Publicação
Antimicrobial protein rBPI21-induced surface changes on Gram-negative and Gram-positive bacteria
| dc.contributor.author | Domingues, Marco M. | |
| dc.contributor.author | Silva, Patrícia M. | |
| dc.contributor.author | Franquelim, Henri G. | |
| dc.contributor.author | Carvalho, Filomena A. | |
| dc.contributor.author | Castanho, Miguel A. R. B. | |
| dc.contributor.author | Santos, Nuno C. | |
| dc.date.accessioned | 2016-04-21T13:04:12Z | |
| dc.date.available | 2016-04-21T13:04:12Z | |
| dc.date.issued | 2014 | |
| dc.description | © 2014 Elsevier Inc. All rights reserved. | pt_PT |
| dc.description.abstract | New classes of antibiotics, such as antimicrobial peptides or proteins (AMPs), are crucial to deal with threatening bacterial diseases. rBPI21 is an AMP based on the human neutrophil BPI protein, with potential clinical use against meningitis. We studied the membrane perturbations promoted by rBPI21 on Gram-negative Escherichia coli and Gram-positive Staphylococcus aureus. Its interaction with bacteria was also studied in the presence of lipopolysaccharide (LPS), rBPI21 major ligand. Flow cytometry analysis of both bacteria shows that rBPI21 induces membrane depolarization. rBPI21 increases the negative surface charge of both bacteria toward positive values, as shown by zeta-potential measurements. This is followed by surface perturbations, culminating in cell lysis, as visualized by atomic force microscopy (AFM). Force spectroscopy measurements show that soluble LPS decreases the interaction of rBPI21 with bacteria, especially with S. aureus. This suggests that the rBPI21 LPS-binding pocket may also participate on the binding to Gram-positive bacteria. | pt_PT |
| dc.description.sponsorship | This work was supported by Fundação para a Ciência e a Tecnologia – Ministério do Ensino e Ciência (FCT-MEC, Portugal). M.M.D. and H.G.F. acknowledge FCT-MEC PhD fellowships SFRH/BD/41750/2007 and SFRH/BD/39039/2007, respectively. | pt_PT |
| dc.identifier.doi | 10.1016/j.nano.2013.11.002 | pt_PT |
| dc.identifier.issn | 1549-9634 | |
| dc.identifier.uri | http://hdl.handle.net/10451/23503 | |
| dc.language.iso | eng | pt_PT |
| dc.peerreviewed | yes | pt_PT |
| dc.publisher | Elsevier | pt_PT |
| dc.relation | ESTUDO DO MECANISMO DE ACÇÃO DE PÉPTIDOS INIBIDORES DE FUSÃO DO HIV DE INTERESSE CLÍNICO COMPROVADO | |
| dc.relation.publisherversion | http://www.journals.elsevier.com/nanomedicine-nanotechnology-biology-and-medicine/ | pt_PT |
| dc.subject | Lipopolysaccharide | pt_PT |
| dc.subject | rBPI21 | pt_PT |
| dc.subject | Atomic force microscopy | pt_PT |
| dc.title | Antimicrobial protein rBPI21-induced surface changes on Gram-negative and Gram-positive bacteria | pt_PT |
| dc.type | journal article | |
| dspace.entity.type | Publication | |
| oaire.awardNumber | SFRH/BD/41750/2007 | |
| oaire.awardNumber | SFRH/BD/39039/2007 | |
| oaire.awardTitle | ESTUDO DO MECANISMO DE ACÇÃO DE PÉPTIDOS INIBIDORES DE FUSÃO DO HIV DE INTERESSE CLÍNICO COMPROVADO | |
| oaire.awardURI | info:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F41750%2F2007/PT | |
| oaire.awardURI | info:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F39039%2F2007/PT | |
| oaire.citation.title | Nanomedicine: Nanotechnology, Biology, and Medicine | pt_PT |
| oaire.fundingStream | SFRH | |
| project.funder.identifier | http://doi.org/10.13039/501100001871 | |
| project.funder.identifier | http://doi.org/10.13039/501100001871 | |
| project.funder.name | Fundação para a Ciência e a Tecnologia | |
| project.funder.name | Fundação para a Ciência e a Tecnologia | |
| rcaap.rights | closedAccess | pt_PT |
| rcaap.type | article | pt_PT |
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| relation.isProjectOfPublication | e26f9a39-b506-4d64-aa57-2aecd2432f59 | |
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