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Keywords = Sado wrinkled frog

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19 pages, 5068 KiB  
Article
Antimicrobial Property and Mode of Action of the Skin Peptides of the Sado Wrinkled Frog, Glandirana susurra, against Animal and Plant Pathogens
by Daisuke Ogawa, Manami Suzuki, Yuriko Inamura, Kaito Saito, Itaru Hasunuma, Tetsuya Kobayashi, Sakae Kikuyama and Shawichi Iwamuro
Antibiotics 2020, 9(8), 457; https://doi.org/10.3390/antibiotics9080457 - 29 Jul 2020
Cited by 7 | Viewed by 4000
Abstract
The Sado wrinkled frog Glandirana susurra has recently been classified as a new frog species endemic to Sado Island, Japan. In this study, we cloned 12 cDNAs encoding the biosynthetic precursors for brevinin-2SSa–2SSd, esculentin-2SSa, ranatuerin-2SSa, brevinin-1SSa–1SSd, granuliberin-SSa, and bradykinin-SSa from the skin of [...] Read more.
The Sado wrinkled frog Glandirana susurra has recently been classified as a new frog species endemic to Sado Island, Japan. In this study, we cloned 12 cDNAs encoding the biosynthetic precursors for brevinin-2SSa–2SSd, esculentin-2SSa, ranatuerin-2SSa, brevinin-1SSa–1SSd, granuliberin-SSa, and bradykinin-SSa from the skin of G. susurra. Among these antimicrobial peptides, we focused on brevinin-2SSb, ranatuerin-2SSa, and granuliberin-SSa, using their synthetic replicates to examine their activities against different reference strains of pathogenic microorganisms that infect animals and plants. In broth microdilution assays, brevinin-2SSb displayed antimicrobial activities against animal pathogens Escherichia coli, Salmonella enterica, Pseudomonas aeruginosa, and Candida albicans and plant pathogens Xanthomonas oryzae pv. oryzae, Clavibacter michiganensis subsp. michiganensis, and Pyricularia oryzae. Ranatuerin-2SSa and granuliberin-SSa were active against C. albicans and C. michiganensis subsp. michiganensis, and granuliberin-SSa also was active against the other plant pathogenic microbes. Scanning electron microscopic observations demonstrated that brevinin-2SSb, ranatuerin-2SSa, and granuliberin-SSa induced morphological abnormalities on the cell surface in a wide range of the reference pathogens. To assess the bacterial-endotoxin-binding ability of the peptides, we developed an enzyme-linked endotoxin-binding assay system and demonstrated that brevinin-2SSb and ranatuerin-2SSa both exhibited high affinity to lipopolysaccharide and moderate affinity to lipoteichoic acid. Full article
(This article belongs to the Special Issue Development of Antimicrobial Peptides from Amphibian)
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