title: Activity of antimicrobial skin peptides from ranid frogs against Batrachochytrium dendrobatidis, the chytrid fungus associated with global amphibian declines.
abstract: Accumulating evidence suggests that a chytrid fungus, Batrachochytrium dendrobatidis, is responsible for recent declines in amphibian populations in Australia, Central America, Europe, and North America. Because the chytrid infects the keratinized epithelium of the skin, we investigated the possible role of antimicrobial peptides produced in the skin as inhibitors of infection and growth. We show here that 10 peptides representing eight families of peptides derived from North American ranid frogs can effectively inhibit growth of this chytrid. The peptides are members of the ranatuerin-1, ranatuerin-2, esculentin-1, esculentin-2, brevinin-2, temporin, palustrin-3, and ranalexin families. All the tested peptides inhibit growth of mature fungal cells at concentrations above 25 microM, and some of them inhibit at concentrations as low as 2 microM. A comparison of the sensitivity of infectious zoospores with that of mature cells showed that the zoospores are inhibited at significantly lower concentrations of peptides. To determine whether cold temperature interferes with the inhibitory effects of these peptides, we tested their effectiveness at both 22 and 10 degrees C. Although the peptides inhibit at both temperatures, they appear to be more effective against zoospores at the lower temperature. These results suggest that the ranid frogs have, within their repertoire of antimicrobial substances, a number of skin peptides that should be a deterrent to chytrid infection. This may provide some natural resistance to infection, but if environmental factors inhibit the synthesis and release of the skin peptides, the pathogen could gain the advantage.
authors.affiliation: Departments of Microbiology and Immunology & Pediatrics, Vanderbilt University, Medical Center North, A-5301, Nashville, TN 37232, USA. louise.rollins-smith@mcmail.vanderbilt.edu
authors.forename: Louise A
authors.initials: LA
authors.lastname: Rollins-Smith
authors.forename: Cynthia
authors.initials: C
authors.lastname: Carey
authors.forename: Joyce
authors.initials: J
authors.lastname: Longcore
authors.forename: Jennifer K
authors.initials: JK
authors.lastname: Doersam
authors.forename: Angela
authors.initials: A
authors.lastname: Boutte
authors.forename: Judsen E
authors.initials: JE
authors.lastname: Bruzgal
authors.forename: J Michael
authors.initials: JM
authors.lastname: Conlon
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000935:Antifungal Agents / Q000494:pharmacology*; D008411:Chytridiomycota / Q000187:drug effects* / Q000254:growth & development; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D009656:North America; D010455:Peptides / Q000276:immunology / Q000302:isolation & purification / Q000494:pharmacology*; D011898:Ranidae / Q000276:immunology* / Q000378:metabolism; D012867:Skin / Q000276:immunology* / Q000378:metabolism
chemical_list: D000935:Antifungal Agents; D010455:Peptides