Potato apyrase reduces granulomatous area and increases presence of multinucleated giant cells in murine schistosomiasis.
ATP diphosphohydrolase
Cross reactivity
Immunomodulation
NTPDase
Schistosoma mansoni
Journal
Parasitology international
ISSN: 1873-0329
Titre abrégé: Parasitol Int
Pays: Netherlands
ID NLM: 9708549
Informations de publication
Date de publication:
Aug 2021
Aug 2021
Historique:
received:
04
07
2020
revised:
23
02
2021
accepted:
25
02
2021
pubmed:
7
3
2021
medline:
22
9
2021
entrez:
6
3
2021
Statut:
ppublish
Résumé
Granulomas are inflammatory tissue responses directed to a set of antigens. Trapped Schistosoma mansoni eggs promote productive granulomas in the tissues, and they are the main damage caused by schistosomiasis. Some S. mansoni antigenic proteins may have a direct involvement in the resolution of the granulomatous response. The ATP diphosphohydrolases isoforms of this parasite are immunogenic, expressed in all phases of the parasite life cycle and secreted by eggs and adult worms. Potato apyrase is a vegetable protein that cross-reactive with parasite ATP diphosphohydrolases isoforms. In this study, the vegetable protein was purified, before being inoculated in C57BL/6 mice that were later infected with cercariae. Sixty days after infection, adult worms were recovered, antibodies and cytokines were measured, and morphological granuloma alterations evaluated. Immunization of the animals induced significant levels of IgG and IgG1 antibodies and IFN-γ, IL-10 and IL-5 cytokines, but not IL-13, suggesting that potato apyrase is an immunoregulatory protein. Supporting this hypothesis, it was found that liver damage associated with schistosomiasis was mitigated, reducing the size of the areas affected by granuloma to 35% and increasing the presence of multinucleated giant cells in this environment. In conclusion, potato apyrase was found to be effective immunomodulatory antigen for murine schistosomiasis.
Identifiants
pubmed: 33676013
pii: S1383-5769(21)00036-2
doi: 10.1016/j.parint.2021.102317
pii:
doi:
Substances chimiques
Apyrase
EC 3.6.1.5
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
102317Informations de copyright
Copyright © 2021 Elsevier B.V. All rights reserved.