doi: 10.15389/agrobiology.2016.5.705eng

UDC 632.4:632.938.1:57.053:577.19:635.262



O.G. Kulikova1, D.I. Mal'tsev1, M.I. Kartashov2, A.P. Il’ina 1,
V.P. Yamskova3, I.A. Yamskov1

1A.N. Nesmeyanov Institute of Organoelement Compounds RAS, Federal Agency of Scientific Organizations, 28, ul. Vavilova, Moscow, 119991 Russia,
2All-Russian Research Institute of Phytopathology, Federal Agency of Scientific Organizations, 5, Institute, pos. Bol’shie Vyazemy, Odintsovskii Region, Moscow Province, 143050 Russia,
3N.K. Kol’tsov Institute of Developmental Biology RAS, Federal Agency of Scientific Organizations, 26, ul. Vavilova, Moscow, 119334 Russia,

ORCID:Kulikova O.G.
ORCID:Mal'tsev D.I.
ORCID:Kartashov M.I.

Received May 15, 2016


Garlic (Allium sativum L., family Amaryllidaceae) plants are usually used because of bioactive compounds in their leaves and bulbs. Compounds extracted from this plant are often able to protect against some diseases. There is not enough information about infusions garlic extracts that can be used for plant pathogen control. Creating effective biologicals to protect plants against various diseases is an urgent task to improve crop yields. In this work, the bioactive compounds possessing activity against some phytopathogens were isolated from garlic plant bulbs Allium sativum L. A complex of lectin-allinase and peptide with molecular weight of 4392 Da was obtained from A. sativum bulbs. This complex described in literature before is consisted of allinase enzyme (molecular weight 54 kDa) and mannose-specific garlic lectin (ASA) with molecular weight of 6.4 kDa, and is formed when the bulb tissues are ground. Since, to our knowledge, no data on the biological action of this complex were reported before, we studied its activity against the pathogen of rice blast Magnaporthe grisea. This study showed that the lectin-allinaza complex had no suppressive effect on the pathogen spore germination (spore germination both in control and under treatment was at the 80-90 % level), but reduced the number of necrosis on treated leaves of rice (the percentage of uninfected leaves increased from 15 % in control to 75 %). Thus, the complex did not affect M. grisea directly, but protected plants upon their infection by this pathogenic fungus. These findings suggest that lectin-allinaza complex isolated from garlic bulbs is able to induce resistance to M. grisea, probably by activation of plant defense responses. The ability of obtained peptide not described in literature before to inhibit action of B. sorokiniana, the causative agent of Helminthosporium root rot and barley leaf blotch, at concentration corresponding to 10-11 mg protein/ml, was shown on wheat and barley leaves. Since the peptide 4392 Da did not inhibit the growth of B. sorokiniana colonies in vitro, it can be assumed that the peptide is capable of activating the protective functions of the plant during the pathogen infection. When evaluating the effect of the peptide 4392 Da on seed germination and growth stimulation in peas, cucumber, mustard, sunflower and garlic, the germination of garlic seeds increased by 13.6 % (р < 0.01), while 65.5 % (р < 0.01) increase in the length of its stems and a four-fold increase of the root length were observed, but the peptide had no effect on seeds and sprouts of the other crops tested. Thus, the resulting substances do not possess phytotoxicity, and due to its high activity at low concentrations show very low discharge at its application. Moreover, by virtue of its origin they are absolutely harmless for humans and animals and are environmentally safe technology of plant protection, which is especially important in modern agriculture.

Keywords: garlic, Allium sativum L., lectin, allinase, rice blast, rice, peptide, helmintospotium, growth stimulation.


Full article (Rus)

Full text (Eng)



  1. Van Damme E.J.M., Allen A.K., Peumans W.J. Related mannose-specific lectins from different species of the family Amaryllidaceae. Physiologia Plantarum, 1998, 73: 52-57 CrossRef
  2. Lanzotti V., Scala F., Bonanomi G. Compounds from Allium species with cytotoxic and antimicrobial activity. Phytochemistry Reviews, 2014, 13: 769-791 CrossRef
  3. Kopec A., Platkowska E., Leszczynska T., Sikora E. Healthy properties of garlic. Current Nutrition & Food Science, 2013, 9(1): 59-64 CrossRef
  4. Van Damme E.J.M., Peumans W.J., Barre A., Rouge P. Plant lectins: a composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles. Crit. Rev. Plant Sci., 1998, 17: 575-692 CrossRef
  5. Borlinghaus J., Albrecht F., Gruhlke C.H., Nwachukwu I.D., Slusarenko A.J. Allicin: Chemistry and biological properties. Molecules, 2014, 19: 12951-12618 CrossRef
  6. Silagy C.A., Neil H.A. A meta-analysis of the effect of garlic on blood pressure. J. Hypertens., 1994, 12: 463-468 CrossRef
  7. Harris J.C., Cottrell S.L., Plummer S., Lloyd D. Antimicrobial properties of Allium sativum (garlic). Applied Microbiology and Biotechnology, 2001, 57: 282-286 CrossRef
  8. Lin X.Y., Liu J.Z., Milner J.A. Dietary garlic suppresses DNA adducts caused by N-nitroso compounds. Carcinogenesis, 1994, 15: 349-352 CrossRef
  9. Warshafsky S., Kamer R.S., Sivak S.L. Effect of garlic on total serum cholesterol. A meta-analysis. Ann. Intern. Med., 1993, 119(7): 599-605 CrossRef
  10. Kiesewetter H., Jung F., Pindur G., Jung E.M., Mrowietz C., Wenzel E. Effect of garlic on thrombocyte aggregation, microcirculation, and other risk factors. Int. J. Clin. Pharmacol. Ther. Toxicol., 1991, 29: 151-155.
  11. Dorant E., Van den Brandt P.A., Goldbohm R.A., Hermus R.J., Sturmans F. Garlic and its significance for the prevention of cancer in humans: A critical view. Br. J. Cancer, 1993, 67: 424-429 CrossRef
  12. Smirnova A.V. Puti povysheniya ekologicheskoi bezopasnosti pri vozdelyvanii kapusty v Priamur'e. Avtoreferat kandidatskoi dissertatsii [Ways to improve environmental safety at cabbage cultivation in the Amur region. PhD Thesis]. Khabarovsk, 2011 (in Russ.).
  13. Bondarenko N.V. Biologicheskaya zashchita rastenii [Bioprotection of plants]. Moscow, 1986 (in Russ.).
  14. Velikanov L.L., Sidorova I.I. Ekologicheskie problemy zashchity rastenii ot boleznei. Itogi nauki i tekhniki. Tom 6. [Ecological problems of plant protecting from disease. Advances in science and technology. V. 6]. Moscow, 1988 (in Russ.).
  15. Gren'e A., Pepen R. Proizvodnye tetragidrofurana, sposob ikh polucheniya i sposob bor'by s gribkami. RU 2079274. MPK6A01N43/08, A01N43/50, A01N43/707, C07D307/18, C07D307/20, C07D405/06. Applicant Rhône-Poulenc Agrochimie (FR) [Tetrahydrofuran derivatives, their preparation and use against fungus. Appl. April 22, 1987. Publ. May 20, 1997] (in Russ.).
  16. Egorov N.S. Osnovy ucheniya ob antibiotikakh [Theory of antibiotics — the fundamenals]. Moscow, 1986 (in Russ.).
  17. Knauf-Baiter G., Tsurflyu R., Gzell B. Sposobbor'bysfitopatogennymiboleznyamikul'turnykhrastenii, fungitsidnayakompozitsiya. RU 2193847. MPK A01N37/50, A01N37/52, A01N43/40, A01N43/54, A01N43/653, A01N43/828 [A method to control phytopathogenic diseases of cultivated plants, a fungicide composition. Applicant Bayer AG (DE). Appl. April 22, 1997. Publ. August 27, 1998] (in Russ.).
  18. Krasnov M.S., Yamskova V.P., Kulikova O.G., Il'ina A.P., Margasyuk D.V., Rybakova E.Yu., Yamskov I.A. Prikladnaya biokhimiya i mikrobiologiya, 2011, 47(2): 146-153 (in Russ.).
  19. Kulikova O.G., Yamskova V.P., Il'ina A.P., Margasyuk D.V., Molyavka A.A., YAmskov I.A. Prikladnaya biokhimiya i mikrobiologiya, 2011, 47(4): 1-5 (in Russ.).
  20. Rabinkov A., Wilchek M., Mirelman D. Alliinase (alliinlyase) from garlic (Alliium sativum) is glycosylated at ASN 146 and forms a complex with a garlic mannose-specific lectin. Glycoconjugate J., 1995, 12: 690-698 CrossRef
  21. Smeets K., Van Damme E.J., Van Leuven F., Peumans W.J. Isolation and characterization of lectins and lectin-alliinase complexes from bulbs of garlic (Allium sativum) and ramsons (Allium ursinum). Glycoconjugate J., 1997, 14(3): 331-343 CrossRef
  22. Mirica A.K., Lockett M.R., Snyder P.W., Shapiro N.D., Mack E.T., Nam S., Whitesides G.M. Selective precipitation and purification of monovalent proteins using oligovalent ligands and ammonium sulfate. Bioconjugate Chem., 2012, 23(2): 293-299 CrossRef
  23. Lapikova V.P., Aver'yanov A.A., Pasechnik T.D. Mikologiya i fitopatologiya, 1995, 29(2): 44-47 (in Russ.).
  24. Latterell F.M., Marchetti M.A., Grove B.R. Co-ordination of effort to establish an international system for race identification in Pyricularia oryzae. In: The rice blast disease. The Johns Hopkins University Press, Baltimore, 1965.
  25. Webster T.M. The southern states 10 most common and troublesome weeds in rice. Proceedings Southern Weed Science Society, 2000, 53: 247-274.
  26. Pyzhikova G.V., Sanina A.A., Suprun L.M., Kurakhtanova T.I., Gogaeva T.I., Meparishvili S.U., Antsiferova L.V., Kuznetsov N.S., Ignatov A.N., Kuz'michev A.A. Metody otsenki ustoichivosti selektsionnogo materiala i sortov pshenitsy k septoriozu [Assessment of resistance to septoriosis in wheat breeding forms and varieties]. Moscow, 1989 (in Russ.).
  27. Skladnev D.A. Metilotrofnye bakterii kak osnova biotekhnologicheskogo polucheniya stabil'no mechenykh biologicheski aktivnykh soedinenii. Doktorskaya dissertatsiya [Methylotrophic bacteria for biotechnological production of stable labeled bioactive compounds. DSci Thesis]. Moscow, 2000 (in Russ.).
  28. Oparin P.B., Mineev K.S., Dunevsky Ya.E., Arseniev A.S., Belozersky M.A., Grishin E.V., Egorov T.A., Vassilevski A.A. Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defense peptides. Biochem. J., 2012, 446(1): 69-77 CrossRef
  29. Slavokhotova A.A., Rogozhin E.A., Musolyamov A.K., Andreev Y.A., Opa-
    rin P.B., Berkut A.A., Vassilevski A.A., Egorov T.A., Grishin T.V., Odintsova T.I. Novel antifungal a-hairpinin peptide from Stellaria media seeds: structure, biosynthesis, gene structure and evolution. Plant Mol. Biol., 2014, 84(1-2): 189-202 CrossRef 
  30. Egorov T.A., Odintsova T.I., Pukhalsky V.A., Grishin E.V. Diversity of wheat antimicrobial peptide. Peptides, 2005, 26: 2064-2073 CrossRef
  31. Odintsova T.I., Egorov Ts.A., Musolyamov A.Kh., Odintsova M.S., Pukhalsky V.A., Grishin E.V. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes. Biochimie, 2007, 89: 605-612 CrossRef