Combating fungal phytopathogens with human salivary antimicrobial peptide histatin 5 through a multi-target mechanism
- PMID: 37269390
- DOI: 10.1007/s11274-023-03667-4
Combating fungal phytopathogens with human salivary antimicrobial peptide histatin 5 through a multi-target mechanism
Abstract
Blast disease caused by Magnaporthe oryzae is a major contributor to decreased crop yield and rice production globally. The use of chemical fungicides to combat crop pathogens is not only unsafe but also promotes the emergence of pathogenic variants, leading to recurrent host infections. To address plant diseases, antimicrobial peptides have emerged as a promising alternative as they are effective, safe, and biodegradable antifungal agents. This study examines the antifungal activity and mechanism of action of the human salivary peptide histatin 5 (Hst5) on M. oryzae. Hst5 causes morphogenetic defects in the fungus, including non-uniform chitin distribution on the fungal cell wall and septa, deformed hyphal branching, and cell lysis. Importantly, a pore-forming mechanism of Hst5 in M. oryzae was ruled out. Furthermore, the interaction of Hst5 with the M. oryzae genomic DNA suggests that the peptide may also influence gene expression in the blast fungus. In addition to its effects on morphogenetic defects and cell lysis, Hst5 also inhibits conidial germination, appressorium formation, and the appearance of blast lesions on rice leaves. The elucidated multi-target antifungal mechanism of Hst5 in M. oryzae provides an environmentally friendly alternative to combating blast infections in rice by preventing fungal pathogenicity. The promising antifungal characteristics of the AMP peptide may also be explored for other crop pathogens, making it a potential biofungicide for the future.
Keywords: Antifungal peptide; Antimicrobial peptide; Magnaporthe oryzae; Plant pathogen; Rice blast; Salivary peptide.
© 2023. The Author(s), under exclusive licence to Springer Nature B.V.
Similar articles
-
Equol, a Clinically Important Metabolite, Inhibits the Development and Pathogenicity of Magnaporthe oryzae, the Causal Agent of Rice Blast Disease.Molecules. 2017 Oct 24;22(10):1799. doi: 10.3390/molecules22101799. Molecules. 2017. PMID: 29064450 Free PMC article.
-
A rice rhizosphere plant growth-promoting Streptomyces corchorusii isolate antagonizes Magnaporthe oryzae and elicits defense responses in rice.J Appl Microbiol. 2024 Dec 2;135(12):lxae266. doi: 10.1093/jambio/lxae266. J Appl Microbiol. 2024. PMID: 39674266
-
In Vitro and Ex Vivo Antifungal Activities of Metconazole against the Rice Blast Fungus Pyricularia oryzae.Molecules. 2024 Mar 19;29(6):1353. doi: 10.3390/molecules29061353. Molecules. 2024. PMID: 38542989 Free PMC article.
-
The role of glycerol in the pathogenic lifestyle of the rice blast fungus Magnaporthe oryzae.Environ Microbiol. 2017 Mar;19(3):1008-1016. doi: 10.1111/1462-2920.13688. Epub 2017 Mar 1. Environ Microbiol. 2017. PMID: 28165657 Review.
-
The link between changing in host carbon allocation and resistance to Magnaporthe oryzae: a possible tactic for mitigating the rice blast fungus.Plant Signal Behav. 2024 Dec 31;19(1):2326870. doi: 10.1080/15592324.2024.2326870. Epub 2024 Mar 11. Plant Signal Behav. 2024. PMID: 38465846 Free PMC article. Review.
Cited by
-
Deciphering optimal molecular determinants of non-hemolytic, cell-penetrating antimicrobial peptides through bioinformatics and Random Forest.Brief Bioinform. 2024 Nov 22;26(1):bbaf049. doi: 10.1093/bib/bbaf049. Brief Bioinform. 2024. PMID: 39973083 Free PMC article.
-
Candida albicans and Antifungal Peptides.Infect Dis Ther. 2023 Dec;12(12):2631-2648. doi: 10.1007/s40121-023-00889-9. Epub 2023 Nov 8. Infect Dis Ther. 2023. PMID: 37940816 Free PMC article.
-
Staphylococcus hominis as a source of antimicrobial peptides: identification of a new peptide with potential antimicrobial properties using in silico approach.Arch Microbiol. 2025 Apr 11;207(5):119. doi: 10.1007/s00203-025-04323-1. Arch Microbiol. 2025. PMID: 40214775
References
-
- Bechinger B, Gorr SU (2017) Antimicrobial peptides: mechanisms of action and resistance. J Dent Res 96(3):254–260. https://doi.org/10.1177/0022034516679973 - DOI - PubMed
-
- Bommarius B, Jenssen H, Elliott M, Kindrachuk J, Pasupuleti M, Gieren H et al (2010) Cost-effective expression and purification of antimicrobial and host defense peptides in Escherichia coli. Peptides 31(11):1957–1965. https://doi.org/10.1016/j.peptides.2010.08.008 - DOI - PubMed - PMC
-
- Brand A, Gow NA (2009) Mechanisms of hypha orientation of fungi. Curr Opin Microbiol 12(4):350–357. https://doi.org/10.1016/j.mib.2009.05.007 - DOI - PubMed - PMC
-
- Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3(3):238–250. https://doi.org/10.1038/nrmicro1098 - DOI - PubMed
-
- Chadha S, Gopalakrishna T (2005) Genetic diversity of Indian isolates of rice blast pathogen (Magnaporthe grisea) using molecular markers. Curr Sci 88:1466–1469
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials