Avaliação do potencial antibacteriano da lectina da esponja marinha Haliclona caerulea (Halilectina – 2)

Detalhes bibliográficos
Ano de defesa: 2024
Autor(a) principal: Cândido, José Gabriel de Sousa
Orientador(a): Sampaio, Alexandre Holanda
Banca de defesa: Não Informado pela instituição
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