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. 1995 May;7(5):549–559. doi: 10.1105/tpc.7.5.549

Long-distance movement factor: a transport function of the potyvirus helper component proteinase.

S Cronin 1, J Verchot 1, R Haldeman-Cahill 1, M C Schaad 1, J C Carrington 1
PMCID: PMC160803  PMID: 7780307

Abstract

Transport of viruses from cell to cell in plants typically involves one or more viral proteins that supply dedicated movement functions. Transport from leaf to leaf through phloem, or long-distance transport, is a poorly understood process with requirements differing from those of cell-to-cell movement. Through genetic analysis of tobacco etch virus (TEV; potyvirus group), a novel long-distance movement factor was identified that facilitates vascular-associated movement in tobacco. A mutation in the central region of the helper component proteinase (HC-Pro), a TEV-encoded protein with previously described activities in aphid-mediated transmission and polyprotein processing, inactivated long-distance movement. This mutant virus exhibited only minor defects in genome amplification and cell-to-cell movement functions. In situ histochemical analysis revealed that the mutant was capable of infecting mesophyll, bundle sheath, and phloem cells within inoculated leaves, suggesting that the long-distance movement block was associated with entry into or exit from sieve elements. The long-distance movement defect was specifically complemented by HC-Pro supplied in trans by a transgenic host. The data indicate that HC-Pro functions in one or more steps unique to long-distance transport.

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Selected References

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  1. A simple and general method for transferring genes into plants. Science. 1985 Mar 8;227(4691):1229–1231. doi: 10.1126/science.227.4691.1229. [DOI] [PubMed] [Google Scholar]
  2. Atreya C. D., Atreya P. L., Thornbury D. W., Pirone T. P. Site-directed mutations in the potyvirus HC-Pro gene affect helper component activity, virus accumulation, and symptom expression in infected tobacco plants. Virology. 1992 Nov;191(1):106–111. doi: 10.1016/0042-6822(92)90171-k. [DOI] [PubMed] [Google Scholar]
  3. Atreya C. D., Pirone T. P. Mutational analysis of the helper component-proteinase gene of a potyvirus: effects of amino acid substitutions, deletions, and gene replacement on virulence and aphid transmissibility. Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11919–11923. doi: 10.1073/pnas.90.24.11919. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Atreya C. D., Raccah B., Pirone T. P. A point mutation in the coat protein abolishes aphid transmissibility of a potyvirus. Virology. 1990 Sep;178(1):161–165. doi: 10.1016/0042-6822(90)90389-9. [DOI] [PubMed] [Google Scholar]
  5. Atreya P. L., Atreya C. D., Pirone T. P. Amino acid substitutions in the coat protein result in loss of insect transmissibility of a plant virus. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7887–7891. doi: 10.1073/pnas.88.17.7887. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Beck D. L., Guilford P. J., Voot D. M., Andersen M. T., Forster R. L. Triple gene block proteins of white clover mosaic potexvirus are required for transport. Virology. 1991 Aug;183(2):695–702. doi: 10.1016/0042-6822(91)90998-q. [DOI] [PubMed] [Google Scholar]
  7. Carrington J. C., Freed D. D. Cap-independent enhancement of translation by a plant potyvirus 5' nontranslated region. J Virol. 1990 Apr;64(4):1590–1597. doi: 10.1128/jvi.64.4.1590-1597.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Carrington J. C., Freed D. D., Oh C. S. Expression of potyviral polyproteins in transgenic plants reveals three proteolytic activities required for complete processing. EMBO J. 1990 May;9(5):1347–1353. doi: 10.1002/j.1460-2075.1990.tb08249.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Carrington J. C., Freed D. D., Sanders T. C. Autocatalytic processing of the potyvirus helper component proteinase in Escherichia coli and in vitro. J Virol. 1989 Oct;63(10):4459–4463. doi: 10.1128/jvi.63.10.4459-4463.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Citovsky V., Knorr D., Schuster G., Zambryski P. The P30 movement protein of tobacco mosaic virus is a single-strand nucleic acid binding protein. Cell. 1990 Feb 23;60(4):637–647. doi: 10.1016/0092-8674(90)90667-4. [DOI] [PubMed] [Google Scholar]
  11. Citovsky V., Wong M. L., Shaw A. L., Prasad B. V., Zambryski P. Visualization and characterization of tobacco mosaic virus movement protein binding to single-stranded nucleic acids. Plant Cell. 1992 Apr;4(4):397–411. doi: 10.1105/tpc.4.4.397. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Dawson W. O. Tobamovirus-plant interactions. Virology. 1992 Feb;186(2):359–367. doi: 10.1016/0042-6822(92)90001-6. [DOI] [PubMed] [Google Scholar]
  13. Deom C. M., Lapidot M., Beachy R. N. Plant virus movement proteins. Cell. 1992 Apr 17;69(2):221–224. doi: 10.1016/0092-8674(92)90403-y. [DOI] [PubMed] [Google Scholar]
  14. Ding B., Haudenshield J. S., Hull R. J., Wolf S., Beachy R. N., Lucas W. J. Secondary plasmodesmata are specific sites of localization of the tobacco mosaic virus movement protein in transgenic tobacco plants. Plant Cell. 1992 Aug;4(8):915–928. doi: 10.1105/tpc.4.8.915. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Dolja V. V., Herndon K. L., Pirone T. P., Carrington J. C. Spontaneous mutagenesis of a plant potyvirus genome after insertion of a foreign gene. J Virol. 1993 Oct;67(10):5968–5975. doi: 10.1128/jvi.67.10.5968-5975.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Dolja V. V., McBride H. J., Carrington J. C. Tagging of plant potyvirus replication and movement by insertion of beta-glucuronidase into the viral polyprotein. Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10208–10212. doi: 10.1073/pnas.89.21.10208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Fujiwara T., Giesman-Cookmeyer D., Ding B., Lommel S. A., Lucas W. J. Cell-to-Cell Trafficking of Macromolecules through Plasmodesmata Potentiated by the Red Clover Necrotic Mosaic Virus Movement Protein. Plant Cell. 1993 Dec;5(12):1783–1794. doi: 10.1105/tpc.5.12.1783. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Giesman-Cookmeyer D., Lommel S. A. Alanine scanning mutagenesis of a plant virus movement protein identifies three functional domains. Plant Cell. 1993 Aug;5(8):973–982. doi: 10.1105/tpc.5.8.973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Klein P. G., Klein R. R., Rodríguez-Cerezo E., Hunt A. G., Shaw J. G. Mutational analysis of the tobacco vein mottling virus genome. Virology. 1994 Nov 1;204(2):759–769. doi: 10.1006/viro.1994.1591. [DOI] [PubMed] [Google Scholar]
  20. Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 1987;154:367–382. doi: 10.1016/0076-6879(87)54085-x. [DOI] [PubMed] [Google Scholar]
  21. Li X. H., Carrington J. C. Complementation of tobacco etch potyvirus mutants by active RNA polymerase expressed in transgenic cells. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):457–461. doi: 10.1073/pnas.92.2.457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Noueiry A. O., Lucas W. J., Gilbertson R. L. Two proteins of a plant DNA virus coordinate nuclear and plasmodesmal transport. Cell. 1994 Mar 11;76(5):925–932. doi: 10.1016/0092-8674(94)90366-2. [DOI] [PubMed] [Google Scholar]
  23. Oh C. S., Carrington J. C. Identification of essential residues in potyvirus proteinase HC-Pro by site-directed mutagenesis. Virology. 1989 Dec;173(2):692–699. doi: 10.1016/0042-6822(89)90582-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Pascal E., Sanderfoot A. A., Ward B. M., Medville R., Turgeon R., Lazarowitz S. G. The geminivirus BR1 movement protein binds single-stranded DNA and localizes to the cell nucleus. Plant Cell. 1994 Jul;6(7):995–1006. doi: 10.1105/tpc.6.7.995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Petty I. T., French R., Jones R. W., Jackson A. O. Identification of barley stripe mosaic virus genes involved in viral RNA replication and systemic movement. EMBO J. 1990 Nov;9(11):3453–3457. doi: 10.1002/j.1460-2075.1990.tb07553.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Restrepo-Hartwig M. A., Carrington J. C. The tobacco etch potyvirus 6-kilodalton protein is membrane associated and involved in viral replication. J Virol. 1994 Apr;68(4):2388–2397. doi: 10.1128/jvi.68.4.2388-2397.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Riechmann J. L., Laín S., García J. A. Highlights and prospects of potyvirus molecular biology. J Gen Virol. 1992 Jan;73(Pt 1):1–16. doi: 10.1099/0022-1317-73-1-1. [DOI] [PubMed] [Google Scholar]
  28. Taliansky M. E., García-Arenal F. Role of cucumovirus capsid protein in long-distance movement within the infected plant. J Virol. 1995 Feb;69(2):916–922. doi: 10.1128/jvi.69.2.916-922.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Thornbury D. W., Patterson C. A., Dessens J. T., Pirone T. P. Comparative sequence of the helper component (HC) region of potato virus Y and a HC-defective strain, potato virus C. Virology. 1990 Oct;178(2):573–578. doi: 10.1016/0042-6822(90)90356-v. [DOI] [PubMed] [Google Scholar]
  30. Waigmann E., Lucas W. J., Citovsky V., Zambryski P. Direct functional assay for tobacco mosaic virus cell-to-cell movement protein and identification of a domain involved in increasing plasmodesmal permeability. Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1433–1437. doi: 10.1073/pnas.91.4.1433. [DOI] [PMC free article] [PubMed] [Google Scholar]

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