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Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection.

ABSTRACT: In the indeterminate nodules of a model legume Medicago truncatula, ?700 nodule-specific cysteine-rich (NCR) peptides with conserved cysteine signature are expressed. NCR peptides are highly diverse in sequence, and some of these cationic peptides exhibit antimicrobial activity in vitro and in vivo. However, there is a lack of knowledge regarding their structural architecture, antifungal activity, and modes of action against plant fungal pathogens. Here, the three-dimensional NMR structure of the 36-amino acid NCR044 peptide was solved. This unique structure was largely disordered and highly dynamic with one four-residue ?-helix and one three-residue antiparallel ?-sheet stabilized by two disulfide bonds. NCR044 peptide also exhibited potent fungicidal activity against multiple plant fungal pathogens, including Botrytis cinerea and three Fusarium spp. It inhibited germination in quiescent spores of B. cinerea In germlings, it breached the fungal plasma membrane and induced reactive oxygen species. It bound to multiple bioactive phosphoinositides in vitro. Time-lapse confocal and superresolution microscopy revealed strong fungal cell wall binding, penetration of the cell membrane at discrete foci, followed by gradual loss of turgor, subsequent accumulation in the cytoplasm, and elevated levels in nucleoli of germlings. Spray-applied NCR044 significantly reduced gray mold disease symptoms caused by the fungal pathogen B. cinerea in tomato and tobacco plants, and postharvest products. Our work illustrates the antifungal activity of a structurally unique NCR peptide against plant fungal pathogens and paves the way for future development of this class of peptides as a spray-on fungistat/fungicide.

SUBMITTER: Velivelli SLS

PROVIDER: S-EPMC7354933 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection.

Velivelli Siva L S SLS Czymmek Kirk J KJ Li Hui H Shaw Jared B JB Buchko Garry W GW Shah Dilip M DM

Proceedings of the National Academy of Sciences of the United States of America 20200622 27

In the indeterminate nodules of a model legume <i>Medicago truncatula</i>, ∼700 nodule-specific cysteine-rich (NCR) peptides with conserved cysteine signature are expressed. NCR peptides are highly diverse in sequence, and some of these cationic peptides exhibit antimicrobial activity in vitro and in vivo. However, there is a lack of knowledge regarding their structural architecture, antifungal activity, and modes of action against plant fungal pathogens. Here, the three-dimensional NMR structur ...[more]

PMID: 32571919

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Project description:The urgent need for new antibacterial drugs arises from the emergence of bacterial multidrug resistance due to antibiotic overuse. Antimicrobial peptides, crucial components of innate immunity in animals and plants, exhibit effectiveness against multidrug-resistant bacteria while minimizing the development of drug resistance. In this study, the antibacterial peptide BsR1, comprising 21 amino acids, was finalized by predicting the active site of an antifungal gene and sequence optimization. BsR1 displayed broad-spectrum antibacterial activities against diverse Gram-positive and Gram-negative bacteria, with a low minimum inhibitory concentration of 4.25-17 μM. Stability experiments demonstrated that BsR1 has high resistance to thermal, ultraviolet, and acid-base conditions, while revealing increased sensitivity to divalent ions Ca2+ and Mg2+. The mode of action of BsR1 involved cell membrane damage, leading to bacterial cell structure disruption and subsequent death. Secondary structure prediction indicated a linear helical conformation with a positive charge of +7.5, facilitating its interaction with the target cell membrane. BsR1 exhibited excellent biological safety, as it did not induce necrosis in tobacco leaves, and the low observed hemolytic effect on mammalian cells with a value of 3.26%. Additionally, BsR1 demonstrated the ability to enhance disease resistance in rice and effectively curbed the spread of rice bacterial blight. This research presents BsR1 as a novel approach and potential medication in the development of antibacterial drugs, offering a valuable tool in combating pathogenic microorganisms, particularly in plants.IMPORTANCEThis study addresses the critical need for new antibacterial drugs in the face of bacterial multidrug resistance resulting from antibiotic overuse. It highlights the significance of antimicrobial peptides as essential components of innate immunity in animals and plants, which have been proven effective against multidrug-resistant bacteria and are difficult to develop resistance against. This study successfully synthesizes a broad-spectrum antibacterial peptide, BsR1, with strong inhibitory activities against various Gram-positive and Gram-negative bacteria. BsR1 demonstrates favorable stability and a mode of action that damages bacterial cell membranes, leading to cell death. It also exhibits biological safety and shows potential in enhancing disease resistance in rice. This research offers a novel approach and potential medication for antibacterial drug development, presenting a valuable tool in combating pathogenic microorganisms, particularly in plants.

Dataset Information

Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection.

Publications

Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection.

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