Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae)

Detalhes bibliográficos
Ano de defesa: 2016
Autor(a) principal: TAVARES, Caio Pavão lattes
Orientador(a): ROSA, Ivone Garros lattes
Banca de defesa: ROSA, Ivone Garros lattes, SOARES, Alexandra Martins dos Santos lattes, LIMA, Mayara Ingrid Sousa lattes
Tipo de documento: Dissertação
Tipo de acesso: Acesso aberto
Idioma: por
Instituição de defesa: Universidade Federal do Maranhão
Programa de Pós-Graduação: PROGRAMA DE PÓS-GRADUAÇÃO EM SAÚDE E AMBIENTE/CCBS
Departamento: DEPARTAMENTO DE PATOLOGIA/CCBS
País: Brasil
Palavras-chave em Português:
Palavras-chave em Inglês:
Área do conhecimento CNPq:
Link de acesso: https://tedebc.ufma.br/jspui/handle/tede/tede/3214
Resumo: Animal venoms have great importance for biotechnology, due to its wealth of components and biological applications. The apitoxin, bee venom of Apis mellifera L., is used as a pharmacological tool for the treatment of diseases as arthritis, cancer and fight against HIV. Lectins have been identified as components of various venoms. Lectin is a class of proteins, non-immunological origin, able to bind specific, reversible and non-covalently to carbohydrates or glycoconjugates. In the present work, we demonstrate the isolation and partial biochemical characterization of lectinic fraction from bee venom of Apis mellifera L. The bee venom was derived from bees raised in apiaries in São Bento, Maranhão, with electric collector use. The isolation of lectin fraction was accomplished by bioaffinity chromatography (affinity matrices of galactomannans). The fractions were analyzed by native and SDS-PAGE electrophoresis. The same fractions were subjected to the hemagglutination test on blood types A, B, AB and O followed by haemagglutination inhibition test for carbohydrates (glucose, mannose, galactose, sucrose and lactose). The divalent cations requirement test was performed using EDTA in hemagglutination system. The fraction was subjected to heating stability test where the samples were exposed to temperatures of 40, 50, 60, 70, 80, 90 and 100° C for 30 minutes and subsequently subjected to the determination of hemagglutinating activity. One lectin fraction D-galactose-biding and recognize α-galactosides was isolated from bee venom. It is 3,2% of the dry weight of bee venom. The electrophoresis analysis under denaturing conditions indicated that this fraction showed three bands with molecular weights of approximately 14, 17 and 19 kDa. When subjected to electrophoresis native (no SDS), the lectin fraction revealed only one band at the top of the gel, suggesting that these bands are subunits of the same protein. The hemagglutination activity was observed for the four human blood types, however, it showed greater sensitivity to the red cells of type A (2048 U.H./mL). The hemagglutination activity of this fraction was inhibited by lactose (150mM) and D-galactose (500mM), thus providing specificity for these two carbohydrates. EDTA (MIC = 0,156 mM) was also capable of inhibiting the hemagglutination activity, indicating that this lectin fraction is dependent on divalent cations. The isolated lectin fraction showed high thermostability being able to maintain its activity even after exposure to 70° C for 30 minutes. The bee venom of africanized bee Apis melliferra L. has no previous reports of the presence of lectins.
id UFMA_207cb8e4392f9485a4013272488914ca
oai_identifier_str oai:tede2:tede/3214
network_acronym_str UFMA
network_name_str Biblioteca Digital de Teses e Dissertações da UFMA
repository_id_str
spelling ROSA, Ivone Garros042034103-04http://lattes.cnpq.br/9599905005153701ROSA, Ivone Garros042034103-04http://lattes.cnpq.br/9599905005153701SOARES, Alexandra Martins dos Santoshttp://lattes.cnpq.br/6434212774237352LIMA, Mayara Ingrid Sousahttp://lattes.cnpq.br/7580136116595038044814603-77http://lattes.cnpq.br/3211114811586303TAVARES, Caio Pavão2021-02-22T13:37:54Z2016-07-29TAVARES, Caio Pavão. Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae). 2016. 91 f. Dissertação (Programa de Pós-Graduação em Saúde e Ambiente/CCBS) - Universidade Federal do Maranhão, São Luís, 2016.https://tedebc.ufma.br/jspui/handle/tede/tede/3214Animal venoms have great importance for biotechnology, due to its wealth of components and biological applications. The apitoxin, bee venom of Apis mellifera L., is used as a pharmacological tool for the treatment of diseases as arthritis, cancer and fight against HIV. Lectins have been identified as components of various venoms. Lectin is a class of proteins, non-immunological origin, able to bind specific, reversible and non-covalently to carbohydrates or glycoconjugates. In the present work, we demonstrate the isolation and partial biochemical characterization of lectinic fraction from bee venom of Apis mellifera L. The bee venom was derived from bees raised in apiaries in São Bento, Maranhão, with electric collector use. The isolation of lectin fraction was accomplished by bioaffinity chromatography (affinity matrices of galactomannans). The fractions were analyzed by native and SDS-PAGE electrophoresis. The same fractions were subjected to the hemagglutination test on blood types A, B, AB and O followed by haemagglutination inhibition test for carbohydrates (glucose, mannose, galactose, sucrose and lactose). The divalent cations requirement test was performed using EDTA in hemagglutination system. The fraction was subjected to heating stability test where the samples were exposed to temperatures of 40, 50, 60, 70, 80, 90 and 100° C for 30 minutes and subsequently subjected to the determination of hemagglutinating activity. One lectin fraction D-galactose-biding and recognize α-galactosides was isolated from bee venom. It is 3,2% of the dry weight of bee venom. The electrophoresis analysis under denaturing conditions indicated that this fraction showed three bands with molecular weights of approximately 14, 17 and 19 kDa. When subjected to electrophoresis native (no SDS), the lectin fraction revealed only one band at the top of the gel, suggesting that these bands are subunits of the same protein. The hemagglutination activity was observed for the four human blood types, however, it showed greater sensitivity to the red cells of type A (2048 U.H./mL). The hemagglutination activity of this fraction was inhibited by lactose (150mM) and D-galactose (500mM), thus providing specificity for these two carbohydrates. EDTA (MIC = 0,156 mM) was also capable of inhibiting the hemagglutination activity, indicating that this lectin fraction is dependent on divalent cations. The isolated lectin fraction showed high thermostability being able to maintain its activity even after exposure to 70° C for 30 minutes. The bee venom of africanized bee Apis melliferra L. has no previous reports of the presence of lectins.As peçonhas e venenos animais apresentam grande importância para a biotecnologia, devido sua riqueza de componentes e aplicações biológicas. A apitoxina, peçonha da abelha Apis mellifera L. é um produto que pode ser utilizado como ferramenta farmacológica para o tratamento de doenças como artrite, câncer e combate ao vírus do HIV. As lectinas vêm sendo detectadas como componentes de diversas peçonhas. Lectina é uma classe de proteínas, de origem não imunológica, capaz de se ligar específica, reversível e não covalentemente a carboidratos ou glicoconjugados. O objetivo deste trabalho é Isolar e caracterizar bioquimicamente a fração lectínica da apitoxina da abelha Apis mellifera L. A apitoxina foi adquirida de abelhas criadas em apiários no município de São Bento, Maranhão, com uso de coletor elétrico. O isolamento da fração lectínica foi realizado por meio de cromatografia de bioafinidade em matriz de galactomananas. Em seguida as frações foram analisadas por eletroforese nativa e SDS-PAGE. As frações foram submetidas ao teste de hemaglutinação sobre os tipos sanguíneos A, B, AB e O seguido de teste de inibição por carboidratos (glicose, manose, galactose, sacarose e lactose). O teste de requerimento de cátions divalentes foi realizado utilizando-se EDTA no sistema de hemaglutinação. A fração foi submetida ao teste de estabilidade por aquecimento, onde amostras foram expostas às temperaturas de 40, 50, 60, 70, 80, 90 e 100°C por 30 minutos e subsequentemente foram submetidas à determinação da atividade hemaglutinante. Uma fração lectínica ligante de D-galactose e que reconhece α-galactosídeos foi isolada da apitoxina da abelha Apis mellifera L., representando a porcentagem de 3,2% do peso seco da apitoxina. A análise eletroforética sob condição desnaturante (SDS-PAGE) da fração lectínica revelou três bandas com pesos moleculares de aproximadamente 14, 17 e 19 kDa. Ao ser submetida a uma eletroforese nativa (ausência de SDS), a fração lectínica revelou apenas uma banda no topo do gel, sugerindo que estas bandas sejam subunidades de uma mesma proteína. A atividade hemaglutinante foi observada para os 4 tipos sanguíneos humanos, no entanto, apresentou maior sensibilidade para os eritrócitos do tipo A (2048 U.H./mL). A atividade foi inibida por lactose (150mM) e D-galactose (500mM), apresentando assim especificidade por estes dois carboidratos. O EDTA (MIC = 0,156 mM) também foi capaz de inibir a atividade hemaglutinante, demonstrando que esta fração lectínica é dependente de cátions divalentes. A fração lectínica isolada demonstrou elevada termoestabilidade, sendo capaz de manter sua atividade mesmo após exposição a 70°C por 30 minutos. A apitoxina da abelha africanizada Apis melliferra L. não apresenta relatos anteriores da presença de lectinas.Submitted by Daniella Santos (daniella.santos@ufma.br) on 2021-02-22T13:37:54Z No. of bitstreams: 1 CAIOPAVÃO.pdf: 968486 bytes, checksum: 7ebd11e896e5ff8dd7b6daeff3c76da7 (MD5)Made available in DSpace on 2021-02-22T13:37:54Z (GMT). No. of bitstreams: 1 CAIOPAVÃO.pdf: 968486 bytes, checksum: 7ebd11e896e5ff8dd7b6daeff3c76da7 (MD5) Previous issue date: 2016-07-29application/pdfporUniversidade Federal do MaranhãoPROGRAMA DE PÓS-GRADUAÇÃO EM SAÚDE E AMBIENTE/CCBSUFMABrasilDEPARTAMENTO DE PATOLOGIA/CCBSApitoxinaApis mellifera L.Fração LectínicaHemaglutinaçãoBee venomApis mellifera L.Lectin fractionHemagglutinationPatologia AnimalEstudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae)Study of the lectin fraction of the bee Apitoxin Apis mellifera L. (Hymenoptera: Apidae)info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisinfo:eu-repo/semantics/openAccessreponame:Biblioteca Digital de Teses e Dissertações da UFMAinstname:Universidade Federal do Maranhão (UFMA)instacron:UFMAORIGINALCAIOPAVÃO.pdfCAIOPAVÃO.pdfapplication/pdf968486http://tedebc.ufma.br:8080/bitstream/tede/3214/2/CAIOPAV%C3%83O.pdf7ebd11e896e5ff8dd7b6daeff3c76da7MD52LICENSElicense.txtlicense.txttext/plain; charset=utf-82255http://tedebc.ufma.br:8080/bitstream/tede/3214/1/license.txt97eeade1fce43278e63fe063657f8083MD51tede/32142021-02-22 10:37:54.375oai:tede2: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Biblioteca Digital de Teses e Dissertaçõeshttps://tedebc.ufma.br/jspui/PUBhttp://tedebc.ufma.br:8080/oai/requestrepositorio@ufma.br||repositorio@ufma.bropendoar:21312021-02-22T13:37:54Biblioteca Digital de Teses e Dissertações da UFMA - Universidade Federal do Maranhão (UFMA)false
dc.title.por.fl_str_mv Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae)
dc.title.alternative.eng.fl_str_mv Study of the lectin fraction of the bee Apitoxin Apis mellifera L. (Hymenoptera: Apidae)
title Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae)
spellingShingle Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae)
TAVARES, Caio Pavão
Apitoxina
Apis mellifera L.
Fração Lectínica
Hemaglutinação
Bee venom
Apis mellifera L.
Lectin fraction
Hemagglutination
Patologia Animal
title_short Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae)
title_full Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae)
title_fullStr Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae)
title_full_unstemmed Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae)
title_sort Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae)
author TAVARES, Caio Pavão
author_facet TAVARES, Caio Pavão
author_role author
dc.contributor.advisor1.fl_str_mv ROSA, Ivone Garros
dc.contributor.advisor1ID.fl_str_mv 042034103-04
dc.contributor.advisor1Lattes.fl_str_mv http://lattes.cnpq.br/9599905005153701
dc.contributor.referee1.fl_str_mv ROSA, Ivone Garros
dc.contributor.referee1ID.fl_str_mv 042034103-04
dc.contributor.referee1Lattes.fl_str_mv http://lattes.cnpq.br/9599905005153701
dc.contributor.referee2.fl_str_mv SOARES, Alexandra Martins dos Santos
dc.contributor.referee2Lattes.fl_str_mv http://lattes.cnpq.br/6434212774237352
dc.contributor.referee3.fl_str_mv LIMA, Mayara Ingrid Sousa
dc.contributor.referee3Lattes.fl_str_mv http://lattes.cnpq.br/7580136116595038
dc.contributor.authorID.fl_str_mv 044814603-77
dc.contributor.authorLattes.fl_str_mv http://lattes.cnpq.br/3211114811586303
dc.contributor.author.fl_str_mv TAVARES, Caio Pavão
contributor_str_mv ROSA, Ivone Garros
ROSA, Ivone Garros
SOARES, Alexandra Martins dos Santos
LIMA, Mayara Ingrid Sousa
dc.subject.por.fl_str_mv Apitoxina
Apis mellifera L.
Fração Lectínica
Hemaglutinação
topic Apitoxina
Apis mellifera L.
Fração Lectínica
Hemaglutinação
Bee venom
Apis mellifera L.
Lectin fraction
Hemagglutination
Patologia Animal
dc.subject.eng.fl_str_mv Bee venom
Apis mellifera L.
Lectin fraction
Hemagglutination
dc.subject.cnpq.fl_str_mv Patologia Animal
description Animal venoms have great importance for biotechnology, due to its wealth of components and biological applications. The apitoxin, bee venom of Apis mellifera L., is used as a pharmacological tool for the treatment of diseases as arthritis, cancer and fight against HIV. Lectins have been identified as components of various venoms. Lectin is a class of proteins, non-immunological origin, able to bind specific, reversible and non-covalently to carbohydrates or glycoconjugates. In the present work, we demonstrate the isolation and partial biochemical characterization of lectinic fraction from bee venom of Apis mellifera L. The bee venom was derived from bees raised in apiaries in São Bento, Maranhão, with electric collector use. The isolation of lectin fraction was accomplished by bioaffinity chromatography (affinity matrices of galactomannans). The fractions were analyzed by native and SDS-PAGE electrophoresis. The same fractions were subjected to the hemagglutination test on blood types A, B, AB and O followed by haemagglutination inhibition test for carbohydrates (glucose, mannose, galactose, sucrose and lactose). The divalent cations requirement test was performed using EDTA in hemagglutination system. The fraction was subjected to heating stability test where the samples were exposed to temperatures of 40, 50, 60, 70, 80, 90 and 100° C for 30 minutes and subsequently subjected to the determination of hemagglutinating activity. One lectin fraction D-galactose-biding and recognize α-galactosides was isolated from bee venom. It is 3,2% of the dry weight of bee venom. The electrophoresis analysis under denaturing conditions indicated that this fraction showed three bands with molecular weights of approximately 14, 17 and 19 kDa. When subjected to electrophoresis native (no SDS), the lectin fraction revealed only one band at the top of the gel, suggesting that these bands are subunits of the same protein. The hemagglutination activity was observed for the four human blood types, however, it showed greater sensitivity to the red cells of type A (2048 U.H./mL). The hemagglutination activity of this fraction was inhibited by lactose (150mM) and D-galactose (500mM), thus providing specificity for these two carbohydrates. EDTA (MIC = 0,156 mM) was also capable of inhibiting the hemagglutination activity, indicating that this lectin fraction is dependent on divalent cations. The isolated lectin fraction showed high thermostability being able to maintain its activity even after exposure to 70° C for 30 minutes. The bee venom of africanized bee Apis melliferra L. has no previous reports of the presence of lectins.
publishDate 2016
dc.date.issued.fl_str_mv 2016-07-29
dc.date.accessioned.fl_str_mv 2021-02-22T13:37:54Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
format masterThesis
status_str publishedVersion
dc.identifier.citation.fl_str_mv TAVARES, Caio Pavão. Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae). 2016. 91 f. Dissertação (Programa de Pós-Graduação em Saúde e Ambiente/CCBS) - Universidade Federal do Maranhão, São Luís, 2016.
dc.identifier.uri.fl_str_mv https://tedebc.ufma.br/jspui/handle/tede/tede/3214
identifier_str_mv TAVARES, Caio Pavão. Estudo da fração lectínica da apitoxina da abelha Apis mellifera L. (Hymenoptera: Apidae). 2016. 91 f. Dissertação (Programa de Pós-Graduação em Saúde e Ambiente/CCBS) - Universidade Federal do Maranhão, São Luís, 2016.
url https://tedebc.ufma.br/jspui/handle/tede/tede/3214
dc.language.iso.fl_str_mv por
language por
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade Federal do Maranhão
dc.publisher.program.fl_str_mv PROGRAMA DE PÓS-GRADUAÇÃO EM SAÚDE E AMBIENTE/CCBS
dc.publisher.initials.fl_str_mv UFMA
dc.publisher.country.fl_str_mv Brasil
dc.publisher.department.fl_str_mv DEPARTAMENTO DE PATOLOGIA/CCBS
publisher.none.fl_str_mv Universidade Federal do Maranhão
dc.source.none.fl_str_mv reponame:Biblioteca Digital de Teses e Dissertações da UFMA
instname:Universidade Federal do Maranhão (UFMA)
instacron:UFMA
instname_str Universidade Federal do Maranhão (UFMA)
instacron_str UFMA
institution UFMA
reponame_str Biblioteca Digital de Teses e Dissertações da UFMA
collection Biblioteca Digital de Teses e Dissertações da UFMA
bitstream.url.fl_str_mv http://tedebc.ufma.br:8080/bitstream/tede/3214/2/CAIOPAV%C3%83O.pdf
http://tedebc.ufma.br:8080/bitstream/tede/3214/1/license.txt
bitstream.checksum.fl_str_mv 7ebd11e896e5ff8dd7b6daeff3c76da7
97eeade1fce43278e63fe063657f8083
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
repository.name.fl_str_mv Biblioteca Digital de Teses e Dissertações da UFMA - Universidade Federal do Maranhão (UFMA)
repository.mail.fl_str_mv repositorio@ufma.br||repositorio@ufma.br
_version_ 1809926261303148544