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Structural Characterization of N-Linked Glycans in the Receptor Binding Domain of the SARS-CoV-2 Spike Protein and their Interactions with Human Lectins

2020-12-21Artigo científico Acesso aberto
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dc.contributor.authorLenza, Maria Pia
dc.contributor.authorOyenarte, Iker
dc.contributor.authorDiercks, Tammo
dc.contributor.authorQuintana, Jon Imanol
dc.contributor.authorGimeno, Ana
dc.contributor.authorCoelho, Helena
dc.contributor.authorDiniz, Ana
dc.contributor.authorPeccati, Francesca
dc.contributor.authorDelgado, Sandra
dc.contributor.authorBosch, Alexandre
dc.contributor.authorValle, Mikel
dc.contributor.authorMillet, Oscar
dc.contributor.authorAbrescia, Nicola G. A.
dc.contributor.authorPalazón, Asís
dc.contributor.authorMarcelo, Filipa
dc.contributor.authorJiménez-Osés, Gonzalo
dc.contributor.authorJiménez-Barbero, Jesús
dc.contributor.authorArdá, Ana
dc.contributor.authorEreño-Orbea, June
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.pblJohn Wiley & Sons, Ltd.
dc.date.accessioned2021-05-05T23:25:28Z
dc.date.available2021-05-05T23:25:28Z
dc.date.issued2020-12-21
dc.descriptioninfo:eu-repo/grantAgreement/WT/Physiological Sciences/095700 ERC‐2017‐AdG, 788143‐RECGLYCANMR grant 200077 grant RTI2018‐094751‐B‐C21 GC2018‐098996‐B‐I00 RTI2018‐099592‐B‐C22 RTI2018‐101269‐B‐I00 SEV‐2016‐0644 IF/00780/2015 PTDC/BIA‐MIB/31028/2017 UCIBIO UIDB/04378/2020 Infrastructure project 22161 PD/BD/142847/2018
dc.description.abstractThe glycan structures of the receptor binding domain of the SARS-CoV2 spike glycoprotein expressed in human HEK293F cells have been studied by using NMR. The different possible interacting epitopes have been deeply analysed and characterized, providing evidence of the presence of glycan structures not found in previous MS-based analyses. The interaction of the RBD 13C-labelled glycans with different human lectins, which are expressed in different organs and tissues that may be affected during the infection process, has also been evaluated by NMR. In particular, 15N-labelled galectins (galectins-3, -7 and -8 N-terminal), Siglecs (Siglec-8, Siglec-10), and C-type lectins (DC-SIGN, MGL) have been employed. Complementary experiments from the glycoprotein perspective or from the lectin's point of view have permitted to disentangle the specific interacting epitopes in each case. Based on these findings, 3D models of the interacting complexes have been proposed.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent2450164
dc.identifier.doi10.1002/anie.202011015
dc.identifier.issn1433-7851
dc.identifier.otherPURE: 26745157
dc.identifier.otherPURE UUID: c487dda0-b449-4962-b2d3-05fb4ad99340
dc.identifier.otherScopus: 85092927434
dc.identifier.otherPubMed: 32915505
dc.identifier.otherPubMedCentral: PMC7894318
dc.identifier.otherWOS: 000580565200001
dc.identifier.otherORCID: /0000-0001-5049-8511/work/93369358
dc.identifier.urihttp://hdl.handle.net/10362/117141
dc.identifier.urlhttps://www.scopus.com/pages/publications/85092927434
dc.language.isoeng
dc.peerreviewedyes
dc.subjectglycan
dc.subjectlectin
dc.subjectmolecular recognition
dc.subjectreceptor binding domain
dc.subjectSARS-CoV2
dc.subjectCatalysis
dc.subjectGeneral Chemistry
dc.titleStructural Characterization of N-Linked Glycans in the Receptor Binding Domain of the SARS-CoV-2 Spike Protein and their Interactions with Human Lectinsen
dc.typejournal article
degois.publication.titleAngewandte Chemie - International Edition
dspace.entity.typePublication
rcaap.rightsopenAccess

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