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Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences

Published online by Cambridge University Press:  02 March 2016

NATALIA MALLO ,
JESÚS LAMAS ,
ANA-PAULA DEFELIPE ,
MARIA-EUGENIA DECASTRO ,
ROSA-ANA SUEIRO  and
JOSÉ-MANUEL LEIRO
NATALIA MALLO
Affiliation:
Departamento de Microbiología y Parasitología, Instituto de Investigación y Análisis Alimentarios, Universidad de Santiago de Compostela, 15782 Santiago De Compostela, Spain
JESÚS LAMAS
Affiliation:
Departamento de Biología Celular y Ecología, Facultad de Biología, Instituto de Acuicultura, Universidad de Santiago de Compostela, 15782 Santiago de Compostela, Spain
ANA-PAULA DEFELIPE
Affiliation:
Departamento de Microbiología y Parasitología, Instituto de Investigación y Análisis Alimentarios, Universidad de Santiago de Compostela, 15782 Santiago De Compostela, Spain
MARIA-EUGENIA DECASTRO
Affiliation:
Departamento de Biología Celular y Molecular, Facultad de Ciencias, Universidad de A Coruña, 15701 A Coruña, Spain
ROSA-ANA SUEIRO
Affiliation:
Departamento de Microbiología y Parasitología, Instituto de Investigación y Análisis Alimentarios, Universidad de Santiago de Compostela, 15782 Santiago De Compostela, Spain Departamento de Biología Celular y Ecología, Facultad de Biología, Instituto de Acuicultura, Universidad de Santiago de Compostela, 15782 Santiago de Compostela, Spain
JOSÉ-MANUEL LEIRO*
Affiliation:
Departamento de Microbiología y Parasitología, Instituto de Investigación y Análisis Alimentarios, Universidad de Santiago de Compostela, 15782 Santiago De Compostela, Spain
*
*Corresponding author: Laboratorio de Parasitología, Instituto de Investigación y Análisis Alimentarios, c/ Constantino Candeira s/n, 15782 Santiago de Compostela (A Coruña), Spain. Tel: 34981563100. Fax: 34881816070. E-mail: josemanuel.leiro@usc.es
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Summary

H+-pyrophosphatases (H+-PPases) are integral membrane proteins that couple pyrophosphate energy to an electrochemical gradient across biological membranes and promote the acidification of cellular compartments. Eukaryotic organisms, essentially plants and protozoan parasites, contain various types of H+-PPases associated with vacuoles, plasma membrane and acidic Ca+2 storage organelles called acidocalcisomes. We used Lysotracker Red DND-99 staining to identify two acidic cellular compartments in trophozoites of the marine scuticociliate parasite Philasterides dicentrarchi: the phagocytic vacuoles and the alveolar sacs. The membranes of these compartments also contain H+-PPase, which may promote acidification of these cell structures. We also demonstrated for the first time that the P. dicentrarchi H+-PPase has two isoforms: H+-PPase 1 and 2. Isoform 2, which is probably generated by splicing, is located in the membranes of the alveolar sacs and has an amino acid motif recognized by the H+-PPase-specific antibody PABHK. The amino acid sequences of different isolates of this ciliate are highly conserved. Gene and protein expression in this isoform are significantly regulated by variations in salinity, indicating a possible physiological role of this enzyme and the alveolar sacs in osmoregulation and salt tolerance in P. dicentrarchi.

Keywords

H+-PPasePhilasterides dicentrarchialveolar sacsosmoregulationturbot
Type
Research Article
Information
Parasitology , Volume 143 , Issue 5 , April 2016 , pp. 576 - 587
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Copyright
Copyright © Cambridge University Press 2016 

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