Biochimie. 2015 Sep;116:125-32. doi: 10.1016/j.biochi.2015.07.014. Epub 2015 Jul 18.

A novel antifungal peptide from leaves of the weed Stellaria media L.

Rogozhin EA1, Slezina MP2, Slavokhotova AA3, Istomina EA4, Korostyleva TV5, Smirnov AN6, Grishin EV7, Egorov TA8, Odintsova TI9.

• 1Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russian Federation. Electronic address: rea21@list.ru.
• 2Vavilov Institute of General Genetics, Russian Academy of Sciences, ul. Gubkina 3, 117809 Moscow, Russian Federation. Electronic address: omey@list.ru.
• 3Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russian Federation; Vavilov Institute of General Genetics, Russian Academy of Sciences, ul. Gubkina 3, 117809 Moscow, Russian Federation. Electronic address: ann.slav@gmail.com.
• 4Vavilov Institute of General Genetics, Russian Academy of Sciences, ul. Gubkina 3, 117809 Moscow, Russian Federation. Electronic address: mer06@yandex.ru.
• 5Vavilov Institute of General Genetics, Russian Academy of Sciences, ul. Gubkina 3, 117809 Moscow, Russian Federation. Electronic address: tatko@hotbox.ru.
• 6Timiryazev Russian State Agrarian University, ul. Timiryazevskaya, 49, 127550 Moscow, Russian Federation. Electronic address: smirnov@timacad.ru.
• 7Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russian Federation. Electronic address: grev@mx.ibch.ru.
• 8Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russian Federation.
• 9Vavilov Institute of General Genetics, Russian Academy of Sciences, ul. Gubkina 3, 117809 Moscow, Russian Federation. Electronic address: odintsova2005@rambler.ru.

Abstract

A novel peptide named SmAMP3 was isolated from leaves of common chickweed (Stellaria media L.) by a combination of acidic extraction and a single-step reversed-phase HPLC and sequenced. The peptide is basic and cysteine-rich, consists of 35 amino acids, and contains three disulphide bridges. Homology search revealed that SmAMP3 belongs to the family of hevein-like antimicrobial peptides carrying a conserved chitin-binding site. Efficient binding of chitin by SmAMP3 was proved by in vitro assays. Molecular modeling confirmed conservation of the chitin-binding module in SmAMP3 locating the variable amino acid residues to the solvent-exposed loops of the molecule. The peptide exhibits potent antifungal activity against important plant pathogens in the micromolar range, although it is devoid of antibacterial activity at concentrations below 10 μM. As judged by chromatographic behavior and mass spectrometric data, the peptide is constitutively expressed in above-ground organs and seeds of S. media plants, thus representing an important player in the preformed branch of the plant immune system.

Copyright © 2015 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.

KEYWORDS:

Antifungal activity; Chitin binding; Hevein-like peptide; Leaves; Stellaria media

PMID:

26196691