{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Monti M"],"funding":["European Research Council","Innovationsfonden","Lundbeck Foundation","Novo Nordisk Fonden","EIT Health"],"pagination":["451-464"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10801686"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["128(2)"],"pubmed_abstract":["It is not well understood why severe acute respiratory syndrome (SARS)-CoV-2 spreads much faster than other β-coronaviruses such as SARS-CoV and Middle East respiratory syndrome (MERS)-CoV. In a previous publication, we predicted the binding of the N-terminal domain (NTD) of SARS-CoV-2 spike to sialic acids (SAs). Here, we experimentally validate this interaction and present simulations that reveal a second possible interaction between SAs and the spike protein via a binding site located in the receptor-binding domain (RBD). The predictions from molecular-dynamics simulations and the previously-published 2D-Zernike binding-site recognition approach were validated through flow-induced dispersion analysis (FIDA)─which reveals the capability of the SARS-CoV-2 spike to bind to SA-containing (g"],"journal":["The journal of physical chemistry. B"],"pubmed_title":["Two Receptor Binding Strategy of SARS-CoV-2 Is Mediated by Both the N-Terminal and Receptor-Binding Spike Domain."],"pmcid":["PMC10801686"],"funding_grant_id":["855923","0211-00066B","R287-2018-1836","825080","R303-2018-3495","NNF18OC0032628"],"pubmed_authors":["Monti M","Di Rienzo L","Miotto M","Otzen DE","Somavarapu AK","Baranov MV","Golbek TW","Gosti G","Frans MT","Tartaglia GG","Roeters SJ","Weidner T","Ruocco G","van den Bogaart G","Boltje TJ","Rossing E","Nagaraj M","Milanetti E","Moons SJ"],"additional_accession":[]},"is_claimable":false,"name":"Two Receptor Binding Strategy of SARS-CoV-2 Is Mediated by Both the N-Terminal and Receptor-Binding Spike Domain.","description":"It is not well understood why severe acute respiratory syndrome (SARS)-CoV-2 spreads much faster than other β-coronaviruses such as SARS-CoV and Middle East respiratory syndrome (MERS)-CoV. In a previous publication, we predicted the binding of the N-terminal domain (NTD) of SARS-CoV-2 spike to sialic acids (SAs). Here, we experimentally validate this interaction and present simulations that reveal a second possible interaction between SAs and the spike protein via a binding site located in the receptor-binding domain (RBD). The predictions from molecular-dynamics simulations and the previously-published 2D-Zernike binding-site recognition approach were validated through flow-induced dispersion analysis (FIDA)─which reveals the capability of the SARS-CoV-2 spike to bind to SA-containing (g","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jan","modification":"2026-05-29T09:46:45.978Z","creation":"2025-04-04T21:16:34.537Z"},"accession":"S-EPMC10801686","cross_references":{"pubmed":["38190651"],"doi":["10.1021/acs.jpcb.3c06258"]}}