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The importance of lipid conjugation on anti-fusion peptides against Nipah virus

2022Journal article Open access
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dc.contributor.authorMarques, Marta C.
dc.contributor.authorLousa, Diana
dc.contributor.authorSilva, Patrícia M.
dc.contributor.authorFaustino, André F.
dc.contributor.authorSoares, Cláudio M.
dc.contributor.authorSantos, Nuno C.
dc.date.accessioned2022-03-29T16:01:14Z
dc.date.available2022-03-29T16:01:14Z
dc.date.issued2022
dc.description© 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).pt_PT
dc.description.abstractNipah virus (NiV) is a recently emerging zoonotic virus that belongs to the Paramyxoviridae family and the Henipavirus genus. It causes a range of conditions, from asymptomatic infection to acute respiratory illness and fatal encephalitis. The high mortality rate of 40 to 90% ranks these viruses among the deadliest viruses known to infect humans. Currently, there is no antiviral drug available for Nipah virus disease and treatment is only supportive. Thus, there is an urgent demand for efficient antiviral therapies. NiV F protein, which catalyzes fusion between the viral and host membranes, is a potential target for antiviral drugs, as it is a key protein in the initial stages of infection. Fusion inhibitor peptides derived from the HRC-domain of the F protein are known to bind to their complementary domain in the protein's transient intermediate state, preventing the formation of a six-helix bundle (6HB) thought to be responsible for driving the fusion of the viral and cell membranes. Here, we evaluated the biophysical and structural properties of four different C-terminal lipid-tagged peptides. Different compositions of the lipid tags were tested to search for properties that might promote efficacy and broad-spectrum activity. Fluorescence spectroscopy was used to study the interaction of the peptides with biomembrane model systems and human blood cells. In order to understand the structural properties of the peptides, circular dichroism measurements and molecular dynamics simulations were performed. Our results indicate a peptide preference for cholesterol-enriched membranes and a lipid conjugation-driven stabilization of the peptide α-helical secondary structure. This work may contribute for the development of highly effective viral fusion against NiV inhibitors.pt_PT
dc.description.sponsorshipThis work was financially supported by Fundação para a Ciência e a Tecnologia—Ministério da Ciência, Tecnologia e Ensino Superior (FCT-MCTES, Portugal), through projects PTDC/BBB-BQB/3494/2014, PTDC/QUI-BIQ/114774/2009, PTDC/CCI-BIO/28200/2017 and Pest-OE/EQB/LA0004/2011, and by National Institute of Allergy and Infectious Diseases, National Institutes of Health (NIH), project R01AI114736, lead by Anne Moscona (Columbia University Medical Center, NY, USA). This work was also financially supported by Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular) funded by FEDER funds through COMPETE2020-Programa Operacional Competitividade e Internacionalização (POCI) and by national funds through FCT-MCTES. MCM, PMS and DL were supported by FCT-MCTES fellowships SFRH/BPD/118731/2016, SFRH/BD/118413/2016 and SFRH/BPD/92537/2013, respectively.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationBiomedicines. 2022 Mar 18;10(3):703pt_PT
dc.identifier.doi10.3390/biomedicines10030703pt_PT
dc.identifier.eissn2227-9059
dc.identifier.urihttp://hdl.handle.net/10451/52076
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relationLISBOA-01-0145-FEDER-007660pt_PT
dc.relationBroad-spectrum antiviral peptides against respiratory viruses
dc.relationMembrane fusion mechanism of Influenza Hemagglutinin: a simulation and biophysical approach.
dc.relationUsing computational and experimental methods to provide a global characterization of viral fusion peptides
dc.relationStrategic Project - LA 4 - 2011-2012
dc.relationEngineering fusion inhibitor peptides against childhood respiratory viruses
dc.relationLipid-tagged peptides as entry inhibitors for respiratory viruses
dc.relationMOLECULAR MECHANISMS OF VIRAL MEMBRANE FUSION: A COMPUTATIONAL ANALYSIS
dc.relation.publisherversionhttps://www.mdpi.com/journal/biomedicinespt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectNipah viruspt_PT
dc.subjectAntiviralspt_PT
dc.subjectFusion inhibitorspt_PT
dc.subjectLipid conjugationpt_PT
dc.subjectPeptidespt_PT
dc.titleThe importance of lipid conjugation on anti-fusion peptides against Nipah viruspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleBroad-spectrum antiviral peptides against respiratory viruses
oaire.awardTitleMembrane fusion mechanism of Influenza Hemagglutinin: a simulation and biophysical approach.
oaire.awardTitleUsing computational and experimental methods to provide a global characterization of viral fusion peptides
oaire.awardTitleStrategic Project - LA 4 - 2011-2012
oaire.awardTitleEngineering fusion inhibitor peptides against childhood respiratory viruses
oaire.awardTitleLipid-tagged peptides as entry inhibitors for respiratory viruses
oaire.awardTitleMOLECULAR MECHANISMS OF VIRAL MEMBRANE FUSION: A COMPUTATIONAL ANALYSIS
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBBB-BQB%2F3494%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQUI-BIQ%2F114774%2F2009/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FCCI-BIO%2F28200%2F2017/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/PEst-OE%2FEQB%2FLA0004%2F2011/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBPD%2F118731%2F2016/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/OE/SFRH%2FBD%2F118413%2F2016/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/OE/SFRH%2FBPD%2F92537%2F2013/PT
oaire.citation.issue3pt_PT
oaire.citation.titleBiomedicinespt_PT
oaire.citation.volume10pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStreamOE
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person.familyNameC. Marques
person.familyNameM. Silva
person.familyNameda Costa Faustino
person.familyNameSantos
person.givenNameMarta
person.givenNamePatrícia
person.givenNameAndré Filipe
person.givenNameNuno
person.identifier.ciencia-id3A1D-10AB-43BC
person.identifier.ciencia-id1A18-2AAE-83A2
person.identifier.ciencia-id3D19-A07A-6E7C
person.identifier.ciencia-idCD13-5E3A-A3C5
person.identifier.orcid0000-0002-5093-5918
person.identifier.orcid0000-0001-5055-785X
person.identifier.orcid0000-0002-7364-8524
person.identifier.orcid0000-0002-0580-0475
person.identifier.ridA-5725-2019
person.identifier.ridN-7248-2013
person.identifier.scopus-author-id35085375600
person.identifier.scopus-author-id55940818300
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
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project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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