THE PHYSIOLOGICAL PROPERTIES OF PLANT LECTINS AS A PREREQUISITE FOR THEIR APPLICATION IN BIOTECHNOLOGY

  • Нинэль (Ninel) Ефимовна (Efimovna) Павловская (Pavlovskaya) Orel State Agrarian University name N.V. Parahina Email: ninel.pavlovsckaya@yandex.ru
  • Ирина Николаевна Гагарина (Gagarina) Orel State Agrarian University name N.V. Parahina Email: i-gagarina@list.ru
Keywords: lectins, proteins, hemagglutinins activity, hydrocarbonic proteins, toxic components, grain protein complex, the inhibitory effect

Abstract

The purpose of this review is a generalization of the available current data on plant lectins and their characteristic area of use in biotechnology.

The review provides current data on the classification of lectins, the functional role of plant lectins, especially legumes, toxicity, nutritional problems and assumptions used in different areas of biotechnology production, including the creation of means of protection against pathogens in plant and medicine.

Glyco-binding properties and a variety of molecular structures observed in lectins, provided them with a wide range of biological activity, and provided them with the ability to serve as a tool for biotechnological applications.

Plant lectins have a multifunctional role: involved in cell defense reactions against pathogens and herbivorous insects, as well as have an impact on symbiosis with micro-organisms play a key role in establishing symbiotic relationships with rhizobia.

The insecticidal properties of lectins are used in genetic engineering to create stable forms of plants from insect pests, as well as bacterial and viral pathogens.

The interaction of lectins with carbohydrates opens the prospects of their application in critical areas such as immunology, oncology and medicine for the diagnosis and treatment of various diseases. They may also be used as markers for determining the blood groups.

Lectins reduce food and feed value of many cultures and cause allergies.

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Author Biographies

Нинэль (Ninel) Ефимовна (Efimovna) Павловская (Pavlovskaya), Orel State Agrarian University name N.V. Parahina
доктор биологических наук, профессор, заведующая кафедрой биотехнологии
Ирина Николаевна Гагарина (Gagarina), Orel State Agrarian University name N.V. Parahina
кандидат сельскохозяйственных наук, доцент кафедры биотехнологии

References

Ana C. Ribeiro, Sara V. Monteiro, Belmira M. Carrapiço, Ricardo B. Ferreira. Are Vicilins Another Major Class of Legume Lectins // Molecules, 2014. Vol. 19. Pp. 20350–20373.

Van Dame J.M., Peumans W.J., Pustai A., Bardocz S. Handbook of plant lectins: properties and biomedical applica-tions. Chichester etc.: John Willey and Sons, 1998. P. 451.

Rüdiger H., Gabius H., Review J. Plant lectins: Occurrence, biochemistry, functions and applications // Glycoconjugate. 2001. Vol. 18. Pp. 589–613.

Sandro Mascena Gomes Filho, Juscélio Donizete Cardoso, Katya Anaya, Edilza Silva do Nascimento, José Thalles Jucelino Gomes de Lacerda, Roberto Mioso, Tatiane Santi Gadelha, Carlos Alberto de Almeida Gadelha. Lectins actual status on properties and biological activities // Molecules. 2015. Vol. 20. Pp. 348–357.

Eri Kenmochi, Syed Rashel Kabir, Tomohisa Ogawa, Ryno Naude, Hiroaki Tateno, Jun Hirabayashi, Koji Muramoto. Isolation and Biochemical Characterization of Apios Tuber Lectin // Molecules. 2015. Vol. 20. Pp. 987–1002.

Лектины [Электронный ресурс]. URL: http://www.horosheezdorovje.ru/lektiny-1/.

Komath S.S., Kavitha M., Swamy M.J. Beyond carbohydrate binding: new directions in plant lectin research // Organic Biomolecular Chemistry. 2006. Vol. 4. Pp. 973–988.

Игнатов В.В. Углеводузнающие белки – лектины // Биология (Соровский образовательный журнал). 1997. №2. С. 15–20.

Косенко Л.В. Сортовые различия углеводсвязывающих свойств лектинов из семян Vicia Jabe // Физиология растений. 2002. Т. 49. №6. С. 859–864.

Косенко Л.В. Сравнительная характеристика углеводсвязывающих свойств лектинов из семян бобовых расте-ний // Физиология растений. 2002. Т. 49. №5. С. 718–724.

Kass H. Some properties of carbohydrate bilding protein (lectins) solubilizied from cell wall of Phaseolis aureus // Plan-ta. 1996. Vol. 130. N2. Pp. 169–214.

Марков Е.Ю., Хавкин Э.Е. Лектины растений: предполагаемые функции // Физиология растений. 1983. Т. 30, вып. 5. С. 852–867.

Maria Lígia R., Macedo, Caio F.R., Carolina T. Oliveira Insecticidal Activity of Plant Lectins and Potential Application in Crop Protection // Molecules. 2015. Vol. 20. Pp. 2014–2033

Peumans W.J., van Damme E. Lectins as plant defense proteins // Plant Physiol. 1995. Vol. 109. Pp. 347–352

Van Damme E.J., Lannoo N., Fouquaert E., Peumans W.J. The identification of inducible cytoplasmic/nuclear carbohy-drate-binding proteins urges to develop novel concepts about the role of plant lectins // Glycoconj. 2003. Vol. 20. Рp. 449–460

Van Damme E.J.M., Peumans W.J., Barre A., Rouge P. Plant lectins: A composite of several distinct families of struc-turally and evolutionary related proteins with diverse biological roles // Crit. Rev. Plant Sci. 1998. Vol. 17. Pp. 575–692.

Antonyuk V.O. Lectins and their stock sources. Lviv, 2005. 554 p.

Zhao J.K., Wang H.X., Ng T.B. Purification and characterization of a novel lectin from the toxic wild mushroom Inocy-be umbrinella // Toxicon. 2009. Vol. 53. Pp. 360–366.

Li Y.R., Liu Q.H., Wang H.X., Ng T.B. A novel lectin with potent antitumor, mitogenic and hiv-1 reverse transcriptase inhibitory activities from the edible mushroom // Glycoconjugate Journal. 2010. Vol. 27. Pp. 259–265

Zhang G., Sun J., Wang H., Ng T.B. First isolation and characterization of a novel lectin with potent antitumor activity from a Russula mushroom // Phytomedicine. 2010. Vol. 17. Pp. 775–781.

Weiwei Zhang, Guoting Tian, Xueran Geng, Yongchang Zhao, Tzi Bun Ng, Liyan Zhao and Hexiang Wang. Isolation and Characterization of a Novel Lectin from the Edible Mushroom Stropharia rugosoannulata // Molecules. 2014. Vol. 19. Pp. 19880–19891

Jun Hirabayashi, Hiroaki Tateno, Toshihide Shikanai, Kiyoko F. Aoki-Kinoshita and Hisashi Narimatsu. The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography // Molecules. 2015. Vol. 20. Pp. 951–973

Aoki-Kinoshita K.F., Bolleman J., Campbell M.P., Kawano S., Kim J.D., Lütteke T., Matsubara M., Okuda S., Ran-zinger R., Sawaki H. Introducing glycomics data into the Semantic Web. J. // Biomedical Semantics. 2013. Vol. 4. P. 39.

Rüdiger H., Gabius, H.J. Plant lectins. in the sugar code // Fundamentals of Glycosciences. 2009. Pp. 301–315.

Chrispeels M.J., Raikhel N.V. Lectins, lectins genes and their role in plant defense // Plant Cell. 1991. Vol. 3. Pp. 1–9.

Bowles D.J. Distribution of lectins in membranes of soybean in root, shood and leaftissues at differetnt stades of growth // Planta. 1997. Vol. 145. N2. P. 193.

Kilpatric D.C., Vcomen M.M., Gould A.R. Tissue and subcellular distribution of the lectin from Datura stramonium (thom apple ) // Biochem. J. 1979. Vol. 2. P. 215.

Ямалеева А.А. Лектины растений и их биологическая роль. Уфа, 2001. 137 с.

Michiels K., van Damme E., Smagghe G. Plant-insect interactions: What can we learn from plant lectins? // Arch. Insect Biochem. Physiol. 2010. Vol. 73. Pp. 193–212.

Lannoo N., van Damme E.J.M. Nucleocytoplasmic plant lectins. Biochim. Biophys // Acta Gen. Subj. 2010. Pp. 190–201

Al Atalah B., Smagghe G., van Damme E.J.M. Orysata, a jacalin-related lectin from rice, could protect plants against biting-chewing and piercing-sucking insects // Plant Sci. 2014. Pp. 221–222.

Roy A., Gupta S., Hess D., Das K.P., Das S. Binding of insecticidal lectin Colocasia esculenta tuber agglutinin (CEA) to midgut receptors of Bemisia tabaci and Lipaphis erysimi provides clues to its insecticidal potential // Proteomics. 2014. Vol. 14. Pp. 1646–1659.

Guo P., Wang Y., Zhou X., Xie Y., Wu H., Gao X. Expression of soybean lectin in transgenic tobacco results in en-hanced resistance to pathogens and pests // Plant Sci. 2013. Vol. 211. Pp. 17–22

Peumans W.J., Barre A., Hao Q., Rougé P., van Damme E.J.M. Higher plants developed structurally different motifs to recognize foreign glycans // Trends Glycosci. Glycotechnol. 2000. Vol. 12. Pp. 83–101.

Sabine André, Herbert Kaltner, Joachim C. Manning, Paul V. Murphy, Hans-Joachim Gabius Lectins. Getting Familiar with Translators of the Sugar Code // Molecules. 2015. Vol. 20. Pp. 1788–1823

Sharon N. Glycoproteins now and then: A personal account // Acta Anat. 1998. Vol. 161. Pp. 7–17.

Rüdiger H., Gabius H.-J. The biochemical basis and coding capacity of the sugar code // In The Sugar Code. Funda-mentals of Glycosciences. 2009. Pp. 3–13.

Shewry P.R., Napier J.A., Tatham A.S. Seed storage proteins: Structures and biosynthesis // Plant Cell. 1995. Vol. 7. Pp. 945–956.

Kovalchuk N.V., Melnykova N.M., Musatenko L.I. Role of phytolectins in the life cycle of plants // Biopolym. Cell. 2012. Vol. 3. Pp. 171–180.

Benoist H., Culerrier R., Poiroux G., Segui B., Jauneau A., Van Damme E.J., Peumans W.J., Barre A., Rouge P. Two structurally identical mannose-specific jacalin-related lectins display dif-ferent effects on human T lymphocyte activation and cell death // J. Leukoc. Biol, 2009. Vol. 1. Pp. 103–114.

Melnykova N.M., Mykhalkiv L.M., Mamenko P.M., Kots S.Ya. The areas of application for plant lectins // Biopoly-mers and Cell. 2013. Vol. 29. N5. Pp. 357–366

Kirichenko E.V., Titova L.V. Soybean lectin as a component of a composite biopreparation involving Bradyrhizobium japonicum // Prikl. Biokhim. Mikrobiol. 2006. Vol. 2. Pp. 219–223.

Alenkina S.A., Zharkova V.R., Nikitina V.E. Stabilizing effect of Azospirillum lectins on beta-glucosidase activity // Prikl. Biokhim. Mikrobiol. 2007. Vol. 6. Pp. 653–656.

Fernandezdel-Carmen A., Juarez P., Presa S., Granell A., Orzaez D. Recombinant jacalinlike plant lectins are produced at high levels in Nicotiana benthamiana and retain agglutination activity and sugar specificity // Biotechnol. 2013. Vol. 4. Рp. 391–400.

Бабош A. В. Лектины и проблема распознавания фитопатогенов растением-хозяином // Журнал общей биоло-гии. 2008. Т. 69. №5. С. 379–396.

Шакирова Ф.М., Безрукова М.В. Современные представления о предполагаемых функциях лектинов растений // Журнал общей биологии. 2007. Т. 68. №2. С. 109–125.

Zhu-Salzman K., Ahn J.E., Salzman R.A., Koiwa H., Shade R.E., Balfe S. Fusion of a soybean cysteine protease inhibi-tor and a legume lectin enhances antiinsect activity synergistically // Agric. Forest Enthomol. 2003. Vol. 4. Pp. 317–323.

Tinjuangiun P., Loe N.T., Gatehouse A.M.R., Gatehouse J.A., Christou P. Enhanced insect resistence in Thai rice varie-ties generated by particle bombardment // Mol. Breed. 2000. Vol. 6. Pp. 391–399.

Ng T.B. Review. Antifungal proteins and peptides of leguminous and non-leguminous origins // Peptides. 2004. Vol. 25. Pp. 1215–1222.

Gomes V.M., Okorokov L.A., Rose T.L., Fernandes K.V.S., Xavier-Filho J. Legume vicilins (7S storage globulins) inhibit yeast growth and glucose stimulated acidification of the medium by yeast cells // Biochim. Biophys. Acta. 1998. Pp.207–216.

Ribeiro A., Catarino S., Ferreira R.B.F. Multiple lectin detection by cell membrane affinity binding // Carbohyd. Res. 2012. Pp. 206–210.

Renata de Oliveira Dias, Leandro dos Santos Machado, Ludovico Migliolo, Octavio Luiz Franco. Insights into Animal and Plant Lectins with Antimicrobial Activities // Molecules. 2015. Vol. 20. Pp.519–541.

Miyakawa T., Hatano K.-I., Miyauch, Y., Suwa Y.-I., Sawano Y., Tanokura M. A secreted protein with plant-specific cysteine-rich motif functions as a mannose-binding lectin that exhibits antifungal activity // Plant Physiol. 2014. Vol. 166. Pp.766–778.

Ang A.S.W., Cheung R.C.F., Dan X., Chan Y.S., Pan W., Ng T.B. Purification and characterization of a glucosamine-binding antifungal lectin from Phaseolus vulgaris cv. Chinese pinto beans with antiproliferative activity towards naso-pharyngeal carcinoma cells // Appl. Biochem. Biotechnol. 2014. Vol. 172. Pp. 672–686.

Kanzaki H., Saitoh H., Takahashi Y., Berberich T., Ito A., Kamoun S., Terauchi R. NbLRK1, a lectin-like receptor ki-nase protein of Nicotiana benthamiana, interacts with Phytophthora infestans INF1 elicitin and mediates INF1-induced cell death // Planta. 2008. Vol. 228. Pp. 977–987.

Bouwmeester K., de Sain M., Weide R., Gouget A., Klamer S., Canut H., Govers F. The lectin receptor kinase LecRK-I.9 is a novel Phytophthora resistance component and a potential host target for a RXLR effector. PLoS Pathog, 2011. 327 p.

Huang P., Ju H.-W., Min J.-H., Zhang X., Kim S.-H., Yang K.-Y., Kim C.S. Overexpression of L-type lectin-like pro-tein kinase 1 confers pathogen resistance and regulates salinity response in Arabidopsis thaliana // Plant Sci. 2013. Vol. 203. Pp. 98–106.

Singh P., Chien C.-C., Mishra S., Tsai C.-H., Zimmerl L. The arabidopsis lectin receptor kinase-VI. 2 is a functional protein kinase and is dispensable for basal resistance to Botrytis cinerea. Plant Signal. Behav, 2012. 611 p.

Singh P., Kuo Y.-C., Mishra S., Tsai C.-H., Chien C.-C., Chen C.-W., Desclos-Theveniau M., Chu P.-W., Schulze B., Chinchilla D. The lectin receptor kinase-VI.2 is required for priming and positively regulates arabidopsis pattern-triggered immunity // Plant Cell. 2012. Vol. 24. Pp. 1256–1270.

Shahidi-Noghabi S., van Damme E.J.M., Smagghe G. Expression of sambucus nigra agglutinin (SNA-I’) from elder-berry bark in transgenic tobacco plants results in enhanced resistance to different insect species // Transgenic Res. 2009. Vol. 18. Pp. 249–259.

Гагарина И.Н. Белковый комплекс семян фасоли и испытание биологической активности его компонентов: дис. … канд. сельхоз. наук. Орел, 2006. 147 с.

Патент №2372763 (РФ). Средство для предпосевной обработки семян гороха / Н.Е. Павловская, И.Н. Гагарина, В.В. Роговин, Г.А. Борзенкова, В.М. Муштакова, В.А. Фомина / 2009.

Ерохин А.И., Павловская Н.Е. Эффективность совместного применения препаратов на семенах гороха // Земле-делие. 2016. №4. С. 17–19.

Bebber D.P., Ramotowski M.A.T., Gurr S.J. Crop pests and pathogens move polewards in a warming world. Nat. // Clim. Chang. 2013. Vol. 3. Pp. 985–988.

Boyd L.A., Ridout C., O’Sullivan D.M., Leach J.E., Leung H. Plant-pathogen interactions: Disease resistance in mod-ern agriculture // Trends Genet. 2013. Vol. 29. Pp. 233–240.

Jin S., Zhang, X., Daniell H. Pinellia ternata agglutinin expression in chloroplasts confers broad spectrum resistance against aphid, whitefly, lepidopteran insects, bacterial and viral pathogens // Plant Biotechnol. 2012. Vol. 10. Pp. 313–327.

Евтушенко А.И. Антивирусные свойства лектинов каланхое: изучение и применение лектинов // Уч. зап. Тартус. ун-та. 1989. Вып. 2. 189 c.

Рожнова Н.А., Геращенков Г.А., Бабоша А.В. Индукция фитогемагглютинирующей активности в растениях кортофеля in vitro арахидоновой кислотой // Физиология растений. 2002. Т. 49. №4. С. 603–607.

Адамо П. 4 группы крови – 4 образа жизни. Минск, 2013. 480 с.

Кириченко О.В., Сергиенко В.Г. Фунгитоксичная активность растительных лектинов // Физиология и биохимия культурных растений. 2006. Т. 38. №6. С. 526–534.

Шакирова Ф.М., Безрукова М.В. Современные представления о предполагаемых функциях лектинов растений // Журнал общей биологии. 2007. Т. 68. №2. С. 98–114.

Максимов И.В., Черепанова Е.А., Яруллина Л.Г., Ахметова И.Э. Выделение «хитинспецифичных» оксидоре-дуктаз пшеницы // Прикладная биохимия и микробиология. 2005. Т. 41. №6. С. 616–620.

Лектины. Влияние на здоровье человека [Электронный ресурс]. URL: http://www.glutenlife.ru/articles/ 4270.html?sphrase_id=1957924

Профилактика бактериальных инфекций [Электронный ресурс]. URL: http://medicalfairway.ru/ page_stat.php?ids=40&n_word=инфекции

Lajolo M.F., Genovese M.I. Nutricional Significanse of lectins and Enzyme Inhibitors from Legumes // Journal of Ag-ricultural and Food Chemistry. 2002. Vol. 50(22). Pp. 6892–6598.

Reynoso C.R., González de Mejía E., Loarca P.G. Purification and acute toxicity of a lectin extracted from tepary bean (Phaseolus acutifolius) // Food and Chemical Toxicology. 2003. Vol. 41(1). Pp. 21–27

Muraro A., Hoffmann-Sommergruber K., Holzhauser T., Poulsen L.K., Gowland M.H., Akdis C.A.. EAACI food al-lergy and anaphylaxis guidelines. Protecting consumers with food allergies: understanding food consumption, meeting regulations and identifying unmet needs // Allergy. 2014. Vol. 69(11). Pp. 1464–1472.

Nwaru B.I., Hickstein L., Panesar S.S., Muraro A., Werfel T., Cardona V. The epidemiology of food allergy in Europe: a systematic review and meta-analysis // Allergy. 2014. Vol. 69 (1). Pp. 62–75.

Geert Houben, Peter Burney, Chun-Han Chan, Rene´ Crevel, Anthony Dubois, Roland Faludi, Rinke Klein Entink, Andre´ Knulst, teve Taylor, Stefan Ronsmans. Prioritisation of allergenic foods with respect to public health relevance // Allergy. 2016. Vol. 89. Pp. 8–18.

Информационная записка ИНФОСАН № 4/2008 – Кодекс Алиментариус Международные пищевые стандарты от 6 июня 2008 г. Совместная программа ФАО/ВОЗ.

Соболев С.М., Николаева Т.Н., Григорьева Е.А., Пронин А.В. Роль лектин субстратного распознавания в им-мунорегуляторном взаимодействии интерлейкина-2 и IgG // Медицинская иммунология. 2010. Т. 12. №1–2. C. 13–20.

Heinrich E.L., Welty A.Y., Banner L.R., Oppenheimer S.B. Direct targeting of cancer cells: A multiparameter approach // National Institutes of Health. 2005. Vol. 107(5). Pp. 335–344.

Петибская В.С. Соя: химический состав и использование. Майкоп, 2012. 432 с.

Nishimura H., Nishimura M., Oda R., Yamanaka K., Matsubara T., Ozaki Y., Sekiya L., Jamada T., Kato Y. Lectins induce resistence to proteases and/or mechanical stimulus in all examined cells-including bone narrow mesenchymal stem cells- on various scaffolds. // Experimental Cell Research. 2004. Vol. 295. Pp.119–127.

Pinto L.S., Nagano C.S., Oliveira T.M., Moura T.R., Sampaio A.H., Debray H., Pinto V.P., Dellagostin O.A., Cava-da B.S. Purification and molecular cloning of a new galactose-specific lectin from Bauhinia variegata seeds // Journal Biosciencia. 2008. Vol. 33. Pp. 355–363.

Lajolo M.F., Genovese M.I. Nutricional Significanse of lectins and Enzyme Inhibitors from Legumes // Journal of Ag-ricultural and Food Chemistry. 2002. Vol. 50(22). Pp. 6892–6598.

Канделинская О.Л., Грищенко Е.Р., Обуховская И.П. Мастибротская О.М. Масловский А.Д. Таганович Е.А. Девина Т.Ю. Принькова Т.В. Шман Н.А. Шуканова В.В. Голубков Л.В. Лектины лекарственных растений ди-корастущей флоры Беларуси: перспективы использования // Вестник Фонда фундаментальных исследований. 2011. №2. C. 169–182.

Published
2016-12-07
How to Cite
1. Павловская (Pavlovskaya)Н. (Ninel) Е. (Efimovna), Гагарина (Gagarina)И. Н. THE PHYSIOLOGICAL PROPERTIES OF PLANT LECTINS AS A PREREQUISITE FOR THEIR APPLICATION IN BIOTECHNOLOGY // chemistry of plant raw material, 2016. № 1. P. 21-35. URL: http://journal.asu.ru/cw/article/view/1298.
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Reviews