1887

Abstract

We have shown previously that, compared to other enteroviruses, the coxsackievirus A9 (CAV-9) prototype strain, Griggs, contains a C-terminal extension to the capsid protein VP1 and that within this extension there is an RGD (arginine-glycine-aspartic acid) motif. To determine whether these features are found in other CAV-9 strains and therefore analyse whether they are likely to be functionally important, we have determined the nucleotide sequence of the appropriate region from five strains, isolated over a 25 year period. The results indicate that there is considerable diversity between the strains and there is little correlation between nucleotide sequence identity and date of isolation. All isolates exhibit the VP1 extension and although its amino acid sequence is otherwise variable, the RGD motif is common to all. This conservation of sequence, within a region which can otherwise vary, implies that the RGD sequence must be functionally significant. The VP1 extension shows similarity to sequences found in foot-and-mouth-disease virus strains and to part of the precursor of the cellular protein, human transforming growth factor , and the possible significance of these observations is discussed.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-73-3-621
1992-03-01
2024-04-18
Loading full text...

Full text loading...

/deliver/fulltext/jgv/73/3/JV0730030621.html?itemId=/content/journal/jgv/10.1099/0022-1317-73-3-621&mimeType=html&fmt=ahah

References

  1. Acharya R., Fry E., Stuart D., Fox G., Rowlands D., Brown F. 1989; The three-dimensional structure of foot-and-mouth disease virus at 2.9Å resolution. Nature, London 337:709–716
    [Google Scholar]
  2. Brown A. L., Campbell R. O., Clarke B. E. 1989; The nucleotide sequence of the structural-protein-coding region of foot- and-mouth disease virus serotype SAT3. Gene 75:225–234
    [Google Scholar]
  3. Chang K. H., Auvinen P., Hyypiä T., Stanway G. 1989; The nucleotide sequence of coxsackievirus A9; implications for receptor binding and enterovirus classification. Journal of General Virology 70:3269–3280
    [Google Scholar]
  4. Carroll A. R., Rowlands D. J., Clarke B. E. 1984; The complete nucleotide sequence of the RNA coding for the primary translation products of foot-and-mouth disease virus. Nucleic Acids Research 12:2461–2472
    [Google Scholar]
  5. Colonno R. J. 1987; Cell surface receptors for picomaviruses. BioEssays 5:270–275
    [Google Scholar]
  6. Colonno R. J., Condra J. H., Mizutani S., Callahan P. L., Davies M.-E., Murcko M. A. 1988; Evidence for the direct involvement of the rhinovirus canyon in receptor binding. Proceedings of the National Academy of Sciences, U.S.A 85:5449–5453
    [Google Scholar]
  7. Crowell R. L., Hsu K.-H. L., Schultz M., Landau B. J. 1987; Cellular receptors in coxsackievirus infections. In Positive-strand RNA Viruses, UCLA Symposium on Molecular and Cellular Biology, New Series vol 54 pp 453–466 Edited by Brinton M. A., Rueckert R. R. New York: Alan R. Liss;
    [Google Scholar]
  8. Felsenstein J. 1989 PHYLIP 3.2 Manual Berkeley: University of California Herbarium;
    [Google Scholar]
  9. Forss S., Streubel K., Beck E., Schaller H. 1984; Nucleotide sequence and genome organization of foot-and-mouth disease virus. Nucleic Acids Research 12:6587–6601
    [Google Scholar]
  10. Fox G., Parry N. R., Barnett P. V., McGinn B., Rowlands D. J., Brown F. 1989; The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginineglycine-aspartic acid). Journal of General Virology 70:625–637
    [Google Scholar]
  11. Gama R. E., Hughes P. J., Bruce C. B., Stanway G. 1988; Polymerase chain reaction amplification of rhinovirus nucleic acids from clinical material. Nucleic Acids Research 16:9346
    [Google Scholar]
  12. Gama R. E., Horsnell P. R., Hughes P. J., North C., Bruce C. B., Al-Nakib W., Stanway G. 1989; Amplification of rhinovirus specific nucleic acids from clinical samples using the polymerase chain reaction. Journal of Medical Virology 28:73–77
    [Google Scholar]
  13. Greve J. M., Davis G., Meyer A. M., Forte C. P., Yost S. C., Marlor C. W., Kamarck M. E., McClelland A. 1989; The major human rhinovirus receptor is ICAM-1. Cell 56:839–847
    [Google Scholar]
  14. Grist N. R., Reid D. 1988; General pathogenicity and epidemiology. In Coxsackieviruses, A General Update pp 221–239 Edited by Bendinelli M., Friedman H. New York: Plenum Press;
    [Google Scholar]
  15. Hirst G. 1962; Genetic recombination with Newcastle disease virus, poliovirus and influenza. Cold Spring Harbor Symposia on Quantitative Biology 27:303–309
    [Google Scholar]
  16. Hughes P. J., North C., Minor P. D., Stanway G. 1989; The complete nucleotide sequence of coxsackievirus A21. Journal of General Virology 70:2943–2952
    [Google Scholar]
  17. Kanzaki T., Olofsson A., Moren A., Wernstedt C., Hellman U., Miyazono K., Claesson-Welsh L., Heldin C.-H. 1990; TGF-β 1 binding protein: a component of the large latent complex of TGF-β 1 with multiple repeat sequences. Cell 61:1051–1061
    [Google Scholar]
  18. Kew O. M., Nottay B. K. 1985; Evolution of the oral polio vaccine strains in humans occurs by both mutation and intermolecular recombination. In Modern Approaches to Vaccines: Molecular and Chemical Basis of Virus Virulence and Immunogenicity pp 357–362 Edited by Chanock R. M., Lerner R. A. New York: Cold Spring Harbor Laboratory;
    [Google Scholar]
  19. Khatchikian D., Orlich M., Rott R. 1989; Increased viral pathogenicity after insertion of a 28S ribosomal RNA sequence into the haemagglutinin gene of an influenza virus. Nature, London 340:156–157
    [Google Scholar]
  20. King A. M. Q., McCahon D., Saunders K., Newman J. W. I., Slade W. R. 1985; Multiple sites of recombination within the RNA genome of foot-and-mouth disease virus. Virus Research 3:373–384
    [Google Scholar]
  21. Makoff A. J., Paynter C. A., Rowlands D. J., Boothroyd J. C. 1982; Comparison of the amino acid sequence of the major immunogen from three serotypes of foot and mouth disease virus. Nucleic Acids Research 10:8285–8295
    [Google Scholar]
  22. Meyers G., Rumenapf T., Theil H.-J. 1989; Ubiquitin in a togavirus. Nature, London 341:491
    [Google Scholar]
  23. Pierschbacher M. D., Ruoslahti E. 1984; Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature, London 309:30–33
    [Google Scholar]
  24. Rico-Hesse R., Pallansch M., Nottay B. K., Kew O. M. 1987; Geographic distribution of wild poliovirus type 1 genotypes. Virology 160:311–322
    [Google Scholar]
  25. Roivainen M., Hyypiä T., Piirainen L., Kalkkinen N., Stanway G., HovI T. 1991; RGD-dependent entry of coxsackievirus A9 to host cells and its bypass after cleavage of VP1 protein by intestinal proteases. Journal of Virology 65:4735–4740
    [Google Scholar]
  26. Rossmann M. G., Arnold E., Erickson T. W., Frankenberger E. A., Griffith T. P., Hecht H. T., Johnson T., Kamer G., Luo M., Mosser A. G., Rueckert R. R., Sherry B., Vriend G. 1985; Structure of a human common cold virus and functional relationship to other picomaviruses. Nature, London 317:145–153
    [Google Scholar]
  27. Ruoslahti E., Pierschbacher M. D. 1987; New perspectives in cell adhesion: RGD and integrins. Science 238:491–493
    [Google Scholar]
  28. Sporn M. B., Roberts A. B., Wakefield L. M., Assoian R. K. 1986; Transforming growth factor-beta: biological function and chemical structure. Science 233:532–534
    [Google Scholar]
  29. Staunton D. E., Merluzzi V. J., Rothlein R., Barton R., Martin S. D., Springer T. A. 1989; A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses. Cell 56:849–853
    [Google Scholar]
  30. Surovoy A. Yu., Ivanov V. T., Chepurkin A. V., Ivanyuschehenkov V. N., Dryagalin N. N. 1988; Is the Arg-Gly-Asp sequence involved in binding of foot-and-mouth disease virus with cell receptor. Bioorganic Chimija 14:965–968 (in Russian)
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-73-3-621
Loading
/content/journal/jgv/10.1099/0022-1317-73-3-621
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error