Structural Aspects of Plant Antimicrobial Peptides

Author(s): Lara Padovan , Marco Scocchi , Alessandro Tossi .

Journal Name: Current Protein & Peptide Science

Volume 11 , Issue 3 , 2010

Become EABM
Become Reviewer


Antimicrobial peptides exert an important role in plant defence and their structure/activity relationship against pathogens is widely described. Although the most striking feature of these antimicrobial peptides is their molecular diversity, they share some common features, such as a relatively low molecular weight, and the presence of a variable number of cysteines residues that contribute to stabilize conserved scaffolds through disulphide bond formation, and can be assigned to different structural classes. Peptides from different classes in some cases act synergistically against pathogens when produced by the same tissue, and contribute to extending defence to a wider range of microbes. In this review we briefly describe the structure of some of the main plant antimicrobial peptide classes: thionins, defensins, lipid transfer proteins, cyclotides and snakins, and how they are reported to contribute to the plant protection. In many cases these antimicrobial peptides show a wider activity spectrum than that suggested by their name, exerting an action also against predatory insects and revealing useful antiviral activities. This extends their interest from defense of important food crops also to the design of novel anti-infective compounds for both pharmaceutical and agricultural applications.

Keywords: Antimicrobial peptides, cyclotides, defensins, plant, lipid transfer proteins, snakins, thionins

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2010
Page: [210 - 219]
Pages: 10
DOI: 10.2174/138920310791112093
Price: $58

Article Metrics

PDF: 22