vavilovВавиловский журнал генетики и селекцииVavilov Journal of Genetics and Breeding2500-3259Institute of Cytology and Genetics of Siberian Branch of the RASvavilov-29Research ArticleСтатьиArticlesАНТИМИКРОБНЫЕ ПЕПТИДЫ ПШЕНИЦЫWHEAT ANTIMICROBIAL PEPTIDESОдинцоваТ. И.OdintsovaT. I.odintsova2005@rambler.ruКоростылеваТ. В.KorostylevaT. V.odintsova2005@rambler.ruУткинаЛ. Л.UtkinaL. L.АндреевЯ. А.AndreevYa. A.СлавохотоваА. А.SlavokhotovaA. A.odintsova2005@rambler.ruИстоминаЕ. А.IstominaE. A.odintsova2005@rambler.ruПухальскийВ. А.Pukhal’skiiV. A.odintsova2005@rambler.ruЕгоровЦ. А.EgorovT. A.Федеральное государственное бюджетное учреждение науки Институт общей генетики им. Н.И. Вавилова РАН, Москва, РоссияРоссияVavilov Institute of General Genetics, Russian Academy of Sciences, Moscow, RussiaRussian FederationФедеральное государственное бюджетное учреждение науки Институт общей генетики им. Н.И. Вавилова РАН, Москва, РоссияРоссияShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, RussiaRussian FederationУчреждение Российской академии наук Институт биоорганической химии им. академиков М.М. Шемякина и Ю.А. Овчинникова РАН, Москва, РоссияРоссияShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, RussiaRussian FederationФедеральное государственное бюджетное учреждение науки Институт биоорганической химии им. академиков М.М. Шемякина и Ю.А. Овчинникова Российской академии наукРоссияShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, RussiaRussian Federation201210122014161107115Copyright © Одинцова Т.И., Коростылева Т.В., Уткина Л.Л., Андреев Я.А., Славохотова А.А., Истомина Е.А., Пухальский В.А., Егоров Ц.А., 20142014Одинцова Т.И., Коростылева Т.В., Уткина Л.Л., Андреев Я.А., Славохотова А.А., Истомина Е.А., Пухальский В.А., Егоров Ц.А.Odintsova T.I., Korostyleva T.V., Utkina L.L., Andreev Y.A., Slavokhotova A.A., Istomina E.A., Pukhal’skii V.A., Egorov T.A.This work is licensed under a Creative Commons Attribution 4.0 License.https://vavilov.elpub.ru/jour/article/view/29

Антимикробные пептиды (АМП) представляют собой низкомолекулярные защитные полипептиды, которые образуются в клетках всех живых организмов постоянно или в ответ на атаку патогена. Они являются важнейшими компонентами защитной системы как животных, так и растений. АМП различаются по структуре и механизмам действия. Большинство из них относится к цистеин-богатым пептидам, содержащим четное число остатков цистеина, образующих дисульфидные связи, что придает их молекулам структурную стабильность. На основе гомологии аминокислотных последовательностей и пространственной структуры выделяют несколько семейств АМП растений. Гены АМП растений могут быть использованы для повышения устойчивости сельскохозяйственных растений путем генетической трансформации, а также для разработки на их основе новых антибактериальных и антигрибковых лекарственных препаратов. В настоящем обзоре кратко изложены свойства и структура генов основных исследованных авторами семейств антимикробных пептидов пшеницы Triticum kiharae – глицин-богатых пептидов, дефензинов, гевеиноподобных пептидов, а также семейства 4-Cys пептидов.

Antimicrobial peptides (AMPs) are low-molecular-weight defense polypeptides, produced in all living organisms either constitutively or upon perception of signals from pathogenic microorganisms. They are important components of the immune system in both animals and plants. AMPs differ in structure and mode of action. Most of them belong to cysteine-rich peptides; their molecules contain even numbers of cysteine residues involved in the formation of disulphide bonds, which stabilize the peptide structure. A number of families of plant AMPs have been isolated on the base of amino acid sequence similarity and 3D structure. Plant AMP genes can be used in the engineering of pest resistance in crops and development of novel antibiotics and antimycotics. We provide a concise review of properties and gene structures of major AMP families discovered by the authors in Triticum kiharae seeds, including glycine-rich peptides, defensins, hevein-like peptides and the so-called 4-Cys peptides.

пшеница Triticum kiharae Dorof. et Migusch.антимикробные пептидысеквенирование аминокислотных последовательностей3′- и 5′-RАСЕиммунитет растенийрегуляция экспрессии геновwheatTriticum kiharae Dorof. et Migusch.antimicrobial peptidesamino acid sequencing3′- and 5′-RАСЕ methodplant immunityregulation of gene expressionгранты РФФИ № 09-04-00250-а и 11-04-00190-а; программа Президиума РАН «Генофонды и генетическое разнообразие»; Госконтракт Минобрнауки № 16.512.11.2156ReferencesAjesh K., Sreejith K. Peptide antibiotics: an alternative and antimicrobial strategy to circumvent fungal infections // Peptides. 2009. V. 30. P. 999–1006.Ajesh K., Sreejith K. Peptide antibiotics: an alternative and antimicrobial strategy to circumvent fungal infections // Peptides. 2009. V. 30. P. 999–1006.Benko-Iseppon A.M., Galdino S.L., Calsa T. Jr. et al. Overview on plant antimicrobial peptides // Curr. Protein Pept. Sci. 2010. V. 11. P. 181–188.Benko-Iseppon A.M., Galdino S.L., Calsa T. Jr. et al. Overview on plant antimicrobial peptides // Curr. Protein Pept. Sci. 2010. V. 11. P. 181–188.Broekaert W.F., Cammue B.P.A., De Bolle M.F.C. et al. Antimicrobial peptides from plants // Crit. Rev. Plant Sci. 1997. V. 16. P. 297–323.Broekaert W.F., Cammue B.P.A., De Bolle M.F.C. et al. Antimicrobial peptides from plants // Crit. Rev. Plant Sci. 1997. V. 16. P. 297–323.Bulet P., Hetru C., Dimarcq J.L., Hoffmann D. Antimicrobial peptides in insects, structure and function // Dev. Comp. Immunol. 1999. V. 23. Nо 4/5. P. 329–44.Bulet P., Hetru C., Dimarcq J.L., Hoffmann D. Antimicrobial peptides in insects, structure and function // Dev. Comp. Immunol. 1999. V. 23. Nо 4/5. P. 329–44.Castro M.S., Fontes W. Plant defense and antimicrobial peptides // Protein Pept. 2005. V. 12. P. 13–18.Castro M.S., Fontes W. Plant defense and antimicrobial peptides // Protein Pept. 2005. V. 12. P. 13–18.da Rocha Pitta M.G., da Rocha Pitta M.G., Galdino S.L. Development of novel therapeutic drugs in humans from plant antimicrobial peptides // Curr. Protein Pept. Sci. 2010. V. 11. P. 236–247.da Rocha Pitta M.G., da Rocha Pitta M.G., Galdino S.L. Development of novel therapeutic drugs in humans from plant antimicrobial peptides // Curr. Protein Pept. Sci. 2010. V. 11. P. 236–247.Dubovskii P.V., Vassilevski A.A., Slavokhotova A.A. et al. Solution structure of a defense peptide from wheat with a 10-cysteine motif // Biochem. Biophys. Res. Commun. 2011. V. 411. Nо 1. Р. 14–18.Dubovskii P.V., Vassilevski A.A., Slavokhotova A.A. et al. Solution structure of a defense peptide from wheat with a 10-cysteine motif // Biochem. Biophys. Res. Commun. 2011. V. 411. Nо 1. Р. 14–18.Egorov T.A., Odintsova T.I., Pukhalsky V.A., Grishin E.V. Diversity of wheat antimicrobial peptides // Peptides. 2005. V. 26. P. 2064–2073.Egorov T.A., Odintsova T.I., Pukhalsky V.A., Grishin E.V. Diversity of wheat antimicrobial peptides // Peptides. 2005. V. 26. P. 2064–2073.Gao G.H., Liu W., Dai J.X. et al. Solution structure of PAFP-S: a new knottin-type antifungal peptide from the seeds of Phytolacca americana // Biochemistry. 2001. V. 40. P. 10973–10978.Gao G.H., Liu W., Dai J.X. et al. Solution structure of PAFP-S: a new knottin-type antifungal peptide from the seeds of Phytolacca americana // Biochemistry. 2001. V. 40. P. 10973–10978.Garcia-Olmedo F., Molina A., Alamillo J.M., Rodriguez-Palenzuela P. Plant defense peptides // Biopolymers (Peptide Sci.). 1998. V. 47. P. 479–491.Garcia-Olmedo F., Molina A., Alamillo J.M., Rodriguez-Palenzuela P. Plant defense peptides // Biopolymers (Peptide Sci.). 1998. V. 47. P. 479–491.Garcia-Olmedo F., Rodriguez-Palenzuela P., Molina A. et al. Antibiotic activities of peptides, hydrogen peroxide and peroxynitrite in plant defence // FEBS Letters. 2001. V. 498. P. 219–222.Garcia-Olmedo F., Rodriguez-Palenzuela P., Molina A. et al. Antibiotic activities of peptides, hydrogen peroxide and peroxynitrite in plant defence // FEBS Letters. 2001. V. 498. P. 219–222.Farrokhi N., Whitelegge J.P., Brusslan J.A. Plant peptides and peptidomics // Plant Biotechnol. J. 2008. V. 6. P. 105–134.Farrokhi N., Whitelegge J.P., Brusslan J.A. Plant peptides and peptidomics // Plant Biotechnol. J. 2008. V. 6. P. 105–134.Huang R-H., Xiang Y., Liu X-Z. et al. Two novel antifungal peptides distinct with a fi ve-disulfi de motif from the bark of Eucommia ulmoides Oliv // FEBS Lett. 2002. V. 521. P. 87–90.Huang R-H., Xiang Y., Liu X-Z. et al. Two novel antifungal peptides distinct with a fi ve-disulfi de motif from the bark of Eucommia ulmoides Oliv // FEBS Lett. 2002. V. 521. P. 87–90.Kido E.A., Pandolfi V., Houllou-Kido L.M. et al. Plant antimicrobial peptides: an overview of SuperSAGE transcriptional profi le and a functional review // Curr. Protein Pept. Sci. 2010. V. 11. P. 220–230.Kido E.A., Pandolfi V., Houllou-Kido L.M. et al. Plant antimicrobial peptides: an overview of SuperSAGE transcriptional profi le and a functional review // Curr. Protein Pept. Sci. 2010. V. 11. P. 220–230.Koike M., Okamoto T., Tsuda S., Imai R. A novel plant defensin-like gene of winter wheat is specifi cally induced during cold acclimation // Biochem. Biophys. Res. Commun. 2002. V. 298. P. 46–53.Koike M., Okamoto T., Tsuda S., Imai R. A novel plant defensin-like gene of winter wheat is specifi cally induced during cold acclimation // Biochem. Biophys. Res. Commun. 2002. V. 298. P. 46–53.Lobo D.S., Pereira I.B., Fragel-Madeira L. et al. Antifungal Pisum sativum defensin 1 interacts with Neurospora crassa cyclin F related to the cell cycle // Biochemistry. 2007. V. 46. P. 987–996.Lobo D.S., Pereira I.B., Fragel-Madeira L. et al. Antifungal Pisum sativum defensin 1 interacts with Neurospora crassa cyclin F related to the cell cycle // Biochemistry. 2007. V. 46. P. 987–996.Manners J.M. Hidden weapons of microbial destruction in plant genomes // Genome Biol. 2007. V. 8. P. 225–234.Manners J.M. Hidden weapons of microbial destruction in plant genomes // Genome Biol. 2007. V. 8. P. 225–234.Nolde S.B., Vassilevski A.A., Rogozhin E.A. et al. Disulfi destabilized helical hairpin structure of a novel antifungal peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli) // J. Biol. Chem. 2011. V. 286. Nо 28. Р. 25145–25153.Nolde S.B., Vassilevski A.A., Rogozhin E.A. et al. Disulfi destabilized helical hairpin structure of a novel antifungal peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli) // J. Biol. Chem. 2011. V. 286. Nо 28. Р. 25145–25153.Odintsova T.I., Egorov Ts.A., Musolyamov A.Kh. et al. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes // Biochimie. 2007. V. 89. P. 605–612.Odintsova T.I., Egorov Ts.A., Musolyamov A.Kh. et al. Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes // Biochimie. 2007. V. 89. P. 605–612.Odintsova T.I., Vassilevski A.A., Slavokhotova A.A. et al. A novel antifungal hevein-type peptide from Triticum kiharae seeds with a unique 10-cysteine motif // FEBS J. 2009. V. 276. P. 4266–4275.Odintsova T.I., Vassilevski A.A., Slavokhotova A.A. et al. A novel antifungal hevein-type peptide from Triticum kiharae seeds with a unique 10-cysteine motif // FEBS J. 2009. V. 276. P. 4266–4275.Padovan L., Scocchi M., Tossi A. Structural aspects of plant antimicrobial peptides // Curr. Protein Pept. Sci. 2010. V. 11. P. 210–219.Padovan L., Scocchi M., Tossi A. Structural aspects of plant antimicrobial peptides // Curr. Protein Pept. Sci. 2010. V. 11. P. 210–219.Sels J., Mathys J., De Coninck B.M. et al. Plant pathogenesis-related (PR) proteins: a focus on PR peptides // Plant Physiol. Biochem. 2008. V. 46. P. 941–950.Sels J., Mathys J., De Coninck B.M. et al. Plant pathogenesis-related (PR) proteins: a focus on PR peptides // Plant Physiol. Biochem. 2008. V. 46. P. 941–950.Tavares L.S., de Santos M., Viccini L.F. et al. Biotechnological potential of antimicrobial peptides from fl owers // Peptides. 2008. V. 29. P. 1842–1851.Tavares L.S., de Santos M., Viccini L.F. et al. Biotechnological potential of antimicrobial peptides from fl owers // Peptides. 2008. V. 29. P. 1842–1851.Van den Bergh K.P.B., Proost P., Van Damme J. et al. Five disulfi de bridges stabilize a hevein-type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.) // FEBS Letters. 2002. V. 530. P. 181–185.Van den Bergh K.P.B., Proost P., Van Damme J. et al. Five disulfi de bridges stabilize a hevein-type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.) // FEBS Letters. 2002. V. 530. P. 181–185.Van der Weerden N.L., Lay F.T., Anderson M.A. The plant defensin, NaD1, enters the cytoplasm of Fusarium oxysporum hyphae // J. Biol. Chem. 2008. V. 283. P. 14445–14452.Van der Weerden N.L., Lay F.T., Anderson M.A. The plant defensin, NaD1, enters the cytoplasm of Fusarium oxysporum hyphae // J. Biol. Chem. 2008. V. 283. P. 14445–14452.Vasil I.K. Molecular genetic improvement of cereals: transgenic wheat (Triticum aestivum L.) // Plant Cell Rep. 2007. V. 26. P. 1133–1154.Vasil I.K. Molecular genetic improvement of cereals: transgenic wheat (Triticum aestivum L.) // Plant Cell Rep. 2007. V. 26. P. 1133–1154.

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