A simplified curcumin targets the membrane of Bacillus subtilis
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1002/mbo3.683 http://hdl.handle.net/11449/185680 |
Resumo: | Curcumin is the main constituent of turmeric, a seasoning popularized around the world with Indian cuisine. Among the benefits attributed to curcumin are anti-inflammatory, antimicrobial, antitumoral, and chemopreventive effects. Besides, curcumin inhibits the growth of the gram-positive bacterium Bacillus subtilis. The anti-B. subtilis action happens by interference with the division protein FtsZ, an ancestral tubulin widespread in Bacteria. FtsZ forms protofilaments in a GTP-dependent manner, with the concomitant recruitment of essential factors to operate cell division. By stimulating the GTPase activity of FtsZ, curcumin destabilizes its function. Recently, curcumin was shown to promote membrane permeabilization in B. subtilis. Here, we used molecular simplification to dissect the functionalities of curcumin. A simplified form, in which a monocarbonyl group substituted the beta-diketone moiety, showed antibacterial action against gram-positive and gram-negative bacteria of clinical interest. The simplified curcumin also disrupted the divisional septum of B. subtilis; however, subsequent biochemical analysis did not support a direct action on FtsZ. Our results suggest that the simplified curcumin exerted its function mainly through membrane permeabilization, with disruption of the membrane potential necessary for FtsZ intra-cellular localization. Finally, we show here experimental evidence for the requirement of the beta-diketone group of curcumin for its interaction with FtsZ. |
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A simplified curcumin targets the membrane of Bacillus subtilisantibacterial compoundcell divisionmembrane permeabilizationturmericCurcumin is the main constituent of turmeric, a seasoning popularized around the world with Indian cuisine. Among the benefits attributed to curcumin are anti-inflammatory, antimicrobial, antitumoral, and chemopreventive effects. Besides, curcumin inhibits the growth of the gram-positive bacterium Bacillus subtilis. The anti-B. subtilis action happens by interference with the division protein FtsZ, an ancestral tubulin widespread in Bacteria. FtsZ forms protofilaments in a GTP-dependent manner, with the concomitant recruitment of essential factors to operate cell division. By stimulating the GTPase activity of FtsZ, curcumin destabilizes its function. Recently, curcumin was shown to promote membrane permeabilization in B. subtilis. Here, we used molecular simplification to dissect the functionalities of curcumin. A simplified form, in which a monocarbonyl group substituted the beta-diketone moiety, showed antibacterial action against gram-positive and gram-negative bacteria of clinical interest. The simplified curcumin also disrupted the divisional septum of B. subtilis; however, subsequent biochemical analysis did not support a direct action on FtsZ. Our results suggest that the simplified curcumin exerted its function mainly through membrane permeabilization, with disruption of the membrane potential necessary for FtsZ intra-cellular localization. Finally, we show here experimental evidence for the requirement of the beta-diketone group of curcumin for its interaction with FtsZ.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Netherlands Organization for Scientific researchINCT CitrosUniv Estadual Paulista, Inst Biociencias, Dept Bioquim & Microbiol, BR-13506900 Rio Claro, SP, BrazilUniv Estadual Paulista, Inst Biociencias Letras & Ciencias Exatas, Dept Quim & Ciencias Ambientais, BR-15054000 Sao Jose Do Rio Preto, SP, BrazilUniv Groningen, Groningen Biomol Sci & Biotechnol Inst, Dept Mol Microbiol, Groningen, NetherlandsUniv Estadual Paulista, Inst Biociencias, Dept Bioquim & Microbiol, BR-13506900 Rio Claro, SP, BrazilUniv Estadual Paulista, Inst Biociencias Letras & Ciencias Exatas, Dept Quim & Ciencias Ambientais, BR-15054000 Sao Jose Do Rio Preto, SP, BrazilFAPESP: 2013/50367-8FAPESP: FAPESP 2014/18330-0Netherlands Organization for Scientific research: 729.004.005INCT Citros: 2014/50880-0INCT Citros: 465440/2014-2Wiley-BlackwellUniversidade Estadual Paulista (Unesp)Univ GroningenMorao, Luana G. [UNESP]Polaquini, Carlos R. [UNESP]Kopacz, MalgorzataTorrezan, Guilherme S. [UNESP]Ayusso, Gabriela M. [UNESP]Dilarri, Guilherme [UNESP]Cavalca, Lucia B. [UNESP]Zielinska, AleksandraScheffers, Dirk-JanRegasini, Luis O. [UNESP]Ferreira, Henrique [UNESP]2019-10-04T12:37:39Z2019-10-04T12:37:39Z2019-04-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article12http://dx.doi.org/10.1002/mbo3.683Microbiologyopen. Hoboken: Wiley, v. 8, n. 4, 12 p., 2019.2045-8827http://hdl.handle.net/11449/18568010.1002/mbo3.683WOS:000466794200030Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengMicrobiologyopeninfo:eu-repo/semantics/openAccess2021-10-23T01:35:49Zoai:repositorio.unesp.br:11449/185680Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:55:06.275017Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
A simplified curcumin targets the membrane of Bacillus subtilis |
title |
A simplified curcumin targets the membrane of Bacillus subtilis |
spellingShingle |
A simplified curcumin targets the membrane of Bacillus subtilis Morao, Luana G. [UNESP] antibacterial compound cell division membrane permeabilization turmeric |
title_short |
A simplified curcumin targets the membrane of Bacillus subtilis |
title_full |
A simplified curcumin targets the membrane of Bacillus subtilis |
title_fullStr |
A simplified curcumin targets the membrane of Bacillus subtilis |
title_full_unstemmed |
A simplified curcumin targets the membrane of Bacillus subtilis |
title_sort |
A simplified curcumin targets the membrane of Bacillus subtilis |
author |
Morao, Luana G. [UNESP] |
author_facet |
Morao, Luana G. [UNESP] Polaquini, Carlos R. [UNESP] Kopacz, Malgorzata Torrezan, Guilherme S. [UNESP] Ayusso, Gabriela M. [UNESP] Dilarri, Guilherme [UNESP] Cavalca, Lucia B. [UNESP] Zielinska, Aleksandra Scheffers, Dirk-Jan Regasini, Luis O. [UNESP] Ferreira, Henrique [UNESP] |
author_role |
author |
author2 |
Polaquini, Carlos R. [UNESP] Kopacz, Malgorzata Torrezan, Guilherme S. [UNESP] Ayusso, Gabriela M. [UNESP] Dilarri, Guilherme [UNESP] Cavalca, Lucia B. [UNESP] Zielinska, Aleksandra Scheffers, Dirk-Jan Regasini, Luis O. [UNESP] Ferreira, Henrique [UNESP] |
author2_role |
author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Univ Groningen |
dc.contributor.author.fl_str_mv |
Morao, Luana G. [UNESP] Polaquini, Carlos R. [UNESP] Kopacz, Malgorzata Torrezan, Guilherme S. [UNESP] Ayusso, Gabriela M. [UNESP] Dilarri, Guilherme [UNESP] Cavalca, Lucia B. [UNESP] Zielinska, Aleksandra Scheffers, Dirk-Jan Regasini, Luis O. [UNESP] Ferreira, Henrique [UNESP] |
dc.subject.por.fl_str_mv |
antibacterial compound cell division membrane permeabilization turmeric |
topic |
antibacterial compound cell division membrane permeabilization turmeric |
description |
Curcumin is the main constituent of turmeric, a seasoning popularized around the world with Indian cuisine. Among the benefits attributed to curcumin are anti-inflammatory, antimicrobial, antitumoral, and chemopreventive effects. Besides, curcumin inhibits the growth of the gram-positive bacterium Bacillus subtilis. The anti-B. subtilis action happens by interference with the division protein FtsZ, an ancestral tubulin widespread in Bacteria. FtsZ forms protofilaments in a GTP-dependent manner, with the concomitant recruitment of essential factors to operate cell division. By stimulating the GTPase activity of FtsZ, curcumin destabilizes its function. Recently, curcumin was shown to promote membrane permeabilization in B. subtilis. Here, we used molecular simplification to dissect the functionalities of curcumin. A simplified form, in which a monocarbonyl group substituted the beta-diketone moiety, showed antibacterial action against gram-positive and gram-negative bacteria of clinical interest. The simplified curcumin also disrupted the divisional septum of B. subtilis; however, subsequent biochemical analysis did not support a direct action on FtsZ. Our results suggest that the simplified curcumin exerted its function mainly through membrane permeabilization, with disruption of the membrane potential necessary for FtsZ intra-cellular localization. Finally, we show here experimental evidence for the requirement of the beta-diketone group of curcumin for its interaction with FtsZ. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-10-04T12:37:39Z 2019-10-04T12:37:39Z 2019-04-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1002/mbo3.683 Microbiologyopen. Hoboken: Wiley, v. 8, n. 4, 12 p., 2019. 2045-8827 http://hdl.handle.net/11449/185680 10.1002/mbo3.683 WOS:000466794200030 |
url |
http://dx.doi.org/10.1002/mbo3.683 http://hdl.handle.net/11449/185680 |
identifier_str_mv |
Microbiologyopen. Hoboken: Wiley, v. 8, n. 4, 12 p., 2019. 2045-8827 10.1002/mbo3.683 WOS:000466794200030 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Microbiologyopen |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
12 |
dc.publisher.none.fl_str_mv |
Wiley-Blackwell |
publisher.none.fl_str_mv |
Wiley-Blackwell |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128721302847488 |