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 Khan, A. G.
Right arrow Articles by Blaas, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Khan, A. G.
Right arrow Articles by Blaas, D.

 Previous Article  |  Next Article 

Journal of Virology, May 2007, p. 4625-4632, Vol. 81, No. 9
0022-538X/07/$08.00+0     doi:10.1128/JVI.02160-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Human Rhinovirus Type 54 Infection via Heparan Sulfate Is Less Efficient and Strictly Dependent on Low Endosomal pH{triangledown}

Abdul Ghafoor Khan, Johannes Pichler,{dagger} Anke Rosemann,{ddagger} and Dieter Blaas*

Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, A-1030 Vienna, Austria

Received 3 October 2006/ Accepted 1 February 2007

K-type major-group human rhinoviruses (HRVs) (including HRV54) share a prominent lysine residue in the HI surface loop of VP1 with all minor-group HRVs. Despite the presence of this residue, they cannot use members of the low-density lipoprotein receptor family for productive infection. Reexamining all K-type viruses for receptor usage, we noticed that HRV54 is able to replicate in RD cells that lack the major-group receptor intercellular adhesion molecule 1 (ICAM-1). By using receptor blocking assays, inhibition of sulfation, enzymatic digestion, and proteoglycan-deficient cell lines, we show here that wild-type HRV54, without any adaptation, uses heparan sulfate (HS) proteoglycan as an alternate receptor. However, infection via HS is less efficient than infection via ICAM-1. Moreover, HRV54 has an acid lability profile similar to that of the minor-group virus HRV2. In ICAM-1-deficient cells its replication is completely blocked by the H+-ATPase inhibitor bafilomycin A1, whereas in ICAM-1-expressing cells it replicates in the presence of the drug. Thus, use of a "noncatalytic" receptor requires the virus to be highly unstable at low pH.

* Corresponding author. Mailing address: Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, A-1030 Vienna, Austria. Phone: 43 1 4277 61630. Fax: 43 1 4277 9616. E-mail: dieter.blaas{at}meduniwien.ac.at

{triangledown} Published ahead of print on 14 February 2007.

{dagger} Present address: University of Natural Resources and Applied Life Sciences, Dept. Biotechnology, Institute of Applied Microbiology, Muthgasse 18, A-1190 Vienna, Austria.

{ddagger} Present address: Euroimmun AG, D-23560 Lübeck, Germany.

Journal of Virology, May 2007, p. 4625-4632, Vol. 81, No. 9
0022-538X/07/$08.00+0     doi:10.1128/JVI.02160-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Blomqvist, S., Savolainen-Kopra, C., Paananen, A., Hovi, T., Roivainen, M. (2009). Molecular characterization of human rhinovirus field strains isolated during surveillance of enteroviruses. J. Gen. Virol. 90: 1371-1381 [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»