Cross-immunoreactivity between anti-potato apyrase antibodies and mammalian ATP diphosphohydrolases: potential use of the vegetal protein in experimental schistosomiasis

dc.creatorPinto, P. Faria
dc.creatorMeirelles, M. N. L.
dc.creatorLenzi, Henrique Leonel
dc.creatorMota, Ester Maria
dc.creatorPenido, M. L. O.
dc.creatorCoelho, Paulo Marcos Zach
dc.creatorVasconcelos, Eveline Gomes
dc.date2012-01-27T14:20:46Z
dc.date2012-01-27T14:20:46Z
dc.date2006
dc.date.accessioned2023-09-26T21:14:49Z
dc.date.available2023-09-26T21:14:49Z
dc.identifierFARIA-PINTO, P. et al. Cross-immunoreactivity between anti-potato apyrase antibodies and mammalian ATP diphosphohydrolases: potential use of the vegetal protein in experimental schistosomiasis. Memórias do Instituto Oswaldo Cruz. v.101, supl.1, p. 359-363, 2006.
dc.identifier0074-0276
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/3746
dc.identifier10.1590/S0074-02762006000900059
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8871450
dc.descriptionAcknowledgments to Dr Jair AK Aguiar for revising the manuscript.
dc.descriptionWe have previously showed that Schistosoma mansoni ATP-diphosphohydrolase and Solanum tuberosum potato apyrase share epitopes and the vegetable protein has immunostimulatory properties. Here, it was verified the in situ cross-immunoreactivity between mice NTPDases and anti-potato apyrase antibodies produced in rabbits, using confocal microscopy. Liver samples were taken from Swiss Webster mouse 8 weeks after infection with S. mansoni cercariae, and anti-potato apyrase and TRITC-conjugated anti-rabbit IgG antibody were tested on cryostat sections. The results showed that S. mansoni egg ATP diphosphohydrolase isoforms, developed by anti-potato apyrase, are expressed in miracidial and egg structures, and not in granulomatous cells and hepatic structures (hepatocytes, bile ducts, and blood vessels). Therefore, purified potato apyrase when inoculated in rabbit generates polyclonal sera containing anti-apyrase antibodies that are capable of recognizing specifically S. mansoni ATP diphosphohydrolase epitopes, but not proteins from mammalian tissues, suggesting that autoantibodies are not induced during potato apyrase immunization. A phylogenetic tree obtained for the NTPDase family showed that potato apyrase had lower homology with mammalian NTPDases 1-4, 7, and 8. Further analysis of potato apyrase epitopes could implement their potential use in schistosomiasis experimental models
dc.formatapplication/pdf
dc.languageeng
dc.publisherFundação Oswaldo Cruz. Instituto Oswaldo Cruz
dc.rightsopen access
dc.subjectCross-immunoreactivity
dc.subjectSchistosoma mansoni ATP diphosphohydrolase
dc.subjectMammalian NTPDases
dc.subjectPotato apyrase - granuloma
dc.subjectAdenosina Trifosfatases
dc.subjectImunologia
dc.subjectApirase
dc.subjectSchistosoma mansoni
dc.subjectEsquistossomose mansoni
dc.subjectAdenosina Trifosfatases
dc.subjectDados de Sequência Molecular
dc.subjectModelos Animais de Doenças
dc.titleCross-immunoreactivity between anti-potato apyrase antibodies and mammalian ATP diphosphohydrolases: potential use of the vegetal protein in experimental schistosomiasis
dc.typeArticle


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