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.