The antimicrobial properties of the puroindolines, a review

Antimicrobial proteins, and especially antimicrobial peptides (AMPs) hold great promise in the control of animal and plant diseases with low risk of pathogen resistance. The two puroindolines, a and b, from wheat control endosperm softness of the wheat caryopsis (grain), but have also been shown to...

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Bibliographic Details
Published in:World journal of microbiology & biotechnology 2019-06, Vol.35 (6), p.86-14, Article 86
Main Author: Morris, Craig F.
Format: Article
Language:English
Subjects:
Amino acids
Animal diseases
Antiinfectives and antibacterials
Antimicrobial activity
Antimicrobial agents
Antimicrobial peptides
Applied Microbiology
Binding
Biochemistry
Biomedical and Life Sciences
Biotechnology
Disruption
Endosperm
Environmental Engineering/Biotechnology
Erythrocytes
Fungi
Ion channels
Life Sciences
Lipids
Microbiology
Nucleic acids
Organic chemistry
Peptides
Plant diseases
Proteins
Puroindoline a
Review
Softness
Toxicity
Tryptophan
Wheat
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Summary:Antimicrobial proteins, and especially antimicrobial peptides (AMPs) hold great promise in the control of animal and plant diseases with low risk of pathogen resistance. The two puroindolines, a and b, from wheat control endosperm softness of the wheat caryopsis (grain), but have also been shown to inhibit the growth and kill various bacteria and fungi, while showing little toxicity to erythrocytes. Puroindolines are small (~ 13 kDa) amphipathic proteins with a characteristic tryptophan-rich domain (TRD) that is part of an 18 or 19 amino acid residue loop subtended by a disulfide bond. This review presents a brief history of the puroindolines, their physical–chemical characteristics, their interaction with lipids and membranes, and their activity as antimicrobial proteins and AMPs. In this latter context, the use of the TRDs of puroindoline a and b in puroindoline AMP function is reviewed. The activity of puroindoline a and b and their AMPs appear to act through similar but somewhat different modes, which may involve membrane binding, membrane disruption and ion channel formation, and intra-cellular nucleic acid binding and metabolic disruption. Natural and synthetic mutants have identified key elements of the puroindolines for antimicrobial activity.
ISSN:0959-3993
1573-0972
DOI:10.1007/s11274-019-2655-4