An antigenic domain within a catalytically active leishmania infantum nucleoside triphosphate diphosphohydrolase (NTPDase 1) is a target of inhibitory antibodies.
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Data
2013
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Resumo
Weidentified a shared B domainwithin nucleoside triphosphate diphosphohydrolases (NTPDases) of plants and
parasites. Now, an NTPDase activity not affected by inhibitors of adenylate kinase and ATPases was detected
in Leishmania infantum promastigotes. By non-denaturing gel electrophoresis of detergent-homogenized
promastigote preparation, an active band hydrolyzing nucleosides di- and triphosphate was visualized and, following
SDS-PAGE and silver staining was identified as a single polypeptide of 50 kDa. By Western blots, it was
recognized by immune sera raised against potato apyrase (SA), r-pot B domain (SB), a recombinant polypeptide
derived fromthe potato apyrase, and LbB1LJ (SC) or LbB2LJ (SD), synthetic peptides derived fromthe Leishmania
NTPDase 1, and by serum samples from dogs with visceral leishmaniasis, identifying the antigenic L. infantum
NTPDase 1 and, also, its conserved B domain (r83–122). By immunoprecipitation assays andWestern blots, immune
sera SA and SB identified the catalytically active NTPDase 1 in promastigote preparation. In addition, the
immune sera SB (44%) and SC or SD (87–99%) inhibited its activity, suggesting a direct effect on the B domain.
By ELISA, 37%, 45% or 50% of 38 infected dogs were seropositive for r-pot B domain, LbB1LJ and LbB2LJ, respectively,
confirming the B domain antigenicity.
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Potato apyrase, Conserved domain, Visceral leishmaniasis
Citação
MAIA, A. C. R. G. et al. An antigenic domain within a catalytically active leishmania infantum nucleoside triphosphate diphosphohydrolase (NTPDase 1) is a target of inhibitory antibodies. Parasitology International, v. 18, p.44-52, 2013. Disponível em: <http://www.sciencedirect.com/science/article/pii/S1383576912001274>. Acesso em: 10 out. 2016.