Antifungal and Reactivation Activity of a Novel Glycine/histidine-rich Linear Peptide from Dog-grass ( Elytrigiarepens  (L.) Desv. ex Nevski) EARS

D. Yu. Ryazantsev; Рязанцев Д. Ю.; E. Yu. Khodzhaev; Ходжаев Е. Ю.; A. E. Kuvarina; Куварина А. Е.; A. S. Barashkova; Барашкова А. С.; E. A. Rogozhin; Рогожин Е. А.

doi:10.31857/S0555109923010099

Antifungal and Reactivation Activity of a Novel Glycine/histidine-rich Linear Peptide from Dog-grass (Elytrigiarepens (L.) Desv. ex Nevski) EARS

作者: Ryazantsev D.Y.¹, Khodzhaev E.Y.², Kuvarina A.E.³, Barashkova A.S.¹, Rogozhin E.A.¹^,3
隶属关系:
1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry
2. Lomonosov Moscow State University
3. Gause Institute New Antibiotics
期: 卷 59, 编号 1 (2023)
页面: 38-45
栏目: Articles
URL: https://journal-vniispk.ru/0555-1099/article/view/138738
DOI: https://doi.org/10.31857/S0555109923010099
EDN: https://elibrary.ru/CVBXOI
ID: 138738

如何引用文章

全文:

详细
作者简介
参考
补充文件
统计

详细

Using a combination of solid-phase extraction, affinity chromatography, and analytical reverse-phase HPLC, a new linear peptide was isolated from dog-grass (Elytrigia repens) ears, which does not contain cysteine residues. Identification of its primary structure by Edman automated degradation made it possible to reveal the presence of several polyglycine regions, each consisting of 6–8 residues, between which short fragments consisting of polar amino acid residues are localized. The C-terminal fragment of the molecule is a positively charged site enriched in arginine and histidine residues. The structural features of this peptide determine its functionality. Thus, checking the presence of antimicrobial properties in its recombinant analogue, obtained by heterologous expression in a prokaryotic system, made it possible to determine the MIC for the tested fungal cultures only at sufficiently high active concentrations (52–104 μM). However, this compound had regulatory properties: at a concentration of 25 μM, a reactivating effect was noted, which increased the level of survival of Saccharomyces cerevisiae to UV-irradiation. The data obtained expand the understanding of the functional features of plant defense peptides of an unusual structural type.

关键词

antimicrobial peptides, reactivation activity, primary structure, dog-grass

参考

van der Weerden N.L., Bleackley M.R., Anderson M.A. // Cell. Mol. Life Sci. 2013. V. 70. № 19.P. 3545–3570. https://doi.org/10.1007/s00018-013-1260-1
Tam J.P., Wang S., Wong K.H., Tan. W.L. // Pharmaceuticals (Basel). 2015. V. 8. № 4. P. 711–757. https://doi.org/10.3390/ph8040711
SarikaIquebal M.A., Rai A. // Peptides. 2012. V. 36. № 2. P. 322–330. https://doi.org/10.1016/j.peptides.2012.05.012
Das K., Datta K., Karmakar S., Datta S.K. // Protein Pept. Lett.2019. V. 26. № 10. P. 720–742. https://doi.org/10.2174/0929866526666190619112438
Stec B. // Cell. Mol. Life Sci. 2006. V. 63. № 12. P. 1370–1385. https://doi.org/10.1007/s00018-005-5574-5
Parisi K., Shafee T.M.A., Quimbar P., van der Weerden N.L., Bleackley M.R., Anderson M.A. // Semin.Cell. Dev. Biol. 2019. V. 88. P. 107–118. https://doi.org/10.1016/j.semcdb.2018.02.004
Рогожин Е.А., Одинцова Т.И., Мусолямов А.Х., Смирнов А.Н., Бабаков А.В., Егоров Ц.А., Гришин Е.В. // Прикл. биохимия и микробиология. 2009. Т. 45. № 4. С. 403–409.
Рязанцев Д.Ю., Рогожин Е.А., Цветков В.О., Яруллина Л.Г., Смирнов А.Н., Завриев С.К. // Доклады Академии Наук. 2019. Т. 484. № 1. С. 104–106.
Odintsova T.I., Rogozhin E.A., Baranov Yu.V., Musolyamov A.Kh., Yalpani N., Egorov Ts.A., Grishin E.V. // Biochimie. 2008. V. 90. P. 1667–1673. https://doi.org/10.1016/j.biochi.2008.06.007
Уткина Л.Л., Жабон Е.О., Славохотова А.А., Рогожин Е.А., Шиян А.А., Гришин Е.В., Егоров Ц.А., Одинцова Т.И., Пухальский В.А. // Генетика. 2010. Т. 46. № 12. С. 1–7.
Slavokhotova A.A., Shelenkov A.A., Odintsova T.I. // Plant Mol. Biol. 2015. V. 89. № 3. P. 203–214. https://doi.org/10.1007/s11103-015-0346-6
Odintsova T.I., Slezina M.P., Istomina E.A. // Biomolecules. 2020. V. 10. № 7. E. 1029. https://doi.org/10.3390/biom10071029
Koetter U., Kaloga M., Schilcher H. // Part I. Planta Med. 1993. V. 59. № 3. P. 279–280. https://doi.org/10.1055/s-2006-959672
Beydokthi S.S., Sendker J., Brandt S., Hensel A. // Fitoterapia. 2017. V. 117. P. 22–27. https://doi.org/10.1016/j.fitote.2016.12.010
Кароматов И.Д. // Биология и интегративная медицина. 2017. № 6. С. 122–128.
Provencher S.W., Glöckner J. // Biochemistry. 1981. V. 20. № 1. P. 33–37. https://doi.org/10.1021/bi00504a006
Andreev Y.A., Kozlov S.A., Vassilevski A.A., Grishin E.V. // Anal. Biochem. 2010. V. 407. № 1. P. 144–146. https://doi.org/10.1016/j.ab.2010.07.023
Воробьева Л.И., Рогожин Е.А., Ходжаев Е.Ю., Володяшкин Р.А., Самойленко В.А. // Микробиология. 2017. Т. 86. № 6. С. 684–695.
Barashkova A.S., Rogozhin E.A. // BMC Plant Methods. 2020. V. 16. E. 143. https://doi.org/10.1186/s13007-020-00687-1
Park C.J., Park C.B., Hong S.S., Lee H.S., Lee S.Y., Kim S.C. // Plant Mol. Biol. 2000. V. 44. № 2. P. 187–197. https://doi.org/10.1023/a:1006431320677
Hilton H., Gaut B.S. // Genetics. 1998. V. 150. № 2. P. 863–872. https://doi.org/10.1093/genetics/150.2.863
Gorinstein S., Jaramillo N.O., Medina O.J., Rogriques W.A., Tosello G.A., Paredes-Lopez O. // J. Protein Chem. 1999. V. 18. № 6. P. 687–693. https://doi.org/10.1023/a:1020610424625
Czolpinska M., Rurek M. // Front Plant. Sci. 2018. V. 8. № 9. E. 302. https://doi.org/10.3389/fpls.2018.00302
Pelegrini P.B., Murad A.M., Silva L.P., Dos Santos R.C., Costa F.T., Tagliari P.D. et al. // Peptides. 2008. V. 29. № 8. P. 1271–1279. https://doi.org/10.1016/j.peptides.2008.03.013
Remuzgo C., Oewel T.S., Daffre S., Lopes T.R., Dyszy F.H., Schreier S. et al. // Amino Acids. 2014. V. 46. № 11. P. 2573–2586. https://doi.org/10.1007/s00726-014-1811-2
Рогожин Е.А., Воробьева Л.И., Ходжаев Е.Ю., Герасимов Е.С. // Микробиология. 2019. Т. 88. № 2. С. 137–143.