Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da FIOCRUZ (ARCA) |
Texto Completo: | https://www.arca.fiocruz.br/handle/icict/15539 |
Resumo: | Universidade Federal de Juiz de Fora. Instituto de Ciências Biológicas. Departamento de Bioquímica. Pós-Graduação em Imunologia e DIP/Genética e Biotecnologia. Juiz de Fora, MG, Brasil. |
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Porcino, Gabriane NascimentoCampos, Cristiane CarvalhoMaia, Ana Carolina Ribeiro GomesDetoni, Michelle LimaPinto, Priscila FariaCoimbra, Elaine SoaresMarques, Marcos JoséJuliano, Maria AparecidaJuliano, LuizDiniz, Vanessa ÁlvaroCorte-Real, SuzanaVasconcelos, Eveline Gomes2016-08-30T15:39:25Z2016-08-30T15:39:25Z2012PORCINO, Gabriane Nascimento; et al. Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): Localization and in vitro inhibition of promastigotes growth by polyclonal antibodies. Experimental Parasitology, v.132, n.2, p.293-299, Oct. 2012.0014-4894https://www.arca.fiocruz.br/handle/icict/1553910.1016/j.exppara.2012.08.0091090-2449engElsevierLeishmaniosePeptídeosApiraseImunocitoquímicaNucleosídeo-TrifosfataseApyraseATP diphosphohydrolaseNTPasePeptideLeishmaniasisImmunocytochemicalLeishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodiesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleUniversidade Federal de Juiz de Fora. Instituto de Ciências Biológicas. Departamento de Bioquímica. Pós-Graduação em Imunologia e DIP/Genética e Biotecnologia. Juiz de Fora, MG, Brasil.Universidade Federal de Juiz de Fora. Instituto de Ciências Biológicas. Departamento de Bioquímica. Pós-Graduação em Imunologia e DIP/Genética e Biotecnologia. Juiz de Fora, MG, Brasil.Universidade Federal de Juiz de Fora. Instituto de Ciências Biológicas. Departamento de Bioquímica. Pós-Graduação em Imunologia e DIP/Genética e Biotecnologia. Juiz de Fora, MG, Brasil.Universidade Federal de Juiz de Fora. Instituto de Ciências Biológicas. Departamento de Bioquímica. Pós-Graduação em Imunologia e DIP/Genética e Biotecnologia. Juiz de Fora, MG, Brasil.Universidade Federal de Juiz de Fora. Instituto de Ciências Biológicas. Departamento de Bioquímica. Pós-Graduação em Imunologia e DIP/Genética e Biotecnologia. Juiz de Fora, MG, Brasil.Universidade Federal de Juiz de Fora. Instituto de Ciências Biológicas. Departamento de Bioquímica. Pós-Graduação em Imunologia e DIP/Genética e Biotecnologia. Juiz de Fora, MG, Brasil.Universidade Federal de Alfenas. Instituto de Ciências Biomédicas. Departamento de Ciências Biológicas. Alfenas, MG, Brasil.Universidade Federal de São Paulo. Escola Paulista de Medicina. Departamento de Biofísica. São Paulo, SP, Brasil.Universidade Federal de São Paulo. Escola Paulista de Medicina. Departamento de Biofísica. São Paulo, SP, Brasil.Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Estrutural. Rio de Janeiro, RJ, Brasil.Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Estrutural. Rio de Janeiro, RJ, Brasil.Universidade Federal de Juiz de Fora. Instituto de Ciências Biológicas. Departamento de Bioquímica. Pós-Graduação em Imunologia e DIP/Genética e Biotecnologia. Juiz de Fora, MG, Brasil.Nucleoside triphosphate diphosphohydrolase (NTPDase) activity was recently characterized in Leishmania (Viannia) braziliensis promastigotes (Lb), and an antigenic conserved domain (r82-121) from the specific NTPDase 1 isoform was identified. In this work, mouse polyclonal antibodies produced against two synthetic peptides derived from this domain (LbB1LJ, r82-103; LbB2LJ, r102-121) were used. The anti-LbB1LJ or anti-LbB2LJ antibodies were immobilized on protein A-sepharose and immunoprecipitated the NTPDase 1 of 48 kDa and depleted approximately 40% of the phosphohydrolytic activity from detergent-homogenized Lb preparation. Ultrastructural immunocytochemical microscopy identified the NTPDase 1 on the parasite surface and in its subcellular cytoplasmic vesicles, mitochondria, kinetoplast and nucleus. The ATPase and ADPase activities of detergent-homogenized Lb preparation were partially inhibited by anti-LbB1LJ antibody (43-79%), which was more effective than that inhibition (18-47%) by anti-LbB2LJ antibody. In addition, the immune serum anti-LbB1LJ (67%) or anti-LbB2LJ (33%) was cytotoxic, significantly reducing the promastigotes growth in vitro. The results appoint the conserved domain from the L. braziliensis NTPDase as an important target for inhibitor design and the potential application of these biomolecules in experimental protocols of disease control.info:eu-repo/semantics/openAccessreponame:Repositório Institucional da FIOCRUZ (ARCA)instname:Fundação Oswaldo Cruz (FIOCRUZ)instacron:FIOCRUZLICENSElicense.txtlicense.txttext/plain; charset=utf-82991https://www.arca.fiocruz.br/bitstream/icict/15539/1/license.txt5a560609d32a3863062d77ff32785d58MD51ORIGINALvanessa_diniz_etal_IOC_2012.pdfvanessa_diniz_etal_IOC_2012.pdfapplication/pdf726309https://www.arca.fiocruz.br/bitstream/icict/15539/2/vanessa_diniz_etal_IOC_2012.pdfb3868905d222156e9dbc2372db35cff5MD52TEXTvanessa_diniz_etal_IOC_2012.pdf.txtvanessa_diniz_etal_IOC_2012.pdf.txtExtracted texttext/plain41674https://www.arca.fiocruz.br/bitstream/icict/15539/3/vanessa_diniz_etal_IOC_2012.pdf.txt35d5097eaddbcfd0010990afd1778303MD53icict/155392018-04-02 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dc.title.pt_BR.fl_str_mv |
Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies |
title |
Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies |
spellingShingle |
Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies Porcino, Gabriane Nascimento Leishmaniose Peptídeos Apirase Imunocitoquímica Nucleosídeo-Trifosfatase Apyrase ATP diphosphohydrolase NTPase Peptide Leishmaniasis Immunocytochemical |
title_short |
Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies |
title_full |
Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies |
title_fullStr |
Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies |
title_full_unstemmed |
Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies |
title_sort |
Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies |
author |
Porcino, Gabriane Nascimento |
author_facet |
Porcino, Gabriane Nascimento Campos, Cristiane Carvalho Maia, Ana Carolina Ribeiro Gomes Detoni, Michelle Lima Pinto, Priscila Faria Coimbra, Elaine Soares Marques, Marcos José Juliano, Maria Aparecida Juliano, Luiz Diniz, Vanessa Álvaro Corte-Real, Suzana Vasconcelos, Eveline Gomes |
author_role |
author |
author2 |
Campos, Cristiane Carvalho Maia, Ana Carolina Ribeiro Gomes Detoni, Michelle Lima Pinto, Priscila Faria Coimbra, Elaine Soares Marques, Marcos José Juliano, Maria Aparecida Juliano, Luiz Diniz, Vanessa Álvaro Corte-Real, Suzana Vasconcelos, Eveline Gomes |
author2_role |
author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Porcino, Gabriane Nascimento Campos, Cristiane Carvalho Maia, Ana Carolina Ribeiro Gomes Detoni, Michelle Lima Pinto, Priscila Faria Coimbra, Elaine Soares Marques, Marcos José Juliano, Maria Aparecida Juliano, Luiz Diniz, Vanessa Álvaro Corte-Real, Suzana Vasconcelos, Eveline Gomes |
dc.subject.other.pt_BR.fl_str_mv |
Leishmaniose Peptídeos Apirase Imunocitoquímica Nucleosídeo-Trifosfatase |
topic |
Leishmaniose Peptídeos Apirase Imunocitoquímica Nucleosídeo-Trifosfatase Apyrase ATP diphosphohydrolase NTPase Peptide Leishmaniasis Immunocytochemical |
dc.subject.en.pt_BR.fl_str_mv |
Apyrase ATP diphosphohydrolase NTPase Peptide Leishmaniasis Immunocytochemical |
description |
Universidade Federal de Juiz de Fora. Instituto de Ciências Biológicas. Departamento de Bioquímica. Pós-Graduação em Imunologia e DIP/Genética e Biotecnologia. Juiz de Fora, MG, Brasil. |
publishDate |
2012 |
dc.date.issued.fl_str_mv |
2012 |
dc.date.accessioned.fl_str_mv |
2016-08-30T15:39:25Z |
dc.date.available.fl_str_mv |
2016-08-30T15:39:25Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
PORCINO, Gabriane Nascimento; et al. Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): Localization and in vitro inhibition of promastigotes growth by polyclonal antibodies. Experimental Parasitology, v.132, n.2, p.293-299, Oct. 2012. |
dc.identifier.uri.fl_str_mv |
https://www.arca.fiocruz.br/handle/icict/15539 |
dc.identifier.issn.pt_BR.fl_str_mv |
0014-4894 |
dc.identifier.doi.none.fl_str_mv |
10.1016/j.exppara.2012.08.009 |
dc.identifier.eissn.none.fl_str_mv |
1090-2449 |
identifier_str_mv |
PORCINO, Gabriane Nascimento; et al. Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): Localization and in vitro inhibition of promastigotes growth by polyclonal antibodies. Experimental Parasitology, v.132, n.2, p.293-299, Oct. 2012. 0014-4894 10.1016/j.exppara.2012.08.009 1090-2449 |
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https://www.arca.fiocruz.br/handle/icict/15539 |
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eng |
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eng |
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info:eu-repo/semantics/openAccess |
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openAccess |
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Elsevier |
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Elsevier |
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