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Identification of Lead Compounds Targeting the Cathepsin B-Like Enzyme of Eimeria tenella
Author(s) -
Marie Schaeffer,
Joerg Schroeder,
Anja R. Heckeroth,
Sandra Noack,
M. Gaßel,
Jeremy C. Mottram,
Paul M. Selzer,
Graham H. Coombs
Publication year - 2011
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.05528-11
Subject(s) - enzyme , eimeria , identification (biology) , biology , microbiology and biotechnology , biochemistry , chemistry , botany
Cysteine peptidases have been implicated in the development and pathogenesis of Eimeria. We have identified a single-copy cathepsin B-like cysteine peptidase gene in the genome database of Eimeria tenella (EtCatB). Molecular modeling of the predicted protein suggested that it differs significantly from host enzymes and could be a good drug target. EtCatB was expressed and secreted as a soluble, active, glycosylated mature enzyme from Pichia pastoris. Biochemical characterization of the recombinant enzyme confirmed that it is cathepsin B-like. Screening of a focused library against the enzyme identified three inhibitors (a nitrile, a thiosemicarbazone, and an oxazolone) that can be used as leads for novel drug discovery against Eimeria. The oxazolone scaffold is a novel cysteine peptidase inhibitor; it may thus find widespread use.

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