IgE antibodies from schistosomiasis patients to recognize epitopes in potato apyrase

Abstract INTRODUCTION: High percentages of structural identity and cross-immunoreactivity have been reported between potato apyrase and Schistosoma mansoni ATP diphosphohydrolase (SmATPDases) isoforms, showing the existence of particular epitopes shared between these proteins. METHODS: Potato apyras...

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Bibliographic Details
Published in:Revista da Sociedade Brasileira de Medicina Tropical
Main Authors: Michélia Antônia do Nascimento Gusmão, Nayara Braga Emídio, Danielle Gomes Marconato, Priscila Silva Grijó Farani, Luiz Felipe Maniezzi, Paulo Marcos Zech Coelho, Rodrigo Correa Oliveira, Eveline Gomes Vasconcelos, Priscila de Faria-Pinto
Format: Article in Journal/Newspaper
Language:English
Published: Sociedade Brasileira de Medicina Tropical (SBMT) 2019
Subjects:
ATP diphosphohydrolase
IgE
Potato apyrase
Arctic medicine. Tropical medicine
RC955-962
Arctic
Online Access:https://doi.org/10.1590/0037-8682-0139-2018
https://doaj.org/article/6126f72de2a4441a978886b656437e6d
Description
Summary:Abstract INTRODUCTION: High percentages of structural identity and cross-immunoreactivity have been reported between potato apyrase and Schistosoma mansoni ATP diphosphohydrolase (SmATPDases) isoforms, showing the existence of particular epitopes shared between these proteins. METHODS: Potato apyrase was employed using ELISA, western blot, and mouse immunization methods to verify IgE reactivity. RESULTS: Most of the schistosomiasis patient’s (75%) serum was seropositive for potato apyrase and this protein was recognized using western blotting, suggesting that parasite and plant proteins share IgE-binding epitopes. C57BL/6 mice immunized with potato apyrase showed increased IgE antibody production. CONCLUSIONS: Potato apyrase and SmATPDases have IgE-binding epitopes.

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