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Pseudogymnoascus destructans  is a pathogenic fungus responsible for White-nose Syndrome (WNS), a disease afflicting multiple species of North American bats.  Pseudogymnoascus destructans  infects susceptible bats during hibernation, invading dermal tissue and causing extensive tissue damage. In contrast, other  Pseudogymnoascus  species are non-pathogenic and cross-species comparisons may therefore reveal factors that contribute to virulence. In this study, we compared the secretome of  P. destructans  with that from several closely related  Pseudogymnoascus  species. A diverse set of hydrolytic enzymes were identified, including a putative serine peptidase, PdCP1, that was unique to the  P. destructans  secretome. A recombinant form of PdCP1 was purified and substrate preference determined using a multiplexed-substrate profiling method based on enzymatic degradation of a synthetic peptide library and analysis by mass spectrometry. Most peptide substrates were sequentially truncated from the carboxyl-terminus revealing that this enzyme is a  bona fide  carboxypeptidase. Peptides with arginine located close to the carboxyl-terminus were rapidly cleaved, and a fluorescent substrate containing arginine was therefore used to characterize PdCP1 activity and to screen a selection of peptidase inhibitors. Antipain and leupeptin were found to be the most potent inhibitors of PdCP1 activity.

Characterization of PdCP1, a serine carboxypeptidase from Pseudogymnoascus destructans , the causal agent of White-nose Syndrome