Echinostoma caproni: Identification of enolase in excretory/secretory products, molecular cloning, and functional expression

In order to investigate molecules that could be involved in host-trematode relationships, we have analysed the excretory/secretory products (ESP) of Echinostoma caproni following a proteomic approach. Actin, Gluthathione S-transferase (GST) and enolase have been identified in the ESP. Enolase, obser...

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Bibliographic Details
Published in:Experimental parasitology 2007-09, Vol.117 (1), p.57-64
Main Authors: Marcilla, Antonio, Pérez-García, Ana, Espert, Ana, Bernal, Dolores, Muñoz-Antolí, Carla, Esteban, José Guillermo, Toledo, Rafael
Format: Article
Language:English
Subjects:
2DE
Amino Acid Sequence
Animals
Biological and medical sciences
Blotting, Western
Cloning, Molecular
Cricetinae
Echinostoma - enzymology
Echinostoma - genetics
Echinostoma caproni
Electrophoresis, Gel, Two-Dimensional
Electrophoresis, Polyacrylamide Gel
Enolase
Escherichia coli
ESP
Excretory/secretory products
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation, Enzymologic
Humans
Life cycle. Host-agent relationship. Pathogenesis
Male
Mesocricetus
Molecular cloning and expression
Molecular Sequence Data
Open reading frame
ORF
Phosphopyruvate Hydratase - chemistry
Phosphopyruvate Hydratase - genetics
Phosphopyruvate Hydratase - isolation & purification
Phosphopyruvate Hydratase - metabolism
Plasminogen - metabolism
Protozoa
Rats
Rats, Wistar
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Reverse Transcriptase Polymerase Chain Reaction
Sequence Alignment
Sequence Homology, Amino Acid
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Two-dimension gel electrophoresis
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Summary:In order to investigate molecules that could be involved in host-trematode relationships, we have analysed the excretory/secretory products (ESP) of Echinostoma caproni following a proteomic approach. Actin, Gluthathione S-transferase (GST) and enolase have been identified in the ESP. Enolase, observed to be one of the most abundant proteins, was further characterized. The molecular cloning and in vitro expression in Escherichia coli of E. caproni enolase allowed us to determine that the protein contains 431 amino acids and a theoretical MW of 46272 Da. E. caproni enolase shows high homology to other trematode enolases. The recombinant protein binds specifically to human plasminogen in vitro, as observed for the native protein, confirming its properties as a host-interacting molecule.
ISSN:0014-4894
1090-2449
DOI:10.1016/j.exppara.2007.03.011