A A Slavokhotova

Publications (5)2.16 Total impact

• Article: Antimutagenic activity of wheat β-purothionin Tk-AMP-BP

  T. I. Odintsova, I. M. Vassilieva, T. V. Korostyleva, L. L. Utkina, A. A. Slavokhotova, E. A. Rogozhin, A. N. Shiyan, V. A. Pukhalskii, G. D. Zasukhina
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  ABSTRACT: Antimutagenic activity on human RD cells was studied for β-purothionin Tk-AMP-BP isolated from seeds of wheat Triticum kiharae, which has high stress resistance. Cadmium chloride at 5 × 10−6 M was used as a mutagen. The numbers of DNA breaks in mutagen-treated and intact cells were inferred from the single-stranded to double-stranded DNA ratio and expressed as protection coefficients. The protective effect was simultaneously assayed for aqueous plant extracts known to possess antioxidant properties. Wheat thionin was the most active among all of the antimutagens examined; its protection coefficient reached 85–88% at micromolar peptide concentrations (8–32 μg/ml). Thus, wheat β-purothionin was for the first time demonstrated to be highly efficient in protecting human cell DNA from the damaging effect of cadmium chloride.
  Russian Journal of Genetics 04/2012; 47(9):1128-1131. · 0.43 Impact Factor
• Article: Heterologous expression of a synthetic gene encoding a novel hevein-type antimicrobial peptide of Leymus arenarius in Escherichia coli cells

  L. L. Utkina, E. O. Zhabon, A. A. Slavokhotova, E. A. Rogozhin, A. N. Shiyan, E. V. Grishin, Ts. A. Egorov, T. I. Odintsova, V. A. Pukhal’skiy
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  ABSTRACT: A novel antifungal peptide, LAMP-1a, was isolated from sand-elymus (Leymus arenarius) seeds. Expression of a synthetic gene encoding this peptide in Escherichia coli cells was obtained. The target peptide was expressed as a fusion with thioredoxin. Identity of the recombinant peptide to native LAMP-1a was confirmed by chromatography, mass spectrometry, and amino acid sequencing. LAMP-1a displayed a high inhibitory activity in respect of a number of phytopathogenic fungi in in vitro assays, which opens up possibilities for the gene encoding it to be used for genetic transformation of plants and for engineering pathogen-resistant crops
  Russian Journal of Genetics 04/2012; 46(12):1449-1454. · 0.43 Impact Factor
• Article: Specifics of the coat protein gene in Russian strains of the cucumber green mottle mosaic virus

  A. A. Slavokhotova, E. N. Andreeva, A. N. Shijan, T. I. Odintsova, V. A. Pukhalskij
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  ABSTRACT: The primary structure of the coat protein (CP) gene was examined for pathogenic strain MS-1 and vaccine strain VIROG-43M of the cucumber green mottle mosaic virus (CGMMV). In CP amino acid composition, strains MS-1 and VIROG-43M are typical representatives of CGMMV: their CPs have 98–100% homology to CPs of other tobamoviruses of the group. The CP gene has the same nucleotide composition in pathogenic MS-1 and vaccine VIROG-43M, indicating that strain attenuation is not determined by this gene. The CP amino acid sequences of the two Russian strains are fully identical to the CP sequences of two Greek strains, GR-3 and GR-5. However, the nucleotide sequences of their genes differ in 13 bp, testifying to the difference between the Russian and Greek strains.
  Russian Journal of Genetics 04/2012; 43(11):1221-1226. · 0.43 Impact Factor
• Article: [Heterologous expression of a synthetic gene encoding a novel hevein-type antimicrobial peptide of Leymus arenarius in Escherichia coli cells].

  L L Utkina, E O Zhabon, A A Slavokhotova, E A Rogozhin, A N Shiian, E V Grishin, Ts A Egorov, T I Odintsova, V A Pukhal'skiĭ
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  ABSTRACT: A novel antifungal peptide, LAMP-Ia, was isolated from sand-elymus (Leymus arenarius) seeds. Expression of a synthetic gene encoding this peptide in Escherichia coli cells was obtained. The target peptide was expressed as a fusion with thioredoxin. Identity of the recombinant peptide to native LAMP-Ia was confirmed by chromatography, mass spectrometry, and amino acid sequencing. LAMP-Ia displayed a high inhibitory activity in respect of a number of phytopathogenic fungi in in vitro assays, which opens up possibilities for the gene encoding it to be used for genetic transformation of plants and for engineering pathogen-resistant crops.
  Genetika 12/2010; 46(12):1645-51. · 0.44 Impact Factor
• Article: [Specifics of the coat protein gene in Russian strains of the cucumber green mottle mosaic virus].

  A A Slavokhotova, E N Andreeva, A N Shiian, T I Odintsova, V A Pukhal'skiĭ
  [show abstract] [hide abstract]
  ABSTRACT: The primary structure of the coat protein (CP) gene was examined for pathogenic strain MS-1 and vaccine strain VIROG-43M of the cucumber green mottle mosaic virus (CGMMV). In CP amino acid composition, strains MS-1 and VIROG-43M are typical representatives of CGMMV: their CPs have 98-100% homology to CPs of other tobamoviruses of the group. The CP gene has the same nucleotide composition in pathogenic MS-1 and vaccine VIROG-43M, indicating that strain attenuation is not determined by this gene. The CP amino acid sequences of the two Russian strains are fully identical to the CP sequences of two Greek strains, GR-3 and GR-5. However, the nucleotide sequences of their genes differ in 13 bp, testifying to the difference between the Russian and Greek strains.
  Genetika 12/2007; 43(11):1461-7. · 0.44 Impact Factor