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Characterization of antigenic proteins of the Taenia solium postoncospheral form.

Authors :
Chile N
Bernal-Teran EG
Condori BJ
Clark T
Garcia HH
Gilman RH
Verastegui MR
Source :
Molecular and biochemical parasitology [Mol Biochem Parasitol] 2024 Sep; Vol. 259, pp. 111621. Date of Electronic Publication: 2024 May 03.
Publication Year :
2024

Abstract

Neurocysticercosis is the leading cause for acquired epilepsy worldwide, and it is caused by the larval stage of the parasite Taenia solium. Several proteins of this stage have been characterized and studied to understand the parasite-host interaction, however, the proteins from the early cysticercus stages (the postoncospheral form) have not yet been characterized. The study of the postoncospheral form proteins is important to understand the host-parasite relationship in the early stages of infection. The aim of this work was to identify postoncospheral form antigenic proteins using sera from neurocysticercosis patients. T. solium activated oncospheres were cultured in HCT-8 cells to obtain the postoncospheral form. Soluble total and excretory/secretory proteins were obtained from the postoncospheral form and were incubated with both pool sera and individual serum of neurocysticercosis positive human patients. Immunoblotting showed target antigenic proteins with apparent molecular weights of 23 kDa and 46-48 kDa. The 46-48 kDa antigen bands present in soluble total and excretory/secretory postoncospheral form proteins were analyzed by LC-MS/MS; proteins identified were: nuclear elongation factor 1 alpha, enolase, unnamed protein product/antigen diagnostic GP50, calcium binding protein calreticulin precursor and annexin. The postoncospheral form expresses proteins related to interaction with the host, some of these proteins are predicted to be exosomal proteins. In conclusion, postoncospheral proteins are consistent targets of the humoral immune response in human and may serve as targets for diagnosis and vaccines.<br />Competing Interests: Declaration of Competing Interest None.<br /> (Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1872-9428
Volume :
259
Database :
MEDLINE
Journal :
Molecular and biochemical parasitology
Publication Type :
Academic Journal
Accession number :
38705360
Full Text :
https://doi.org/10.1016/j.molbiopara.2024.111621