Molecular and functional characterization of a Schistosoma bovis annexin: fibrinolytic and anticoagulant activity |
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Authors: | de la Torre-Escudero Eduardo Manzano-Román Raúl Siles-Lucas Mar Pérez-Sánchez Ricardo Moyano J Carlos Barrera Inmaculada Oleaga Ana |
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Affiliation: | a Parasitology Laboratory, Instituto de Recursos Naturales y Agrobiología de Salamanca (IRNASA, CSIC), Cordel de Merinas, 40-52, 37008 Salamanca, Spain b Servicio de Análisis Clínicos, Complejo Hospitalario de Salamanca, Paseo de San Vicente 58-182, 37007 Salamanca, Spain c Departamento de Estadística, Facultad de Medicina, Universidad de Salamanca, Alfonso X El Sabio s/n, 37007 Salamanca, Spain |
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Abstract: | Annexins belong to an evolutionarily conserved multigene family of proteins expressed throughout the animal and plant kingdoms. Although they are soluble cytosolic proteins that lack signal sequences, they have also been detected in extracellular fluids and have been associated with cell surface membranes, where they could be involved in anti-haemostatic and anti-inflammatory functions. Schistosome annexins have been identified on the parasite's tegument surface and excretory/secretory products, but their functions are still unknown. Here we report the cloning, sequencing, in silico analysis, and functional characterization of a Schistosoma bovis annexin. The predicted protein has typical annexin secondary and tertiary structures. Bioassays with the recombinant protein revealed that the protein is biologically active in vitro, showing fibrinolytic and anticoagulant properties. Finally, the expression of the native protein on the tegument surface of S. bovis schistosomula and adult worms is demonstrated, revealing the possibility of exposure to the host's immune system and thus offering a potential vaccine target for the control of schistosomiasis in ruminants. |
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Keywords: | Annexin Schistosoma bovis Plasminogen Anticoagulant activity Tegument |
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