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 Zautner, A. E.
Right arrow Articles by Schmidtke, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zautner, A. E.
Right arrow Articles by Schmidtke, M.

 Previous Article  |  Next Article 

Journal of Virology, September 2003, p. 10071-10077, Vol. 77, No. 18
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.18.10071-10077.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Heparan Sulfates and Coxsackievirus-Adenovirus Receptor: Each One Mediates Coxsackievirus B3 PD Infection

A. E. Zautner,1 U. Körner,1 A. Henke,1 C. Badorff,2 and M. Schmidtke1*

Institute of Virology and Antiviral Therapy, Friedrich Schiller University Jena, D-07745 Jena,1 Molecular Cardiology, Department of Cardiology, University of Frankfurt, 60590 Frankfurt/Main, Germany2

Received 3 February 2003/ Accepted 17 June 2003

Amino acid exchanges in the virus capsid protein VP1 allow the coxsackievirus B3 variant PD (CVB3 PD) to replicate in decay accelerating factor (DAF)-negative and coxsackievirus-adenovirus receptor (CAR)-negative cells. This suggests that molecules other than DAF and CAR are involved in attachment of this CVB3 variant to cell surfaces. The observation that productive infection associated with cytopathic effect occurred in Chinese hamster ovary (CHO-K1) cells, whereas heparinase-treated CHO-K1 cells, glucosaminoglycan-negative pgsA-745, heparan sulfate (HS)-negative pgsD-677, and pgsE-606 cells with significantly reduced N-sulfate expression resist CVB3 PD infection, indicates a critical role of highly sulfated HS. 2-O-sulfate-lacking pgsF-17 cells represented the cell line with minimum HS modifications susceptible for CVB3 PD. Inhibition of virus replication in CHO-K1 cells by polycationic compounds, pentosan polysulfate, lung heparin, and several intestinal but not kidney HS supported the hypothesis that CVB3 PD uses specific modified HS for entry. In addition, recombinant human hepatocyte growth factor blocked CVB3 PD infection. However, CAR also mediates CVB3 PD infection, because this CVB3 variant replicates in HS-lacking but CAR-bearing Raji cells, infection could be prevented by pretreatment of cells with CAR antibody, and HS-negative pgsD-677 cells transfected with CAR became susceptible for CVB3 PD. These results demonstrate that the amino acid substitutions in the viral capsid protein VP1 enable CVB3 PD to use specific modified HS as an entry receptor in addition to CAR.

* Corresponding author. Mailing address: Institute of Virology and Antiviral Therapy, Medical Center of the Friedrich Schiller University, Winzerlaer Str. 10, D-07745 Jena, Germany. Phone: 49 3641 657222. Fax: 49 3641 657202. E-mail: michaela.schmidtke{at}med.uni-jena.de.

Journal of Virology, September 2003, p. 10071-10077, Vol. 77, No. 18
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.18.10071-10077.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Artemenko, A. G., Muratov, E. N., Kuz'min, V. E., Kovdienko, N. A., Hromov, A. I., Makarov, V. A., Riabova, O. B., Wutzler, P., Schmidtke, M. (2007). Identification of individual structural fragments of N,N'-(bis-5-nitropyrimidyl)dispirotripiperazine derivatives for cytotoxicity and antiherpetic activity allows the prediction of new highly active compounds. J Antimicrob Chemother 60: 68-77 [Abstract] [Full Text]  
  • Khan, A. G., Pichler, J., Rosemann, A., Blaas, D. (2007). Human Rhinovirus Type 54 Infection via Heparan Sulfate Is Less Efficient and Strictly Dependent on Low Endosomal pH. J. Virol. 81: 4625-4632 [Abstract] [Full Text]  
  • Jenssen, H., Hamill, P., Hancock, R. E. W. (2006). Peptide Antimicrobial Agents. Clin. Microbiol. Rev. 19: 491-511 [Abstract] [Full Text]  
  • Zautner, A. E., Jahn, B., Hammerschmidt, E., Wutzler, P., Schmidtke, M. (2006). N- and 6-O-Sulfated Heparan Sulfates Mediate Internalization of Coxsackievirus B3 Variant PD into CHO-K1 Cells.. J. Virol. 80: 6629-6636 [Abstract] [Full Text]  
  • Schmidtke, M., Hammerschmidt, E., Schuler, S., Zell, R., Birch-Hirschfeld, E., Makarov, V. A., Riabova, O. B., Wutzler, P. (2005). Susceptibility of coxsackievirus B3 laboratory strains and clinical isolates to the capsid function inhibitor pleconaril: antiviral studies with virus chimeras demonstrate the crucial role of amino acid 1092 in treatment. J Antimicrob Chemother 56: 648-656 [Abstract] [Full Text]  
  • Fry, E. E., Newman, J. W. I., Curry, S., Najjam, S., Jackson, T., Blakemore, W., Lea, S. M., Miller, L., Burman, A., King, A. M. Q., Stuart, D. I. (2005). Structure of Foot-and-mouth disease virus serotype A1061 alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variation. J. Gen. Virol. 86: 1909-1920 [Abstract] [Full Text]  
  • Vlasak, M., Goesler, I., Blaas, D. (2005). Human Rhinovirus Type 89 Variants Use Heparan Sulfate Proteoglycan for Cell Attachment. J. Virol. 79: 5963-5970 [Abstract] [Full Text]  
  • Milstone, A. M., Petrella, J., Sanchez, M. D., Mahmud, M., Whitbeck, J. C., Bergelson, J. M. (2005). Interaction with Coxsackievirus and Adenovirus Receptor, but Not with Decay-Accelerating Factor (DAF), Induces A-Particle Formation in a DAF-Binding Coxsackievirus B3 Isolate. J. Virol. 79: 655-660 [Abstract] [Full Text]  
  • Basu, A., Beyene, A., Meyer, K., Ray, R. (2004). The Hypervariable Region 1 of the E2 Glycoprotein of Hepatitis C Virus Binds to Glycosaminoglycans, but This Binding Does Not Lead to Infection in a Pseudotype System. J. Virol. 78: 4478-4486 [Abstract] [Full Text]  
  • Escribano-Romero, E., Jimenez-Clavero, M. A., Gomes, P., Garcia-Ranea, J. A., Ley, V. (2004). Heparan sulphate mediates swine vesicular disease virus attachment to the host cell. J. Gen. Virol. 85: 653-663 [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»