Biopolym. Cell. 2002; 18(5):429-435.
Viruses and Cell
Comparison of capsid proteins of tobacco mosaic virus Ukrainian isolates and common strain after trypsin fragmentation
1Shevchenko T. P., 2Tkachenko T. Yu., 2Viter S. S., 2Radavsky Yu. L., 1Boyko A. L., 1Polischuk V. P.
  1. Taras Shevchenko National University of Kyiv
    64, Volodymyrska Str., Kyiv, Ukraine, 01033
  2. Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine
    1, Murmans'ka Str., Kyiv, Ukraine, 02094


The comparative analysis of tobacco mosaic virus two Ukrainian isolates (TMVch and TMVsh) and common strain (TMV VI) was carried out by means of peptide mapping of capsid protein hydrolyzed by trypsin with the following analysis of tryptic fragments using homo- and heterospecific antisera. Peptide mapping results were not shown significant differences at the peptide maps of investigated proteins with the exception of fraction 7 that was absent at TMV Ul capsid protein elution profile. The analysis of each protein tryptic fractions using virusspecific antisera revealed certain differences at the reactions of antisera with some fractions. The amino acid sequence of peptide from fraction 12 TMVch capsid protein was established. This sequence coincides completely with the polypeptide sequence of TMV Ul capsid protein at the position 72–90, however the recognition of this fragment by antisera was varied.


[1] Molecular basis of virus evolution. Eds A. Gibbs, C. H. Calisher, F. Garcia-Arenal. Cambridge: Univ. press, 1995. 603 p.
[2] Shevchenko TP, Polyschuk VP, Boiko AL. Classification Toba virus strain characteristics and diversity of tobacco mosaic virus as a typical representative of the genus. Viruses of plants: strain diversity. Kyiv: Fitosocio-Tcentr. 2002;30-43.
[3] Tyvonchuk TP, Polyschuk VP, Boiko AL. Study of strain diversity of tobacco mosaic virus in Ukraine. Agroecology and Biotechnology. Coll Sci Works. Kyiv, 1998; Iss. 2; 209-13.
[4] Practicum on general virology. Ed. IG Atabekova. Moscow: Moscow State University Press, 1981; 192 p.
[5] Tyvonchuk TP, Shevchenko OV, Boiko AL, Polyschuk VP. Comparative study of molecular and serological properties of two isolates of tobacco mosaic virus (BTM) and its typical strain (U1). Bull. Inst agr microbiol. 2000;(7):34-6.
[6] Van Regenmortel MH. The antigenicity of tobacco mosaic virus. Philos Trans R Soc Lond B Biol Sci. 1999;354(1383):559-68.
[7] Westhof E, Altschuh D, Moras D, Bloomer AC, Mondragon A, Klug A, Van Regenmortel MH. Correlation between segmental mobility and the location of antigenic determinants in proteins. Nature. 1984 Sep 13-19;311(5982):123-6.
[8] Moudallal ZA, Briand JP, Regenmortel MH. A major part of the polypeptide chain of tobacco mosaic virus protein is antigenic. EMBO J. 1985;4(5):1231-5.
[9] Bhyravbhatla B, Watowich SJ, Caspar DL. Refined atomic model of the four-layer aggregate of the tobacco mosaic virus coat protein at 2.4-A resolution. Biophys J. 1998;74(1):604-15.
[10] Colman PM, Air GM, Webster RG, Varghese JN, Baker AT, Lentz MR, Tulloch PA, Laver WG. How antibodies recognize virus proteins. Immunol Today. 1987;8(11):323-6.
[11] Van Regenmortel MH, Altschuh D, Zeder-Lutz G. Tobacco mosaic virus: a model antigen to study virus-antibody interactions. Biochimie. 1993;75(8):731-9.