The evolution, function and mechanisms of action for plant defensins
journal contributionposted on 04.01.2021, 05:26 by Kathy ParisiKathy Parisi, Thomas ShafeeThomas Shafee, Pedro Quimbar Dominguez, Nicole Van Der WeerdenNicole Van Der Weerden, Mark BleackleyMark Bleackley, Marilyn AndersonMarilyn Anderson
https://doi.org/10.1016/j.semcdb.2018.02.004© 2018 Elsevier Ltd Plant defensins are an extensive family of small cysteine rich proteins characterised by a conserved cysteine stabilised alpha beta protein fold which resembles the structure of insect and vertebrate defensins. However, secondary structure and disulphide topology indicates two independent superfamilies of defensins with similar structures that have arisen via an extreme case of convergent evolution. Defensins from plants and insects belong to the cis-defensin superfamily whereas mammalian defensins belong to the trans-defensin superfamily. Plant defensins are produced by all species of plants and although the structure is highly conserved, the amino acid sequences are highly variable with the exception of the cysteine residues that form the stabilising disulphide bonds and a few other conserved residues. The majority of plant defensins are components of the plant innate immune system but others have evolved additional functions ranging from roles in sexual reproduction and development to metal tolerance. This review focuses on the antifungal mechanisms of plant defensins. The activity of plant defensins is not limited to plant pathogens and many of the described mechanisms have been elucidated using yeast models. These mechanisms are more complex than simple membrane permeabilisation induced by many small antimicrobial peptides. Common themes that run through the characterised mechanisms are interactions with specific lipids, production of reactive oxygen species and induction of cell wall stress. Links between sequence motifs and functions are highlighted where appropriate. The complexity of the interactions between plant defensins and fungi helps explain why this protein superfamily is ubiquitous in plant innate immunity.
This work was supported by ARC Discovery Projects to MAA and NLV (DP150104386) and MAA (DP160100309).
ARC | DP150104386
ARC | DP160100309
JournalSeminars in Cell and Developmental Biology
Paginationpp. 107-118 (12p.)
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Science & TechnologyLife Sciences & BiomedicineCell BiologyDevelopmental BiologyDefensinAntifungal peptideAMPInnate immunityTEPHROSIA-VILLOSA DEFENSINPISUM-SATIVUM DEFENSIN-1INSECT ALPHA-AMYLASESDAHLIA DAHLIA-MERCKIIANTIFUNGAL PLANTRAPHANUS-SATIVUSSACCHAROMYCES-CEREVISIAEANTIMICROBIAL PEPTIDESNEUROSPORA-CRASSAPROTEIN-SYNTHESISCell WallFungiPlantsReactive Oxygen SpeciesLipidsDefensinsPlant ProteinsEvolution, MolecularPlant DiseasesGene Expression Regulation, PlantConserved SequenceProtein Structure, SecondaryProtein FoldingHost-Pathogen InteractionsPlant ImmunityDisease Resistance