Growth Characteristics and Enzyme Activity in Batrachochytrium dendrobatidis Isolates

Batrachochytrium dendrobatidis is a member of the phylum Chytridiomycota and the causative organism chytridiomycosis, a disease of amphibians associated with global population declines and mass mortality events. The organism targets keratin-forming epithelium in adult and larval amphibians, which su...

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Bibliographic Details
Published in:Mycopathologia (1975) 2008-09, Vol.166 (3), p.143-147
Main Authors: Symonds, E. Pearl, Trott, Darren J, Bird, Philip S, Mills, Paul
Format: Article
Language:English
Subjects:
Agar
Animals
Anura
Anura - microbiology
Batrachochytrium dendrobatidis
Biomedical and Life Sciences
Chytridiomycota - enzymology
Chytridiomycota - growth & development
Chytridiomycota - isolation & purification
Culture Media - chemistry
Dermatomycoses - veterinary
Dermatomycoses - virology
Enzymes
Eukaryotic Microbiology
Keratin
Keratins - metabolism
Life Sciences
Medical Microbiology
Microbial Ecology
Microbiology
Peptide Hydrolases - classification
Peptide Hydrolases - metabolism
Plant Sciences
Reptiles & amphibians
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Summary:Batrachochytrium dendrobatidis is a member of the phylum Chytridiomycota and the causative organism chytridiomycosis, a disease of amphibians associated with global population declines and mass mortality events. The organism targets keratin-forming epithelium in adult and larval amphibians, which suggests that keratinolytic activity may be required to infect amphibian hosts. To investigate this hypothesis, we tested 10 isolates of B. dendrobatidis for their ability to grow on a range of keratin-supplemented agars and measured keratolytic enzyme activity using a commercially available kit (bioMerieux API ZYM). The most dense and fastest growth of isolates were recorded on tryptone agar, followed by growth on frog skin agar and the slowest growth recorded on feather meal and boiled snake skin agar. Growth patterns were distinctive for each nutrient source. All 10 isolates were strongly positive for a range of proteolytic enzymes which may be keratinolytic, including trypsin and chymotrypsin. These findings support the predilection of B. dendrobatidis for amphibian skin.
ISSN:0301-486X
1573-0832
DOI:10.1007/s11046-008-9135-y