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Current Protein & Peptide Science

Editor-in-Chief

ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Review Article

Snakin: Structure, Roles and Applications of a Plant Antimicrobial Peptide

Author(s): Marx Oliveira-Lima, Ana Maria Benko-Iseppon, Jose Ribamar Costa Ferreira Neto, Susana Rodriguez-Decuadro, Ederson Akio Kido, Sergio Crovella and Valesca Pandolfi

Volume 18, Issue 4, 2017

Page: [368 - 374] Pages: 7

DOI: 10.2174/1389203717666160619183140

Price: $65

Abstract

Snakins are plant antimicrobial peptides (AMPs) of the Snakin/GASA family, formed by three distinct regions: an N-terminal signal peptide; a variable site; and the GASA domain in the Cterminal region composed by twelve conserved cysteine residues that contribute to the biochemical stability of the molecule. These peptides are known to play different roles in response to a variety of biotic (i.e., induced by bacteria, fungi and nematode pathogens) and abiotic (salinity, drought and ROS) stressors, as well as in crosstalk promoted by plant hormones, with emphasis on abscisic and salicylic acid (ABA and SA, respectively). Such properties make snakin/GASA members promising biotechnological sources for potential therapeutic and agricultural applications. However, information regarding their tertiary structure, mode of action and function are not yet completely elucidated. The present review presents aspects of snakin structure, expression, functional studies and perspectives about the potential applications for agricultural and medical purposes.

Keywords: Snakin/GASA domain, cysteine-bridges, stress response, crosstalk.

Graphical Abstract

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