Mapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseases
Autor(a) principal: | |
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Data de Publicação: | 2008 |
Outros Autores: | , , , , , , , , , , , |
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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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). No. of bitstreams: 5 Mapping of the conserved antigenic domains shared between.PDF: 249741 bytes, checksum: 6ac6ab0d5b30165c912bd06b1e723817 (MD5) license_url: 52 bytes, checksum: 2f32edb9c19a57e928372a33fd08dba5 (MD5) license_text: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5) license_rdf: 24623 bytes, checksum: 378d22d8fe50e084ee2f354be78cbe62 (MD5) license.txt: 1887 bytes, checksum: 445d1980f282ec865917de35a4c622f6 (MD5) Previous issue date: 2008SimPublicadoTextoATP diphosphohydrolaseApyraseNTPDaseLeishmania braziliensisSchistosoma mansoniTrypanosoma cruziSolanum tuberosumAntibodyMolecular modellingPhylogeneticMapping of the conserved antigenic domains shared between potato apyrase and parasite ATP diphosphohydrolases: potential application in human parasitic diseasesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleParasitologyinfo:eu-repo/semantics/openAccessengreponame:Repositório Institucional da UCBinstname:Universidade Católica de Brasília (UCB)instacron:UCBORIGINALMapping of the conserved antigenic domains shared between.PDFapplication/pdf249741https://200.214.135.178:9443/jspui/bitstream/123456789/7841/1/Mapping%20of%20the%20conserved%20antigenic%20domains%20shared%20between.PDF6ac6ab0d5b30165c912bd06b1e723817MD51CC-LICENSElicense_urlapplication/octet-stream52https://200.214.135.178:9443/jspui/bitstream/123456789/7841/2/license_url2f32edb9c19a57e928372a33fd08dba5MD52license_textapplication/octet-stream0https://200.214.135.178:9443/jspui/bitstream/123456789/7841/3/license_textd41d8cd98f00b204e9800998ecf8427eMD53license_rdfapplication/octet-stream24623https://200.214.135.178:9443/jspui/bitstream/123456789/7841/4/license_rdf378d22d8fe50e084ee2f354be78cbe62MD54LICENSElicense.txttext/plain1887https://200.214.135.178:9443/jspui/bitstream/123456789/7841/5/license.txt445d1980f282ec865917de35a4c622f6MD55TEXTMapping of the conserved antigenic domains shared between.PDF.txtMapping of the conserved antigenic domains shared between.PDF.txtExtracted texttext/plain43765https://200.214.135.178:9443/jspui/bitstream/123456789/7841/6/Mapping%20of%20the%20conserved%20antigenic%20domains%20shared%20between.PDF.txte7a48a19f5d12c6bdcdf11e0b1ed154fMD56123456789/78412017-01-17 15:11:07.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ório de Publicaçõeshttps://repositorio.ucb.br:9443/jspui/ |
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 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
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publishedVersion |
format |
article |
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http://twingo.ucb.br:8080/jspui/handle/10869/682 https://repositorio.ucb.br:9443/jspui/handle/123456789/7841 |
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http://twingo.ucb.br:8080/jspui/handle/10869/682 https://repositorio.ucb.br:9443/jspui/handle/123456789/7841 |
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eng |
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eng |
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openAccess |
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