Proteomic analysis of Toxocara canis excretory and secretory (TES) proteins

•This is the first study that identified the proteins present on TES using LC–MS/MS.•A total of 19 proteins were identified in the TES sample.•The identification of TES proteins can be useful for the use in diagnosis or vaccination. Toxocariasis is a neglected disease, and its main etiological agent...

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Published in:	Molecular and biochemical parasitology Vol. 211; pp. 39 - 47
Main Authors:	Sperotto, Rita Leal, Kremer, Frederico Schmitt, Aires Berne, Maria Elisabeth, Costa de Avila, Luciana F., da Silva Pinto, Luciano, Monteiro, Karina Mariante, Caumo, Karin Silva, Ferreira, Henrique Bunselmeyer, Berne, Natália, Borsuk, Sibele
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier B.V 01-01-2017
Subjects:	Animals Chromatography, Liquid Computational Biology - methods Dogs Exosomes - metabolism Female Helminth Proteins - secretion LC–MS/MS Proteome Proteomic analysis Proteomics - methods Secretory Vesicles - metabolism Tandem Mass Spectrometry TES Toxocara canis Toxocara canis - metabolism Toxocariasis - parasitology Toxocara canis Proteomic analysis TES LC–MS/MS
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Summary:	•This is the first study that identified the proteins present on TES using LC–MS/MS.•A total of 19 proteins were identified in the TES sample.•The identification of TES proteins can be useful for the use in diagnosis or vaccination. Toxocariasis is a neglected disease, and its main etiological agent is the nematode Toxocara canis. Serological diagnosis is performed by an enzyme-linked immunosorbent assay using T. canis excretory and secretory (TES) antigens produced by in vitro cultivation of larvae. Identification of TES proteins can be useful for the development of new diagnostic strategies since few TES components have been described so far. Herein, we report the results obtained by proteomic analysis of TES proteins using a liquid chromatography−tandem mass spectrometry (LC–MS/MS) approach. TES fractions were separated by one-dimensional SDS-PAGE and analyzed by LC–MS/MS. The MS/MS spectra were compared with a database of protein sequences deduced from the genome sequence of T. canis, and a total of 19 proteins were identified. Classification according to the signal peptide prediction using the SignalP server showed that seven of the identified proteins were extracellular, 10 had cytoplasmic or nuclear localization, while the subcellular localization of two proteins was unknown. Analysis of molecular functions by BLAST2GO showed that the majority of the gene ontology (GO) terms associated with the proteins present in the TES sample were associated with binding functions, including but not limited to protein binding (GO:0005515), inorganic ion binding (GO:0043167), and organic cyclic compound binding (GO:0097159). This study provides additional information about the exoproteome of T. canis, which can lead to the development of new strategies for diagnostics or vaccination.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0166-6851 1872-9428
DOI:	10.1016/j.molbiopara.2016.09.002