Publication: Characterization of acid phosphatases from marine scuticociliate parasites and their activation by host’s factors
Authors
Salinas, I. ; Maas, E.W. ; Muñoz, P.
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Publisher
Cambridge University Press
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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/S0031182011000527
Abstract
Scuticociliates 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.
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