vavilovВавиловский журнал генетики и селекцииVavilov Journal of Genetics and Breeding2500-3259Institute of Cytology and Genetics of Siberian Branch of the RAS10.18699/VJ18.409vavilov-1651Research ArticleГЕНЕТИЧЕСКИЕ РЕСУРСЫ И БИОКОЛЛЕКЦИИPLANT GENETICSТионины растений: строение, биологические функции и перспективы использования в биотехнологииPlant thionins: structure, biological functions and potential use in biotechnologyhttps://orcid.org/0000-0002-5563-9755ОдинцоваТ. И.OdintsovaT. I.

Москва.

Moscow.

odintsova2005@rambler.ruhttps://orcid.org/0000-0003-1653-5993СлезинаМ. П.SlezinaM. P.

Москва.

Moscow.

https://orcid.org/0000-0001-6426-6009ИстоминаЕ. А.IstominaE. A.

Москва.

Moscow.

Институт общей генетики им. Н.И. Вавилова Российской академии наук.РоссияVavilov Institute of General Genetics, RAS.Russian Federation201825092018226667675Copyright © Одинцова Т.И., Слезина М.П., Истомина Е.А., 20182018Одинцова Т.И., Слезина М.П., Истомина Е.А.Odintsova T.I., Slezina M.P., Istomina E.A.This work is licensed under a Creative Commons Attribution 4.0 License.https://vavilov.elpub.ru/jour/article/view/1651

Антимикробные пептиды (АМП) – важнейшие компоненты  защитной системы растений и животных, они представляют собой древний механизм врожденной устойчивости, обеспечивающий «первую линию обороны» против патогенов. Выделяют несколько семейств АМП растений: тионины, дефензины, неспецифические липид-переносящие  белки (ЛПБ), гевеино- и ноттиноподобные пептиды, гарпинины, а также макроциклические пептиды (циклотиды). Обзор посвящен характеристике семейства тионинов. Тионины – характерное только для растений семейство АМП, состоящее из коротких (~5 кДа) цистеинбогатых пептидов (с шестью или восемью остатками цистеина в молекуле), которые обладают антимикробными и токсическими свойствами. На основании сходства амино- кислотных последовательностей и расположения дисульфидных связей выделяют пять структурных классов тионинов. Установлена пространственная структура ряда тионинов. Показано, что амфипатическая молекула тионина имеет форму греческой буквы Г, у которой длинное плечо  образовано двумя антипараллельными α-спиралями, а короткое – двумя параллельными β-тяжами. Выявлены аминокислотные остатки, ответственные за антимикробную активность тионинов. Тионины синтезируются в виде предшественников, состоящих из сигнального пептида, зрелого пептида и С-концевого продомена. Тионины являются защитными пептидами растений против патогенных бактерий и грибов, которые действуют в микромолярных концентрациях непосредственно на мембраны микроорганизмов, хотя детальный механизм действия этих АМП до конца не выяснен. Помимо патогенов растений, тионины подавляют рост ряда патогенных и условно патогенных микроорганизмов человека, таких как Candida spp., Saccharomyces cerevisiae, Fusarium solani, Staphylococcus aureus, Escherichia coli. Тионины токсичны для различного типа клеток, включая линии раковых клеток млекопитающих. Трансгенные растения, в которых экспрессируются гены тионинов, обладают повышенной устойчивостью к патогенам. Широкий спектр антимикробной и токсической активности тионинов открывает возможности их практического использования в сельском хозяйстве и медицине.

Antimicrobial peptides (AMPs) are important components of defense system in both plants and animals. They represent an ancient mechanism of innate immunity providing rapid first line of defense against pathogens. Plant AMPs are classified into several families: thionins, defensins, nonspecific lipid-transfer proteins, hevein- and knottin-type peptides, hairpinins and macrocyclic peptides (cyclotides). The review focuses on the thionin family. Thionins comprise a plant-specific AMP family that consists of short (~5 kDA) cysteine-rich peptides containing 6 or 8 cysteine residues with antimicrobial and toxic properties. Based on similarity in amino acid sequences and the arrangement of disulphide bonds, five structural classes of thionins are discriminated. The three-dimensional structures of a number of thionins were determined. The amphipathic thionin molecule resembles the Greek letter Г, in which the long arm is formed by two antiparallel α-helices, while the short one, by two parallel β-strands. The residues responsible for the antimicrobial activity of thionins were identified. Thionins are synthesized as precursor proteins consisting of a signal peptide, the mature peptide region and the C-terminal prodomain. Thionins protect plants from pathogenic bacteria and fungi acting directly on the membranes of microorganisms at micromolar concentrations, although their precise mode of action remains unclear. In addition to plant pathogens, thionins inhibit growth of a number of human pathogens and opportunistic microorganisms, such as Candida spp., Saccharomyces cerevisiae, Fusarium solani, Staphylococcus aureus and Escherichia coli. Thionins are toxic to different types of cells including mammalian cancer cell lines. Transgenic plants expressing thionin genes display enhanced resistance to pathogens. A wide range of biological activities makes thionins promising candidates for practical application in agriculture and medicine.

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The authors declare that there are no conflicts of interest present.