1887

Abstract

Potato virus X (PVX) and narcissus mosaic virus (NMV) were studied using vibrational Raman optical activity (ROA) in order to obtain new information on the structures of their coat protein subunits. The ROA spectra of the two intact virions are very similar to each other and similar to that of tobacco mosaic virus (TMV) studied previously, being dominated by signals characteristic of proteins with helix bundle folds. In particular, PVX and NMV show strong positive ROA bands at ∼1340 cm assigned to hydrated α-helix and perhaps originating in surface exposed helical residues, together with less strong positive ROA intensity in the range ∼1297–1312 cm assigned to α-helix in a more hydrophobic environment and perhaps originating in residues at helix–helix interfaces. The positive ∼1340 cm ROA band of TMV is less intense than those of PVX and NMV, suggesting that TMV contains less hydrated α-helix. Small differences in other spectral regions reflect differences in some loop, turn and side-chain compositions and conformations among the three viruses. A pattern recognition program based on principal component analysis of ROA spectra indicates that the coat protein subunit folds of PVX and NMV may be very similar to each other and similar to that of TMV. These results suggest that PVX and NMV may have coat protein subunit structures based on folds similar to the TMV helix bundle and hence that the helical architecture of the PVX and NMV particles may be similar to that of TMV but with different structural parameters.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-83-1-241
2002-01-01
2019-10-14
Loading full text...

Full text loading...

/deliver/fulltext/jgv/83/1/0830241a.html?itemId=/content/journal/jgv/10.1099/0022-1317-83-1-241&mimeType=html&fmt=ahah

References

  1. Abou Haidar, M. G., Xu, H. & Hefferon, K. L. ( 1998; ). Potexvirus isolation and RNA extraction. In Plant Virus Protocols , pp. 131-143. Edited by G. D. Foster & S. C. Taylor. Totowa, NJ:Humana Press.
  2. Baratova, L. A., Grebenshchikov, N. I., Dobrov, E. N., Gedrovich, A. V., Kashirin, I. A., Shishkov, A. V., Efimov, A. V., Järvekülg, L., Radavsky, Y. L. & Saarma, M. ( 1992a; ). The organization of potato virus X coat proteins in virus particles studied by tritium planigraphy and model building. Virology 188, 175-180.[CrossRef]
    [Google Scholar]
  3. Baratova, L. A., Grebenshchikov, N. I., Shishkov, A. V., Kashirin, I. A., Radavsky, J. L., Järvekülg, L. & Saarma, M. ( 1992b; ). The topography of the surface of potato virus X: tritium planigraphy and immunological analysis. Journal of General Virology 73, 229-235.[CrossRef]
    [Google Scholar]
  4. Barron, L. D. & Hecht, L. ( 2000; ). Vibrational Raman optical activity: from fundamentals to biochemical applications. In Circular Dichroism. Principles and Applications , pp. 667-701. Edited by N. Berova, K. Nakanishi & R. W. Woody. New York:John Wiley & Sons.
  5. Barron, L. D., Hecht, L., Blanch, E. W. & Bell, A. F. ( 2000; ). Solution structure and dynamics of biomolecules from Raman optical activity. Progress in Biophysics & Molecular Biology 73, 1-49.[CrossRef]
    [Google Scholar]
  6. Bell, A. F., Hecht, L. & Barron, L. D. ( 1997; ). Vibrational Raman optical activity as a probe of polyribonucleotide stereochemistry. Journal of the American Chemical Society 119, 6006-6013.[CrossRef]
    [Google Scholar]
  7. Bell, A. F., Hecht, L. & Barron, L. D. ( 1998; ). Vibrational Raman optical activity of DNA and RNA. Journal of the American Chemical Society 120, 5820-5821.[CrossRef]
    [Google Scholar]
  8. Blanch, E. W., Bell, A. F., Hecht, L., Day, L. A. & Barron, L. D. ( 1999; ). Raman optical activity of filamentous bacteriophages: hydration of α-helices. Journal of Molecular Biology 290, 1-7.[CrossRef]
    [Google Scholar]
  9. Blanch, E. W., Robinson, D. J., Hecht, L. & Barron, L. D. ( 2001a; ). A comparison of the solution structures of tobacco rattle and tobacco mosaic viruses from Raman optical activity. Journal of General Virology 82, 1499-1502.
    [Google Scholar]
  10. Blanch, E. W., Pederson, D. M., Hecht, L., Day, L. A. & Barron, L. D. ( 2001b; ). Tryptophan absolute stereochemistry in viral coat proteins from Raman optical activity. Journal of the American Chemical Society 123, 4863-4864.[CrossRef]
    [Google Scholar]
  11. Brunt, A. A., Foster, G. D., Morozov, S. Y. & Zavriev, S. K. ( 2000; ). Genus Potexvirus. In Virus Taxonomy. Seventh Report of the International Committee on Taxonomy of Viruses , pp. 975-981. Edited by M. H. V. van Regenmortel, C. M. Fauquet, D. H. L. Bishop, E. B. Carstens, M. K. Estes, S. M. Lemon, J. Maniloff, M. A. Mayo, D. J. McGeoch, C. R. Pringle & R. B. Wickner. San Diego:Academic Press.
  12. Carey, P. R. (1982). Biochemical Applications of Raman and Resonance Raman Spectroscopies. New York: Academic Press.
  13. Goldanskii, V. I., Kashirin, I. A., Shishkov, A. V., Baratova, L. A. & Grebenshchikov, N. I. ( 1988; ). The use of thermally activated tritium atoms for structural-biological investigations: the topography of the TMV protein-accessible surface of the virus. Journal of Molecular Biology 201, 567-574.[CrossRef]
    [Google Scholar]
  14. Goodman, R. M. (1973). Purification of potato virus X and the molecular weight of its coat protein subunits. John Innes Institute, 64 th Annual Report, 126.
  15. Hecht, L., Barron, L. D., Blanch, E. W., Bell, A. F. & Day, L. A. ( 1999; ). Raman optical activity instrument for studies of biopolymer structure and dynamics. Journal of Raman Spectroscopy 30, 815-825.[CrossRef]
    [Google Scholar]
  16. Homer, R. B. & Goodman, R. M. ( 1975; ). Circular dichroism and fluorescence studies on potato virus X and its structural components. Biochimica et Biophysica Acta 378, 296-304.[CrossRef]
    [Google Scholar]
  17. Jones, R. A. C. ( 1982; ). Breakdown of potato virus X resistance gene Nx: selection of a group four strain from strain group three. Plant Pathology 31, 325-331.[CrossRef]
    [Google Scholar]
  18. Miura, T. & Thomas, G. J.Jr ( 1995; ). Raman spectroscopy of proteins and their assemblies. In Subcellular Biochemistry, vol. 24, Proteins: Structure, Function, and Engineering , pp. 55-99. Edited by B. B. Biswas & S. Roy. New York:Plenum Press.
  19. Nafie, L. A. ( 1997; ). Infrared and Raman vibrational optical activity. Annual Review of Physical Chemistry 48, 357-386.[CrossRef]
    [Google Scholar]
  20. Namba, K., Pattanayek, R. & Stubbs, G. ( 1989; ). Visualization of protein–nucleic acid interactions in a virus. Refined structure of intact tobacco mosaic virus at 2·9 Å by X-ray fiber diffraction. Journal of Molecular Biology 208, 307-325.[CrossRef]
    [Google Scholar]
  21. Nielsen, K., Garp, T., Paulsen, A. & Boghosian, S. ( 1999; ). Principal component analysis of Raman spectra of parchment. In Proceedings of the International George Papatheodorou Symposium , pp. 244-248. Edited by S. Boghosian, V. Dracopoulos, C. G. Kontoyannis & G. A. Voyiatzis. Greece:Patras Science Park.
  22. Pancoska, P., Yasui, S. C. & Keiderling, T. A. ( 1991; ). Statistical analysis of the vibrational circular dichroism of selected proteins and relationship to secondary structure. Biochemistry 30, 5089-5103.[CrossRef]
    [Google Scholar]
  23. Sawyer, L., Tollin, P. & Wilson, H. R. ( 1987; ). A comparison between the predicted secondary structures of potato virus X and papaya mosaic virus coat proteins. Journal of General Virology 68, 1229-1232.[CrossRef]
    [Google Scholar]
  24. Stubbs, G. ( 1989; ). Virus structure. In Prediction of Protein Structure and Principles of Protein Conformation , pp. 117-148. Edited by G. Fasman. New York:Plenum Press.
  25. Stubbs, G. ( 1999; ). Tobacco mosaic virus particle structure and the initiation of disassembly. Philosophical Transactions of the Royal Society B 354, 551-557.[CrossRef]
    [Google Scholar]
  26. Thomas, G. J.Jr. ( 1987; ). Viruses and nucleoproteins. In Biological Applications of Raman Spectroscopy , pp. 135-201. Edited by T. G. Spiro. New York:John Wiley & Sons.
  27. Thomas, G. J.Jr. ( 1999; ). Raman spectroscopy of protein and nucleic acid assemblies. Annual Review of Biophysics and Biomolecular Structure 28, 1-27.[CrossRef]
    [Google Scholar]
  28. Tollin, P., Wilson, H. R. & Bancroft, J. B. ( 1980; ). Further observations on the structure of particles of potato virus X. Journal of General Virology 49, 407-410.[CrossRef]
    [Google Scholar]
  29. Venyaminov, S. Y. & Yang, J. T. ( 1996; ). Determination of protein secondary structure. In Circular Dichroism and the Conformational Analysis of Biomolecules , pp. 69-107. Edited by G. D. Fasman. New York:Plenum Press.
  30. Wilson, H. R., Tollin, P., Sawyer, L., Robinson, D. J., Price, N. C. & Kelly, S. M. ( 1991; ). Secondary structures of narcissus mosaic virus coat protein. Journal of General Virology 72, 1479-1480.[CrossRef]
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-83-1-241
Loading
/content/journal/jgv/10.1099/0022-1317-83-1-241
Loading

Data & Media loading...

Most Cited This Month

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