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