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

Authors :
Sperotto RL
Kremer FS
Aires Berne ME
Costa de Avila LF
da Silva Pinto L
Monteiro KM
Caumo KS
Ferreira HB
Berne N
Borsuk S
Source :
Molecular and biochemical parasitology [Mol Biochem Parasitol] 2017 Jan; Vol. 211, pp. 39-47. Date of Electronic Publication: 2016 Sep 13.
Publication Year :
2017

Abstract

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.<br /> (Copyright © 2016 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1872-9428
Volume :
211
Database :
MEDLINE
Journal :
Molecular and biochemical parasitology
Publication Type :
Academic Journal
Accession number :
27638150
Full Text :
https://doi.org/10.1016/j.molbiopara.2016.09.002