Please use this identifier to cite or link to this item: http://hdl.handle.net/2067/43603
DC FieldValueLanguage
dc.contributor.authorBorocci, Stefanoit
dc.contributor.authorCerchia, Carmenit
dc.contributor.authorGrottesi, Alessandroit
dc.contributor.authorSanna, Nicoit
dc.contributor.authorPrandi, Ingrid Guarnettiit
dc.contributor.authorAbid, Nabilit
dc.contributor.authorBeccari, Andrea Rit
dc.contributor.authorChillemi, Giovanniit
dc.contributor.authorTalarico, Carmineit
dc.date.accessioned2021-08-16T17:14:17Z-
dc.date.available2021-08-16T17:14:17Z-
dc.date.issued2021it
dc.identifier.issn1661-6596it
dc.identifier.urihttp://hdl.handle.net/2067/43603-
dc.description.abstractThe COVID-19 pandemic is caused by SARS-CoV-2. Currently, most of the research efforts towards the development of vaccines and antibodies against SARS-CoV-2 were mainly focused on the spike (S) protein, which mediates virus entry into the host cell by binding to ACE2. As the virus SARS-CoV-2 continues to spread globally, variants have emerged, characterized by multiple mutations of the S glycoprotein. Herein, we employed microsecond-long molecular dynamics simulations to study the impact of the mutations of the S glycoprotein in SARS-CoV-2 Variant of Concern 202012/01 (B.1.1.7), termed the "UK variant", in comparison with the wild type, with the aim to decipher the structural basis of the reported increased infectivity and virulence. The simulations provided insights on the different dynamics of UK and wild-type S glycoprotein, regarding in particular the Receptor Binding Domain (RBD). In addition, we investigated the role of glycans in modulating the conformational transitions of the RBD. The overall results showed that the UK mutant experiences higher flexibility in the RBD with respect to wild type; this behavior might be correlated with the increased transmission reported for this variant. Our work also adds useful structural information on antigenic "hotspots" and epitopes targeted by neutralizing antibodies.it
dc.format.mediumELETTRONICOit
dc.language.isoengit
dc.titleAltered Local Interactions and Long-Range Communications in UK Variant (B.1.1.7) Spike Glycoproteinit
dc.typearticle*
dc.identifier.doi10.3390/ijms22115464it
dc.identifier.pmid34067272it
dc.identifier.scopus2-s2.0-85106016149it
dc.identifier.urlhttps://api.elsevier.com/content/abstract/scopus_id/85106016149it
dc.relation.journalINTERNATIONAL JOURNAL OF MOLECULAR SCIENCESit
dc.relation.firstpage5464it
dc.relation.volume22it
dc.relation.issue11it
dc.subject.scientificsectorAGR/17it
dc.subject.ercsectorLS2_12 Bioinformaticsit
dc.description.internationalit
dc.contributor.countryITAit
dc.type.refereeREF_1it
dc.type.miur262*
item.fulltextWith Fulltext-
item.openairetypearticle-
item.cerifentitytypePublications-
item.grantfulltextrestricted-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.journal.journalissn1661-6596-
crisitem.journal.anceE217024-
Appears in Collections:A1. Articolo in rivista
Files in This Item:
File Description SizeFormat Existing users please
ijms-22-05464.pdf8.23 MBAdobe PDF    Request a copy
Show simple item record

SCOPUSTM   
Citations 20

7
Last Week
0
Last month
0
checked on Apr 9, 2024

Page view(s)

101
Last Week
0
Last month
0
checked on Apr 13, 2024

Download(s)

5
checked on Apr 13, 2024

Google ScholarTM

Check

Altmetric


All documents in the "Unitus Open Access" community are published as open access.
All documents in the community "Prodotti della Ricerca" are restricted access unless otherwise indicated for specific documents