{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Flo M"],"funding":["Consejo Nacional de Ciencia y Tecnología","Comisión Académica de Posgrado, Universidad de la República UY","Comisión Sectorial de Investigación Científica","Agencia Nacional de Investigación e Innovación"],"pagination":["e1006169"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5325619"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(2)"],"pubmed_abstract":["We previously reported a multigene family of monodomain Kunitz proteins from Echinococcus granulosus (EgKU-1-EgKU-8), and provided evidence that some EgKUs are secreted by larval worms to the host interface. In addition, functional studies and homology modeling suggested that, similar to monodomain Kunitz families present in animal venoms, the E. granulosus family could include peptidase inhibitors as well as channel blockers. Using enzyme kinetics and whole-cell patch-clamp, we now demonstrate that the EgKUs are indeed functionally diverse. In fact, most of them behaved as high affinity inhibitors of either chymotrypsin (EgKU-2-EgKU-3) or trypsin (EgKU-5-EgKU-8). In contrast, the close paralogs EgKU-1 and EgKU-4 blocked voltage-dependent potassium channels (Kv); and also pH-dependent sodi"],"journal":["PLoS pathogens"],"pubmed_title":["Functional diversity of secreted cestode Kunitz proteins: Inhibition of serine peptidases and blockade of cation channels."],"pmcid":["PMC5325619"],"funding_grant_id":["BE_POS_2011_3635","BE_POS_2009_1206","169835","BE_INI_2008_462","167052","I+D_407"],"pubmed_authors":["Margenat M","Duran R","Salceda E","Baez A","Soto E","Pellizza L","Alvarez B","Flo M","Grana M","Fernandez C"],"additional_accession":[]},"is_claimable":false,"name":"Functional diversity of secreted cestode Kunitz proteins: Inhibition of serine peptidases and blockade of cation channels.","description":"We previously reported a multigene family of monodomain Kunitz proteins from Echinococcus granulosus (EgKU-1-EgKU-8), and provided evidence that some EgKUs are secreted by larval worms to the host interface. In addition, functional studies and homology modeling suggested that, similar to monodomain Kunitz families present in animal venoms, the E. granulosus family could include peptidase inhibitors as well as channel blockers. Using enzyme kinetics and whole-cell patch-clamp, we now demonstrate that the EgKUs are indeed functionally diverse. In fact, most of them behaved as high affinity inhibitors of either chymotrypsin (EgKU-2-EgKU-3) or trypsin (EgKU-5-EgKU-8). In contrast, the close paralogs EgKU-1 and EgKU-4 blocked voltage-dependent potassium channels (Kv); and also pH-dependent sodi","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Feb","modification":"2026-05-30T09:04:57.592Z","creation":"2019-03-26T22:49:18Z"},"accession":"S-EPMC5325619","cross_references":{"pubmed":["28192542"],"doi":["10.1371/journal.ppat.1006169"]}}