title: Evaluation of the skin peptide defenses of the Oregon spotted frog Rana pretiosa against infection by the chytrid fungus Batrachochytrium dendrobatidis.
abstract: Population declines due to amphibian chytridiomycosis among selected species of ranid frogs from western North America have been severe, but there is evidence that the Oregon spotted frog, Rana pretiosa Baird and Girard, 1853, displays resistance to the disease. Norepinephrine-stimulated skin secretions were collected from a non-declining population of R. pretiosa that had been exposed to the causative agent Batrachochytrium dendrobatidis. Peptidomic analysis led to identification and isolation, in pure form, of a total of 18 host-defense peptides that were characterized structurally. Brevinin-1PRa, -1PRb, -1PRc, and -1PRd, esculentin-2PRa and -PRb, ranatuerin-2PRa, -2PRb, -2PRc, and -2PRe, temporin-PRb and -PRc were identified in an earlier study of skin secretions of frogs from a different population of R. pretiosa known to be declining. Ranatuerin-2PRf, -2PRg, -2PRh, temporin-PRd, -PRe, and -PRf were not identified in skin secretions from frogs from the declining population, whereas temporin-PRa and ranatuerin-2PRd, present in skin secretions from the declining population, were not detected in the current study. All purified peptides inhibited the growth of B. dendrobatidis zoospores. Peptides of the brevinin-1 and esculentin-2 families displayed the highest potency (minimum inhibitory concentration = 6.25-12.5 μM). The study provides support for the hypothesis that the multiplicity and diversity of the antimicrobial peptide repertoire in R. pretiosa and the high growth-inhibitory potency of certain peptides against B. dendrobatidis are important in conferring a measure of resistance to fatal chytridiomycosis.
authors: Department of Biochemistry, College of Medicine and Health Sciences, United Arab Emirates University, 17666, Al Ain, United Arab Emirates. jmconlon@uaeu.ac.ae
authors: J Michael
authors: JM
authors: Conlon
authors: Laura K
authors: LK
authors: Reinert
authors: Milena
authors: M
authors: Mechkarska
authors: Manju
authors: M
authors: Prajeep
authors: Mohammed A
authors: MA
authors: Meetani
authors: Laurent
authors: L
authors: Coquet
authors: Thierry
authors: T
authors: Jouenne
authors: Marc P
authors: MP
authors: Hayes
authors: Gretchen
authors: G
authors: Padgett-Flohr
authors: Louise A
authors: LA
authors: Rollins-Smith
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D012634:Bodily Secretions; D008411:Chytridiomycota / Q000187:drug effects*; D003247:Conservation of Natural Resources; D003881:Dermatomycoses / Q000378:metabolism / Q000662:veterinary*; D008826:Microbial Sensitivity Tests / Q000662:veterinary; D011157:Population Dynamics; D011898:Ranidae; D012867:Skin / Q000737:chemistry / Q000378:metabolism; D013045:Species Specificity; D021241:Spectrometry, Mass, Electrospray Ionization / Q000662:veterinary; D014861:Washington
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides
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