Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases

Detalhes bibliográficos
Autor(a) principal: Faria-Pinto, Priscila de
Data de Publicação: 2008
Outros Autores: Soares, Fabrícia Aparecida Rezende, Molica, Andréia Maria, Montesano, Maria Angela, Marques, Marcos José, Rocha, Manoel Otávio da Costa, Coelho, Paulo Marcos Zech, Gomes, Juliana de Assis Silva, Enk, Martin Johannes, Oliveira, Rodrigo Corrêa, Maria Neto, Simone, Franco, Octávio Luiz, Vasconcelos, Eveline Gomes
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UCB
Texto Completo: http://twingo.ucb.br:8080/jspui/handle/10869/682
https://repositorio.ucb.br:9443/jspui/handle/123456789/7841
Resumo: 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.
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spelling Faria-Pinto, Priscila deSoares, Fabrícia Aparecida RezendeMolica, Andréia MariaMontesano, Maria AngelaMarques, Marcos JoséRocha, Manoel Otávio da CostaCoelho, Paulo Marcos ZechGomes, Juliana de Assis SilvaEnk, Martin JohannesOliveira, Rodrigo CorrêaCoelho, Paulo Marcos ZechMaria Neto, SimoneFranco, Octávio LuizVasconcelos, Eveline Gomes2016-10-10T03:52:51Z2016-10-10T03:52:51Z2008http://twingo.ucb.br:8080/jspui/handle/10869/682https://repositorio.ucb.br:9443/jspui/handle/123456789/7841Evolutionary 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.Made available in DSpace on 2016-10-10T03:52:51Z (GMT). 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dc.title.pt_BR.fl_str_mv Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
title Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
spellingShingle Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
Faria-Pinto, Priscila de
ATP diphosphohydrolase
Apyrase
NTPDase
Leishmania braziliensis
Schistosoma mansoni
Trypanosoma cruzi
Solanum tuberosum
Antibody
Molecular modelling
Phylogenetic
title_short Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
title_full Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
title_fullStr Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
title_full_unstemmed Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
title_sort Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
author Faria-Pinto, Priscila de
author_facet Faria-Pinto, Priscila de
Soares, Fabrícia Aparecida Rezende
Molica, Andréia Maria
Montesano, Maria Angela
Marques, Marcos José
Rocha, Manoel Otávio da Costa
Coelho, Paulo Marcos Zech
Gomes, Juliana de Assis Silva
Enk, Martin Johannes
Oliveira, Rodrigo Corrêa
Maria Neto, Simone
Franco, Octávio Luiz
Vasconcelos, Eveline Gomes
author_role author
author2 Soares, Fabrícia Aparecida Rezende
Molica, Andréia Maria
Montesano, Maria Angela
Marques, Marcos José
Rocha, Manoel Otávio da Costa
Coelho, Paulo Marcos Zech
Gomes, Juliana de Assis Silva
Enk, Martin Johannes
Oliveira, Rodrigo Corrêa
Maria Neto, Simone
Franco, Octávio Luiz
Vasconcelos, Eveline Gomes
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Faria-Pinto, Priscila de
Soares, Fabrícia Aparecida Rezende
Molica, Andréia Maria
Montesano, Maria Angela
Marques, Marcos José
Rocha, Manoel Otávio da Costa
Coelho, Paulo Marcos Zech
Gomes, Juliana de Assis Silva
Enk, Martin Johannes
Oliveira, Rodrigo Corrêa
Coelho, Paulo Marcos Zech
Maria Neto, Simone
Franco, Octávio Luiz
Vasconcelos, Eveline Gomes
dc.subject.por.fl_str_mv ATP diphosphohydrolase
Apyrase
NTPDase
Leishmania braziliensis
Schistosoma mansoni
Trypanosoma cruzi
Solanum tuberosum
Antibody
Molecular modelling
Phylogenetic
topic ATP diphosphohydrolase
Apyrase
NTPDase
Leishmania braziliensis
Schistosoma mansoni
Trypanosoma cruzi
Solanum tuberosum
Antibody
Molecular modelling
Phylogenetic
dc.description.abstract.por.fl_txt_mv 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.
dc.description.version.pt_BR.fl_txt_mv Sim
dc.description.status.pt_BR.fl_txt_mv Publicado
description 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.
publishDate 2008
dc.date.issued.fl_str_mv 2008
dc.date.accessioned.fl_str_mv 2016-10-10T03:52:51Z
dc.date.available.fl_str_mv 2016-10-10T03:52:51Z
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