Publicação
Dengue virus capsid protein interacts specifically with very low-density lipoproteins
| dc.contributor.author | Faustino, André F. | |
| dc.contributor.author | Carvalho, Filomena A. | |
| dc.contributor.author | Martins, Ivo C. | |
| dc.contributor.author | Castanho, Miguel A. R. B. | |
| dc.contributor.author | Mohana-Borges, Ronaldo | |
| dc.contributor.author | Almeida, Fábio C. L. | |
| dc.contributor.author | Da Poian, Andrea T. | |
| dc.contributor.author | Santos, Nuno C. | |
| dc.date.accessioned | 2014-03-10T12:41:01Z | |
| dc.date.available | 2014-03-10T12:41:01Z | |
| dc.date.issued | 2014 | |
| dc.description | © 2014 Elsevier Inc. All rights reserved. | eng |
| dc.description.abstract | Dengue affects millions of people worldwide. No specific treatment is currently available, in part due to an incomplete understanding of the viral components' interactions with host cellular structures. We tested dengue virus (DENV) capsid protein (C) interaction with low- and very low-density lipoproteins (LDL and VLDL, respectively) using atomic force microscopy-based force spectroscopy, dynamic light scattering, NMR and computational analysis. Data reveal a specific DENV C interaction with VLDL, but not LDL. This binding is potassium-dependent and involves the DENV C N-terminal region, as previously observed for the DENV C-lipid droplets (LDs) interaction. A successful inhibition of DENV C-VLDL binding was achieved with a peptide drug lead. The similarities between LDs and VLDL, and between perilipin 3 (DENV C target on LDs) and ApoE, indicate ApoE as the molecular target on VLDL. We hypothesize that DENV may form lipoviroparticles, which would constitute a novel step on DENV life cycle. | eng |
| dc.description.sponsorship | This work was supported by Fundação para a Ciência e Tecnologia – Ministério da Educação e Ciência (FCT-MEC, Portugal, projects PTDC/QUI-BIQ/112929/2009 and PTDC/SAU-ENB/117013/2010), Calouste Gulenkian Foundation (Portugal), European Union FP7-IRSES project MEMPEPACROSS, FCT-CAPES Portugal-Brazil joint cooperation projects, and by the Brazilian Funding Agencies CNPq, FAPERJ, FINEP, CAPES (PVE171/2012) and INCT-Dengue. AFF and ICM acknowledge FCT-MEC for fellowships SFRH/BD/77609/2011 and SFRH/BPD/74287/2010, respectively. | eng |
| dc.identifier.citation | Nanomedicine: Nanotechnology, Biology, and Medicine 10 (2014) 247–255 | eng |
| dc.identifier.issn | 1549-9634 | |
| dc.identifier.uri | http://dx.doi.org/10.1016/j.nano.2013.06.004 | |
| dc.identifier.uri | http://hdl.handle.net/10451/10709 | |
| dc.language.iso | eng | por |
| dc.peerreviewed | yes | por |
| dc.publisher | Elsevier | por |
| dc.relation.publisherversion | The definitive version is available at http://www.elsevier.com | eng |
| dc.subject | Dengue virus capsid protein | eng |
| dc.subject | Lipoproteins | eng |
| dc.subject | Single-molecule studies | eng |
| dc.subject | AFM-based force spectroscopy | eng |
| dc.subject | Dynamic light scattering | eng |
| dc.title | Dengue virus capsid protein interacts specifically with very low-density lipoproteins | eng |
| dc.type | journal article | |
| dspace.entity.type | Publication | |
| oaire.awardURI | info:eu-repo/grantAgreement/EC/FP7/247513 | |
| oaire.citation.endPage | 255 | por |
| oaire.citation.startPage | 247 | por |
| oaire.citation.title | Nanomedicine: Nanotechnology, Biology, and Medicine | eng |
| oaire.citation.volume | 10 | por |
| oaire.fundingStream | FP7 | |
| project.funder.identifier | http://doi.org/10.13039/501100008530 | |
| project.funder.name | European Commission | |
| rcaap.rights | closedAccess | por |
| rcaap.type | article | por |
| relation.isProjectOfPublication | 9a14f3fc-9671-4460-8a00-79594f5854e0 | |
| relation.isProjectOfPublication.latestForDiscovery | 9a14f3fc-9671-4460-8a00-79594f5854e0 |
