Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2)
| Ano de defesa: | 2024 |
|---|---|
| Autor(a) principal: | |
| Orientador(a): | |
| Banca de defesa: | |
| Tipo de documento: | Dissertação |
| Tipo de acesso: | Acesso aberto |
| Idioma: | por |
| Instituição de defesa: |
Não Informado pela instituição
|
| Programa de Pós-Graduação: |
Não Informado pela instituição
|
| Departamento: |
Não Informado pela instituição
|
| País: |
Não Informado pela instituição
|
| Área do conhecimento CNPq: | |
| Link de acesso: | http://repositorio.ufc.br/handle/riufc/81122 |
Resumo: | Sponges, phylum Porifera (from the Latin porus, pore + beast, bearer), are multicellular beings whose body consists of a mass of cells immersed in a gelatinous matrix and perforated by a complex system of canals. The genus Haliclona includes species widely distributed throughout the oceans, occurring at different depths and presenting a variety of colors. Throughout evolution, sponges have developed several physiological and phenotypic adaptations to maintain themselves in the marine environment. One of these adaptations was the production of metabolites, among which lectins stand out. These proteins of non-immune origin have the ability to bind specifically and reversibly to carbohydrates. Several biological activities associated with these molecules have been described, including anticancer, antiviral, antifungal and antibacterial properties. The present study aims to evaluate the antibacterial and antibiofilm potential of Halilectin (H-2), present in the sponge Haliclona caerulea. H-2 is a homodimeric protein with 15 kDa monomers interconnected by weakly interacting bonds that oligomerize to form a 29 kDa dimer. The lectin showed affinity for the glycoproteins asialofetuin, fetuin, and porcine stomach mucin type II and type III (PSM). Circular dichroism analysis demonstrated the predominant presence of β-sheet structures with spectra of β1 proteins. H-2 was able to agglutinate Staphylococcus aureus ATCC 25923, Staphylococcus aureus ATCC 700698, and Escherichia coli ATCC 11303 cells. The lectin showed antibacterial potential, since when associated with tetracycline, the protein potentiated the effect of the antibiotic, in addition to inhibiting biofilm formation. Thus, H-2 was shown to be a lectin with high biotechnological potential with antibacterial action in association with the antibiotic tetracycline. |
| id |
UFC-7_f9e144daeaea123676e31edd7a9382d9 |
|---|---|
| oai_identifier_str |
oai:repositorio.ufc.br:riufc/81122 |
| network_acronym_str |
UFC-7 |
| network_name_str |
Repositório Institucional da Universidade Federal do Ceará (UFC) |
| repository_id_str |
|
| spelling |
Cândido, José Gabriel de SousaCarneiro, Rômulo FariasSampaio, Alexandre Holanda2025-05-29T16:22:58Z2025-05-29T16:22:58Z2024CÂNDIDO, José Gabriel de Sousa. Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2). 2025. Dissertação (Mestrado em Biotecnologia de Recursos Naturais) – Centro de Ciências Agrárias, Universidade Federal do Ceará, Fortaleza, 2024.http://repositorio.ufc.br/handle/riufc/81122Sponges, phylum Porifera (from the Latin porus, pore + beast, bearer), are multicellular beings whose body consists of a mass of cells immersed in a gelatinous matrix and perforated by a complex system of canals. The genus Haliclona includes species widely distributed throughout the oceans, occurring at different depths and presenting a variety of colors. Throughout evolution, sponges have developed several physiological and phenotypic adaptations to maintain themselves in the marine environment. One of these adaptations was the production of metabolites, among which lectins stand out. These proteins of non-immune origin have the ability to bind specifically and reversibly to carbohydrates. Several biological activities associated with these molecules have been described, including anticancer, antiviral, antifungal and antibacterial properties. The present study aims to evaluate the antibacterial and antibiofilm potential of Halilectin (H-2), present in the sponge Haliclona caerulea. H-2 is a homodimeric protein with 15 kDa monomers interconnected by weakly interacting bonds that oligomerize to form a 29 kDa dimer. The lectin showed affinity for the glycoproteins asialofetuin, fetuin, and porcine stomach mucin type II and type III (PSM). Circular dichroism analysis demonstrated the predominant presence of β-sheet structures with spectra of β1 proteins. H-2 was able to agglutinate Staphylococcus aureus ATCC 25923, Staphylococcus aureus ATCC 700698, and Escherichia coli ATCC 11303 cells. The lectin showed antibacterial potential, since when associated with tetracycline, the protein potentiated the effect of the antibiotic, in addition to inhibiting biofilm formation. Thus, H-2 was shown to be a lectin with high biotechnological potential with antibacterial action in association with the antibiotic tetracycline.As esponjas, filo Porífera (do latim porus, poro + fera, portador de), são seres multicelulares, cujo corpo consiste em uma massa de células imersa em uma matriz gelatinosa, e perfurada por um complexo sistema de canais. O gênero Haliclona, inclui espécies amplamente distribuídas por todos os oceanos, ocorrendo em diferentes profundidades e apresentando uma variedade de cores. Ao longo da evolução, as esponjas desenvolveram diversas adaptações fisiológicas e fenotípicas para se manterem no ambiente marinho. Uma dessas adaptações foi a produção de metabolitos, entre os quais se destacam as lectinas. Essas proteínas de origem não imune, possuem a capacidade de se ligar de forma especifica e reversível a carboidratos. Já foram descritas diversas atividades biológicas associada à essas moléculas, incluindo propriedades anticancerígenas, antivirais, antifúngicas e antibacterianas. O presente trabalho tem como objetivo avaliar o potencial antibacteriano e antibiofilme da Halilectina (H-2), presente na esponja Haliclona caerulea. H-2 é uma proteína homodimérica com monômeros de 15 kDa interligados por ligações de interações fracas que se oligomeriza formando um dímero de 29 kDa. A lectina apresentou afinidade pelas glicoproteínas asialofetuina, fetuína, mucina estômago de porco tipo II e tipo III (PSM - porcine stomach mucin). A análise de dicroísmo circular demonstrou a presença predominante de estruturas β-folhas com espectros de proteínas-β1. A H-2 foi capaz de aglutinar células de Staphylococcus aureus ATCC 25923, Staphylococcus aureus ATCC 700698 e Escherichia coli ATCC 11303. A lectina apresentou potencial antibacteriano, visto que quando associada com tetraciclina a proteína potencializou o efeito do antibiótico, além de inibir a formação de biofilme. Assim, H-2 demonstrou ser uma lectina com elevado potencial biotecnológico com ação antibacteriana em associação ao antibiótico tetraciclina.Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2)info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisEsponjas marinhasLectinasSinergismoAtividade antibacterianaMarine spongesLectinsSynergismAntibacterial activityCNPQ::CIENCIAS BIOLOGICASinfo:eu-repo/semantics/openAccessporreponame:Repositório Institucional da Universidade Federal do Ceará (UFC)instname:Universidade Federal do Ceará (UFC)instacron:UFChttps://orcid.org/0009-0009-7671-8266https://lattes.cnpq.br/7183421168176641https://orcid.org/0000-0003-3871-0502http://lattes.cnpq.br/3049512216393338https://orcid.org/0000-0003-0024-2512http://lattes.cnpq.br/86614497341289552025-05-29LICENSElicense.txtlicense.txttext/plain; charset=utf-81748http://repositorio.ufc.br/bitstream/riufc/81122/4/license.txt8a4605be74aa9ea9d79846c1fba20a33MD54ORIGINAL2024_dis_jgscandido.pdf2024_dis_jgscandido.pdfapplication/pdf1156955http://repositorio.ufc.br/bitstream/riufc/81122/3/2024_dis_jgscandido.pdf0e2298813243bca882b647a578e7feffMD53riufc/811222025-05-30 07:34:34.014oai:repositorio.ufc.br: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Repositório InstitucionalPUBhttp://www.repositorio.ufc.br/ri-oai/requestbu@ufc.br || repositorio@ufc.bropendoar:2025-05-30T10:34:34Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)false |
| dc.title.pt_BR.fl_str_mv |
Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2) |
| title |
Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2) |
| spellingShingle |
Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2) Cândido, José Gabriel de Sousa CNPQ::CIENCIAS BIOLOGICAS Esponjas marinhas Lectinas Sinergismo Atividade antibacteriana Marine sponges Lectins Synergism Antibacterial activity |
| title_short |
Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2) |
| title_full |
Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2) |
| title_fullStr |
Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2) |
| title_full_unstemmed |
Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2) |
| title_sort |
Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2) |
| author |
Cândido, José Gabriel de Sousa |
| author_facet |
Cândido, José Gabriel de Sousa |
| author_role |
author |
| dc.contributor.co-advisor.none.fl_str_mv |
Carneiro, Rômulo Farias |
| dc.contributor.author.fl_str_mv |
Cândido, José Gabriel de Sousa |
| dc.contributor.advisor1.fl_str_mv |
Sampaio, Alexandre Holanda |
| contributor_str_mv |
Sampaio, Alexandre Holanda |
| dc.subject.cnpq.fl_str_mv |
CNPQ::CIENCIAS BIOLOGICAS |
| topic |
CNPQ::CIENCIAS BIOLOGICAS Esponjas marinhas Lectinas Sinergismo Atividade antibacteriana Marine sponges Lectins Synergism Antibacterial activity |
| dc.subject.ptbr.pt_BR.fl_str_mv |
Esponjas marinhas Lectinas Sinergismo Atividade antibacteriana |
| dc.subject.en.pt_BR.fl_str_mv |
Marine sponges Lectins Synergism Antibacterial activity |
| description |
Sponges, phylum Porifera (from the Latin porus, pore + beast, bearer), are multicellular beings whose body consists of a mass of cells immersed in a gelatinous matrix and perforated by a complex system of canals. The genus Haliclona includes species widely distributed throughout the oceans, occurring at different depths and presenting a variety of colors. Throughout evolution, sponges have developed several physiological and phenotypic adaptations to maintain themselves in the marine environment. One of these adaptations was the production of metabolites, among which lectins stand out. These proteins of non-immune origin have the ability to bind specifically and reversibly to carbohydrates. Several biological activities associated with these molecules have been described, including anticancer, antiviral, antifungal and antibacterial properties. The present study aims to evaluate the antibacterial and antibiofilm potential of Halilectin (H-2), present in the sponge Haliclona caerulea. H-2 is a homodimeric protein with 15 kDa monomers interconnected by weakly interacting bonds that oligomerize to form a 29 kDa dimer. The lectin showed affinity for the glycoproteins asialofetuin, fetuin, and porcine stomach mucin type II and type III (PSM). Circular dichroism analysis demonstrated the predominant presence of β-sheet structures with spectra of β1 proteins. H-2 was able to agglutinate Staphylococcus aureus ATCC 25923, Staphylococcus aureus ATCC 700698, and Escherichia coli ATCC 11303 cells. The lectin showed antibacterial potential, since when associated with tetracycline, the protein potentiated the effect of the antibiotic, in addition to inhibiting biofilm formation. Thus, H-2 was shown to be a lectin with high biotechnological potential with antibacterial action in association with the antibiotic tetracycline. |
| publishDate |
2024 |
| dc.date.issued.fl_str_mv |
2024 |
| dc.date.accessioned.fl_str_mv |
2025-05-29T16:22:58Z |
| dc.date.available.fl_str_mv |
2025-05-29T16:22:58Z |
| 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 |
CÂNDIDO, José Gabriel de Sousa. Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2). 2025. Dissertação (Mestrado em Biotecnologia de Recursos Naturais) – Centro de Ciências Agrárias, Universidade Federal do Ceará, Fortaleza, 2024. |
| dc.identifier.uri.fl_str_mv |
http://repositorio.ufc.br/handle/riufc/81122 |
| identifier_str_mv |
CÂNDIDO, José Gabriel de Sousa. Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2). 2025. Dissertação (Mestrado em Biotecnologia de Recursos Naturais) – Centro de Ciências Agrárias, Universidade Federal do Ceará, Fortaleza, 2024. |
| url |
http://repositorio.ufc.br/handle/riufc/81122 |
| 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.source.none.fl_str_mv |
reponame:Repositório Institucional da Universidade Federal do Ceará (UFC) instname:Universidade Federal do Ceará (UFC) instacron:UFC |
| instname_str |
Universidade Federal do Ceará (UFC) |
| instacron_str |
UFC |
| institution |
UFC |
| reponame_str |
Repositório Institucional da Universidade Federal do Ceará (UFC) |
| collection |
Repositório Institucional da Universidade Federal do Ceará (UFC) |
| bitstream.url.fl_str_mv |
http://repositorio.ufc.br/bitstream/riufc/81122/4/license.txt http://repositorio.ufc.br/bitstream/riufc/81122/3/2024_dis_jgscandido.pdf |
| bitstream.checksum.fl_str_mv |
8a4605be74aa9ea9d79846c1fba20a33 0e2298813243bca882b647a578e7feff |
| bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 |
| repository.name.fl_str_mv |
Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC) |
| repository.mail.fl_str_mv |
bu@ufc.br || repositorio@ufc.br |
| _version_ |
1847793070133739520 |