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Characterization of acid phosphatases from marine scuticociliate parasites and their activation by host’s factors

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dc.contributor.authorSalinas, I.
dc.contributor.authorMaas, E.W.
dc.contributor.authorMuñoz, P.
dc.contributor.departmentSanidad Animal
dc.date.accessioned2024-03-06T12:50:55Z
dc.date.available2024-03-06T12:50:55Z
dc.date.issued2011-04-18
dc.description© Cambridge University Press 2011. This manuscript version is made available under the CC-BY-NC 4.0 license http://creativecommons.org/licenses/by-nc/4.0/. This document is the accepted, version of a published work that appeared in final form in Parasitology. To access the final edited and published work see https://doi.org/10.1017/S0031182011000527es
dc.description.abstractScuticociliates are histophagous marine parasites that cause mortality in fish. Acid phosphatases (AcPs) are considered virulence factors and they are used by different parasites to dephosphorylate host molecules. The aim of this work was to characterize the AcPs from 3 scuticociliate species, Uronema marinum, Miamiensis avidus and Parauronema virginianum, which parasitize marine fin fish species. We identified AcP activity (pH 5·2) with differential cellular distribution in the 3 parasite species. Native gel electrophoresis of ciliate lysates revealed the presence of 1 high molecular weight AcP activity band in M. avidus (tartrate-sensitive), several low molecular weight AcPs in U. marinum and 1 low molecular weight band only in P. virginianum (tartrate-resistant). Scuticociliate AcP was inhibited by specific inhibitors of tyrosine protein phosphatases. AcP decreased upon starvation but rapid reactivation occurred following exposure to skin mucus. Groper (Polyprion oxygeneios) peripheral blood leucocytes (PBLs) and, to a lesser extent, red blood cells, also increased AcP activity. Protein tyrosine phosphatase PTP1b was primarily detected in the plasma membrane of M. avidus and ingestion of groper PBLs upregulated its expression. M. avidus recovered from experimentally infected groper had greater levels of PTP1b expression than the injected suspension. The present results highlight the importance of PTPs in histophagous parasites and their interaction with fish host’s factors.es
dc.formatapplication/pdfes
dc.format.extent12es
dc.identifier.doihttps://doi.org/10.1017/S0031182011000527
dc.identifier.eisbnParasitology, 138 (7): 836-847. 2011es
dc.identifier.issnPrint: 0031-1820
dc.identifier.issnElectronic: 1469-8161
dc.identifier.urihttp://hdl.handle.net/10201/139972
dc.languageenges
dc.publisherCambridge University Presses
dc.relationFundacion Seneca for a Post-doctoral Fellowship. This work was supported by the capability fund project CF113351 funded by NIWAes
dc.relation.publisherversionhttps://www.cambridge.org/core/journals/parasitology/article/characterization-of-acid-phosphatases-from-marine-scuticociliate-parasites-and-their-activation-by-hosts-factors/E6A24F2921EB52D9B6E36B960532FE12es
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAtribución-NoComercial 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/*
dc.subjectScuticociliate parasiteses
dc.subjectAcid phosphataseses
dc.subjectProtein-tyrosine phosphataseses
dc.subjectPTP1bes
dc.subjectHost-pathogen interactionses
dc.titleCharacterization of acid phosphatases from marine scuticociliate parasites and their activation by host’s factorses
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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