to MGP and to attach to goblet cells. Our results suggest a role of MGP in the enteropathogenicity of TGEV.

* Corresponding author. Mailing address: Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany. Phone: 49 (0) 511-28-8842. Fax: 49 (0) 511-28-8898. E-mail: Christel.Schwegmann{at}tiho-hannover.de.

Journal of Virology, November 2003, p. 11846-11848, Vol. 77, No. 21
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.21.11846-11848.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Schwegmann-Wessels, C., Glende, J., Ren, X., Qu, X., Deng, H., Enjuanes, L., Herrler, G. (2009). Comparison of vesicular stomatitis virus pseudotyped with the S proteins from a porcine and a human coronavirus. J. Gen. Virol. 90: 1724-1729 [Abstract] [Full Text]  
  • Ren, X., Glende, J., Al-Falah, M., de Vries, V., Schwegmann-Wessels, C., Qu, X., Tan, L., Tschernig, T., Deng, H., Naim, H. Y., Herrler, G. (2006). Analysis of ACE2 in polarized epithelial cells: surface expression and function as receptor for severe acute respiratory syndrome-associated coronavirus. J. Gen. Virol. 87: 1691-1695 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»