Phosphorylation of structural viral proteins — essential condition for plant viruses reproduction

Authors

  • L.O. Maksymenko Danylo Zabolotny Institute of Microbiology and Virology
  • N.Y. Parkhomenko Danylo Zabolotny Institute of Microbiology and Virology

DOI:

https://doi.org/10.15407/dopovidi2021.05.107

Keywords:

potato X-virus, structural protein of PVX, phosphorylation, protein kinases

Abstract

Phosphorylation of proteins is characteristic for structural proteins of cauliflower mosaic virus, potato virus A (PVA), plum beetle virus, and others. This process is necessary for the development of viral infection in the plant. Potato virus X (PVX) is a typical member of the genus Potexvirus. It was found that the structural viral protein of potato virus X is able to phosphorylation in a standard incubation medium in vitro, which contained (gamma-32P)ATP. In contrast, PVX protein in a standard incubation medium in the presence of (alpha-32P)ATP is not phosphorylated. Thus, the final ATP phosphate plays a major role in the phosphorylation of the structural PVX protein. Phosphorylated PVX protein in the system in vivo was detected by exposing nitrocellulose with immunoblot on X-ray film PM-1. As a result, an autograph of the phosphorylated in vivo structural protein PVX was obtained. The concentration of Ca and EDTA ions in the in vitro phosphorylation system affects the process of phosphorylation of the structural protein of PVX . The presence of 10 mM EDTA and 10 mM CaCl2 in the in vitro phosphorylation system inhibited the phosphorylation process of the PVX structural protein. The phenomenon of phosphorylation of the structural protein of PVX is probably used in the processes of virus reproduction in an infected cell.

Downloads

Download data is not yet available.

References

Ivanov, K. I., Puustinen, P., Merits, A., Saarma, M. & Makinen, K. (2001). Phosphorylation down-regulates the RNA binding function of the coat protein of potato virus A. J. Biol. Chem., 276, pp. 13530-13540. https://doi.org/10.1074/jbc.M009551200

Law, L. M., Everitt, J. C., Beatch, M. D., Holmes, C. F. & Hobman, T. C. (2003). Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication. J. Virol., 77, pp. 1764-1771. https://doi.org/10.1128/jvi.77.3.1764-1771.2003

Makarov, V. V., Iconnicova, A. Y., Guseinov, M. A., Vishnichenko, V. K. & Kalinina, N. O. (2012). In vitro phosphorylation of the N-terminal half of hordeivirus movement protein. Biochemistry (Mosc.), 77, pp. 1072-1081. https://doi.org/10.1134/S0006297912090155

Atabekov, J. G., Rodionova, N. P., Karpova, O. V., Kozlovsky, S. V., Novikov, V. K. & Arkhipenko, M. V. (2001). Translational activation of encapsidated potato virus X RNA by coat protein phosphorylation. Virology, 286, pp. 466-474. https://doi.org/10.1006/viro.2001.1013

Koenig, H., Tremaine, J. H. & Shepard, J. F. (1978). In situ degradation of the protein chain of potato virus X at the N- and C-termini. J. gen. Virol., 38, pp. 329-337. https://doi.org/10.1099/0022-1317-38-2-329

Wu, G. & Bruening, G. (1971). Two proteins from cowpea mosaic virus. Virology, 46, No. 3, pp. 596-612. https://doi.org/10.1016/0042-6822(71)90063-8

Shepard, J. F. & Secor, G. A. (1969). Detection of potato virus X in infected plant tissue by radial and double-diffusion tests in agar. Phytopathology, 59, No. 12, pp. 1838-1844.

Towbin, H., Staehelin T. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA, 76, No. 9, pp. 4350-4354. https://doi.org/10.1073/pnas.76.9.4350

Menissier-De Murcia, J., Geldreich, A. & Lebeurier, J. (1986). Evidence for a protein kinase activity associated with purified particles of cauliflower mosaic virus. J. gen. Virol., 67, pp. 1885-1891. https://doi.org/10.1099/0022-1317-67-9-1885

Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacterio - phage T4. Nature, 227, No. 5259, pp. 680-685. https://doi.org/10.1038/227680a0

Oparka, K. J., Roberts, A. G., Roberts, I. M., Prior, D. A. M. & Santa Crus, S. (1996). Viral coat protein is targeted to, but does not gate, plasmodesmata during cell-to-cell movement of potato virus X. Plant J., 10, pp. 805-813. https://doi.org/10.1046/j.1365-313X.1996.10050805.x

Karpova, O. V., Rodionova, N. P., Ivanov, K. I., Kozlovsky, S. V., Dorokhov, Yu. L. & Atabekov, I. G. (1999). Phosphorylation of tobacco mosaic virus movement protein abolishes its translation repressing ability. Virology, 261, pp. 20-24. https://doi.org/10.1006/viro.1999.9842

Didenko, L. F., Maksymenko, L. A. & Parkhomenko, N. I. (1993). In vitro phosphorylation of informosome proteins from leaves of stramonium infected with potato X-virus. Mikrobiol. Zhurn., 55, No. 2, pp. 68-74 (in Russian).

Fellers, J., Wan, J., Hong, Y., Collins, G. B. & Hunt, A. G. (1998). In vitro interactions between a potyvirusencoded, genome-linked protein and RNA-dependent RNA polymerase. J. gen. Virol., 79, pp. 2043-2049. https://doi.org/10.1099/0022-1317-79-8-2043

Watanabe, Y., Ogawa, T. & Okada, Y. (1992). In vivo phosphorylation of the 30-kDa protein of tobacco mosaic virus. FEBS Lett., 313, pp.181-184. https://doi.org/10.1016/0014-5793(92)81440-w

Published

27.10.2021

How to Cite

Maksymenko, L., & Parkhomenko, N. (2021). Phosphorylation of structural viral proteins — essential condition for plant viruses reproduction. Reports of the National Academy of Sciences of Ukraine, (5), 107–113. https://doi.org/10.15407/dopovidi2021.05.107