1 research outputs found
Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
Evolutionary and closer structural relationships are demonstrated by phylogenetic analysis, peptide prediction and molecular
modelling between Solanum tuberosum apyrase, Schistosoma mansoni SmATPase 2 and Leishmania braziliensis
NDPase. Specific protein domains are suggested to be potentially involved in the immune response, and also seem to be
conserved during host and parasite co-evolution. Significant IgG antibody reactivity was observed in sera from patients
with American cutaneous leishmaniasis (ACL) and schistosomiasis using potato apyrase as antigen in ELISA. S. mansoni
adult worm or egg, L. braziliensis promastigote (Lb) and Trypanosoma cruzi epimastigote (EPI) have ATP diphosphohydrolases,
and antigenic preparations of them were evaluated. In ACL patients, IgG seropositivity was about 43%
and 90% for Lb and potato apyrase, respectively, while IgM was lower (<19%) for both. In schistosomiasis patients IgM
(>40%) or IgG (100%) seropositivity for both soluble egg (SEA) and adult worm (SWAP) antigens was higher than that
found for potato apyrase (IgM=10%; IgG=39%). In Chagas disease, IgG seropositivity for EPI and potato apyrase was
97% and 17%, respectively, while the IgM was low (3%) for both antigens. The study of the conserved domains from both
parasite proteins and potato apyrase could lead to the development of new drug targets or molecular markers