Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | , , , , |
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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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 |
_version_ |
1818602406961741824 |