Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole

Detalhes bibliográficos
Autor(a) principal: Barbosa, Fabiane M.
Data de Publicação: 2007
Outros Autores: Daffre, Sirlei, Maldonado, Rosa A., Miranda, Antonio [UNIFESP], Nimrichter, Leonardo, Rodrigues, Marcio L.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
dARK ID: ark:/48912/0013000005cv5
Texto Completo: http://dx.doi.org/10.1111/j.1574-6968.2007.00850.x
http://repositorio.unifesp.br/handle/11600/29982
Resumo: Gomesin is an 18-residue cysteine-rich antimicrobial peptide produced by hemocytes of the spider Acanthoscurria gomesiana. in the present study, the antifungal properties of gomesin against Cryptococcus neoformans, the etiologic agent of cryptococcosis, were evaluated. Gomesin bound to the cell surface of cryptococci, which resulted in cell death associated with membrane permeabilization. Antifungal concentrations of gomesin were not toxic for human brain cells. Supplementation of cryptococcal cultures with the peptide (1 mu M) caused a decrease in capsule expression and rendered fungal cells more susceptible to killing by human brain phagocytes. the possible use of gomesin in combination with fluconazole, a standard antifungal drug, was also evaluated. in association with fluconazole, gomesin concentrations with low antimicrobial activity (0.1-1 mu M) inhibited fungal growth and enhanced the antimicrobial activity of brain phagocytes. These results reveal the potential of gomesin to promote inhibition of cryptococcal growth directly or by enhancing the effectiveness of host defenses.
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spelling Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazolegomesinCryptococcus neoformansantimicrobial peptideGomesin is an 18-residue cysteine-rich antimicrobial peptide produced by hemocytes of the spider Acanthoscurria gomesiana. in the present study, the antifungal properties of gomesin against Cryptococcus neoformans, the etiologic agent of cryptococcosis, were evaluated. Gomesin bound to the cell surface of cryptococci, which resulted in cell death associated with membrane permeabilization. Antifungal concentrations of gomesin were not toxic for human brain cells. Supplementation of cryptococcal cultures with the peptide (1 mu M) caused a decrease in capsule expression and rendered fungal cells more susceptible to killing by human brain phagocytes. the possible use of gomesin in combination with fluconazole, a standard antifungal drug, was also evaluated. in association with fluconazole, gomesin concentrations with low antimicrobial activity (0.1-1 mu M) inhibited fungal growth and enhanced the antimicrobial activity of brain phagocytes. These results reveal the potential of gomesin to promote inhibition of cryptococcal growth directly or by enhancing the effectiveness of host defenses.Univ Fed Rio de Janeiro, Inst Microbiol Prof Paulo Goes, Dept Microbiol Geral, Lab Estudos Integrados Bioquim Microbiana, BR-21941590 Rio de Janeiro, BrazilUniv São Paulo, Inst Ciencias Biomed, Dept Parasitol, BR-05508 São Paulo, BrazilUniv Texas, Dept Biol Sci, El Paso, TX 79968 USAUniversidade Federal de São Paulo, Dept Biofis, São Paulo, BrazilUniversidade Federal de São Paulo, Dept Biofis, São Paulo, BrazilWeb of ScienceBlackwell PublishingUniversidade Federal do Rio de Janeiro (UFRJ)Universidade de São Paulo (USP)Univ TexasUniversidade Federal de São Paulo (UNIFESP)Barbosa, Fabiane M.Daffre, SirleiMaldonado, Rosa A.Miranda, Antonio [UNIFESP]Nimrichter, LeonardoRodrigues, Marcio L.2016-01-24T13:49:01Z2016-01-24T13:49:01Z2007-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion279-286http://dx.doi.org/10.1111/j.1574-6968.2007.00850.xFems Microbiology Letters. Oxford: Blackwell Publishing, v. 274, n. 2, p. 279-286, 2007.10.1111/j.1574-6968.2007.00850.x0378-1097http://repositorio.unifesp.br/handle/11600/29982WOS:000248960500017ark:/48912/0013000005cv5engFems Microbiology Lettersinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2022-07-08T10:33:28Zoai:repositorio.unifesp.br/:11600/29982Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-12-11T19:58:50.223162Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole
title Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole
spellingShingle Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole
Barbosa, Fabiane M.
gomesin
Cryptococcus neoformans
antimicrobial peptide
title_short Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole
title_full Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole
title_fullStr Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole
title_full_unstemmed Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole
title_sort Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole
author Barbosa, Fabiane M.
author_facet Barbosa, Fabiane M.
Daffre, Sirlei
Maldonado, Rosa A.
Miranda, Antonio [UNIFESP]
Nimrichter, Leonardo
Rodrigues, Marcio L.
author_role author
author2 Daffre, Sirlei
Maldonado, Rosa A.
Miranda, Antonio [UNIFESP]
Nimrichter, Leonardo
Rodrigues, Marcio L.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal do Rio de Janeiro (UFRJ)
Universidade de São Paulo (USP)
Univ Texas
Universidade Federal de São Paulo (UNIFESP)
dc.contributor.author.fl_str_mv Barbosa, Fabiane M.
Daffre, Sirlei
Maldonado, Rosa A.
Miranda, Antonio [UNIFESP]
Nimrichter, Leonardo
Rodrigues, Marcio L.
dc.subject.por.fl_str_mv gomesin
Cryptococcus neoformans
antimicrobial peptide
topic gomesin
Cryptococcus neoformans
antimicrobial peptide
description Gomesin is an 18-residue cysteine-rich antimicrobial peptide produced by hemocytes of the spider Acanthoscurria gomesiana. in the present study, the antifungal properties of gomesin against Cryptococcus neoformans, the etiologic agent of cryptococcosis, were evaluated. Gomesin bound to the cell surface of cryptococci, which resulted in cell death associated with membrane permeabilization. Antifungal concentrations of gomesin were not toxic for human brain cells. Supplementation of cryptococcal cultures with the peptide (1 mu M) caused a decrease in capsule expression and rendered fungal cells more susceptible to killing by human brain phagocytes. the possible use of gomesin in combination with fluconazole, a standard antifungal drug, was also evaluated. in association with fluconazole, gomesin concentrations with low antimicrobial activity (0.1-1 mu M) inhibited fungal growth and enhanced the antimicrobial activity of brain phagocytes. These results reveal the potential of gomesin to promote inhibition of cryptococcal growth directly or by enhancing the effectiveness of host defenses.
publishDate 2007
dc.date.none.fl_str_mv 2007-09-01
2016-01-24T13:49:01Z
2016-01-24T13:49:01Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1111/j.1574-6968.2007.00850.x
Fems Microbiology Letters. Oxford: Blackwell Publishing, v. 274, n. 2, p. 279-286, 2007.
10.1111/j.1574-6968.2007.00850.x
0378-1097
http://repositorio.unifesp.br/handle/11600/29982
WOS:000248960500017
dc.identifier.dark.fl_str_mv ark:/48912/0013000005cv5
url http://dx.doi.org/10.1111/j.1574-6968.2007.00850.x
http://repositorio.unifesp.br/handle/11600/29982
identifier_str_mv Fems Microbiology Letters. Oxford: Blackwell Publishing, v. 274, n. 2, p. 279-286, 2007.
10.1111/j.1574-6968.2007.00850.x
0378-1097
WOS:000248960500017
ark:/48912/0013000005cv5
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Fems Microbiology Letters
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 279-286
dc.publisher.none.fl_str_mv Blackwell Publishing
publisher.none.fl_str_mv Blackwell Publishing
dc.source.none.fl_str_mv reponame:Repositório Institucional da UNIFESP
instname:Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
instname_str Universidade Federal de São Paulo (UNIFESP)
instacron_str UNIFESP
institution UNIFESP
reponame_str Repositório Institucional da UNIFESP
collection Repositório Institucional da UNIFESP
repository.name.fl_str_mv Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)
repository.mail.fl_str_mv biblioteca.csp@unifesp.br
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