Purification and biological effects of a C-type lectin isolated from Bothrops moojeni

Detalhes bibliográficos
Autor(a) principal: Barbosa, P. S.F.
Data de Publicação: 2010
Outros Autores: Martins, A. M.C., Toyama, M. H. [UNESP], Joazeiro, P. P., Beriam, L. O.S., Fonteles, M. C., Monteiro, H. A.S.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1590/S1678-91992010000300016
http://hdl.handle.net/11449/226101
Resumo: Snake venom proteins from the C-type lectin family have very distinct biological activities despite their highly conserved primary structure, which is homologous to the carbohydrate recognition region of true C-type lectins. We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and investigated its effect on platelet aggregation, insulin secretion, antibacterial activity, and isolated kidney cells. The BmLec was purified using two chromatographic steps: affinity chromatography and reverse phase high performance liquid chromatography (HPLC). BmLec showed a dose-dependent platelet aggregation and significantly decreased the bacterial growth rate in approximately 15%. During scanning electron microscopy, the profile of Xanthomonas axonopodis pv. passiflorae treated with lectin disclosed a high vesiculation and membrane rupture. BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 μg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. In conclusion, the C-type lectin isolated from Bothrops moojeni affected platelet aggregation, insulin secretion, antibacterial activity and isolated kidney function. © CEVAP 2010.
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spelling Purification and biological effects of a C-type lectin isolated from Bothrops moojeniAntibacterial activityBothrops moojeniInsulinKidneyPlatelet aggregationSnake venom proteins from the C-type lectin family have very distinct biological activities despite their highly conserved primary structure, which is homologous to the carbohydrate recognition region of true C-type lectins. We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and investigated its effect on platelet aggregation, insulin secretion, antibacterial activity, and isolated kidney cells. The BmLec was purified using two chromatographic steps: affinity chromatography and reverse phase high performance liquid chromatography (HPLC). BmLec showed a dose-dependent platelet aggregation and significantly decreased the bacterial growth rate in approximately 15%. During scanning electron microscopy, the profile of Xanthomonas axonopodis pv. passiflorae treated with lectin disclosed a high vesiculation and membrane rupture. BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 μg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. In conclusion, the C-type lectin isolated from Bothrops moojeni affected platelet aggregation, insulin secretion, antibacterial activity and isolated kidney function. © CEVAP 2010.Department of Physiology and Pharmacology Federal University of Ceará, Fortaleza, Ceará StateDepartment of Clinical and Toxicological Analyses Federal University of Ceará, Fortaleza, Ceará StateSão Paulo Experimental Coast Campus São Paulo State University (UNESP - Univ Estadual Paulista), São Vicente, São Paulo StateDepartment of Histology Institute of Biology State University of Campinas, Campinas, São Paulo StateLaboratory of Plant Microbiology Experimental Center Biological Institute, Campinas, São Paulo StateSão Paulo Experimental Coast Campus São Paulo State University (UNESP - Univ Estadual Paulista), São Vicente, São Paulo StateFederal University of CearáUniversidade Estadual Paulista (UNESP)Universidade Estadual de Campinas (UNICAMP)Biological InstituteBarbosa, P. S.F.Martins, A. M.C.Toyama, M. H. [UNESP]Joazeiro, P. P.Beriam, L. O.S.Fonteles, M. C.Monteiro, H. A.S.2022-04-28T21:25:28Z2022-04-28T21:25:28Z2010-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article493-504http://dx.doi.org/10.1590/S1678-91992010000300016Journal of Venomous Animals and Toxins Including Tropical Diseases, v. 16, n. 3, p. 493-504, 2010.1678-9199http://hdl.handle.net/11449/22610110.1590/S1678-919920100003000162-s2.0-78049479441Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Venomous Animals and Toxins Including Tropical Diseasesinfo:eu-repo/semantics/openAccess2022-04-28T21:25:29Zoai:repositorio.unesp.br:11449/226101Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-06T00:06:57.124597Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
title Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
spellingShingle Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
Barbosa, P. S.F.
Antibacterial activity
Bothrops moojeni
Insulin
Kidney
Platelet aggregation
title_short Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
title_full Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
title_fullStr Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
title_full_unstemmed Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
title_sort Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
author Barbosa, P. S.F.
author_facet Barbosa, P. S.F.
Martins, A. M.C.
Toyama, M. H. [UNESP]
Joazeiro, P. P.
Beriam, L. O.S.
Fonteles, M. C.
Monteiro, H. A.S.
author_role author
author2 Martins, A. M.C.
Toyama, M. H. [UNESP]
Joazeiro, P. P.
Beriam, L. O.S.
Fonteles, M. C.
Monteiro, H. A.S.
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Federal University of Ceará
Universidade Estadual Paulista (UNESP)
Universidade Estadual de Campinas (UNICAMP)
Biological Institute
dc.contributor.author.fl_str_mv Barbosa, P. S.F.
Martins, A. M.C.
Toyama, M. H. [UNESP]
Joazeiro, P. P.
Beriam, L. O.S.
Fonteles, M. C.
Monteiro, H. A.S.
dc.subject.por.fl_str_mv Antibacterial activity
Bothrops moojeni
Insulin
Kidney
Platelet aggregation
topic Antibacterial activity
Bothrops moojeni
Insulin
Kidney
Platelet aggregation
description Snake venom proteins from the C-type lectin family have very distinct biological activities despite their highly conserved primary structure, which is homologous to the carbohydrate recognition region of true C-type lectins. We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and investigated its effect on platelet aggregation, insulin secretion, antibacterial activity, and isolated kidney cells. The BmLec was purified using two chromatographic steps: affinity chromatography and reverse phase high performance liquid chromatography (HPLC). BmLec showed a dose-dependent platelet aggregation and significantly decreased the bacterial growth rate in approximately 15%. During scanning electron microscopy, the profile of Xanthomonas axonopodis pv. passiflorae treated with lectin disclosed a high vesiculation and membrane rupture. BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 μg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. In conclusion, the C-type lectin isolated from Bothrops moojeni affected platelet aggregation, insulin secretion, antibacterial activity and isolated kidney function. © CEVAP 2010.
publishDate 2010
dc.date.none.fl_str_mv 2010-01-01
2022-04-28T21:25:28Z
2022-04-28T21:25:28Z
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.uri.fl_str_mv http://dx.doi.org/10.1590/S1678-91992010000300016
Journal of Venomous Animals and Toxins Including Tropical Diseases, v. 16, n. 3, p. 493-504, 2010.
1678-9199
http://hdl.handle.net/11449/226101
10.1590/S1678-91992010000300016
2-s2.0-78049479441
url http://dx.doi.org/10.1590/S1678-91992010000300016
http://hdl.handle.net/11449/226101
identifier_str_mv Journal of Venomous Animals and Toxins Including Tropical Diseases, v. 16, n. 3, p. 493-504, 2010.
1678-9199
10.1590/S1678-91992010000300016
2-s2.0-78049479441
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal of Venomous Animals and Toxins Including Tropical Diseases
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 493-504
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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