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dc.contributor.authorYang, Jinsung
dc.contributor.authorPark, Jeongsoo
dc.contributor.authorKoehler, Melanie
dc.contributor.authorSimpson, Joshua
dc.contributor.authorLuque, Daniel 
dc.contributor.authorRodríguez, Javier M.
dc.contributor.authorAlsteens, David
dc.date.accessioned2022-07-21T08:56:53Z
dc.date.available2022-07-21T08:56:53Z
dc.date.issued2021
dc.identifier.citationAdv. NanoBiomed Res. 2021;1(12):2100077.es_ES
dc.identifier.issn2699-9307es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/14769
dc.description.abstractRotavirus interactions with endogenous cell surface receptors are of fundamental interest in virology and medicine; however, the evidence of rotavirus directly binding to the receptors and the consequent dynamic behaviors are still elusive. Force–distance curve-based atomic force microscopy allows for the extraction of biophysical properties underlying binding of single virions to receptors and clarification of the dynamics of rotavirus–receptor interactions. Unfortunately, this method is time-consuming due to the lack of automation when analyzing large data sets. Herein, rotavirus–receptor interactions and early endocytosis behaviors using automated high-throughput analysis are examined. It is demonstrated that rotavirus binds to α-linked sialic acid and α2β1 integrin. The effect of trypsinization is investigated on the capsid protein VP4 binding to the receptors. Using fluidic force microscopy, it is demonstrated that the interaction leads to α2 integrin recruitment to the cell-bound rotavirus on the plasma membrane. Further, it is illustrated that an integrin-derived peptide can impede binding and alter downstream dynamics. Taken together, these results open a new understanding of the infection mechanism of rotavirus and suggest a novel inhibitory peptide against rotavirus binding.es_ES
dc.description.sponsorshipThis project received funding from the European Research Council under the European Union's Horizon 2020 research and innovation program (grant agreement no. 758224), from the FNRS-Welbio (grant no. CR-2019S-01), from the Spanish Ministry of Economy and Competitivity BFU2013-43149-R, and from the ISCIII AESI PI20CIII/00014.es_ES
dc.language.isoenges_ES
dc.publisherWiley es_ES
dc.type.hasVersionVoRes_ES
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.titleRotavirus Binding to Cell Surface Receptors Directly Recruiting α2 Integrines_ES
dc.typejournal articlees_ES
dc.rights.licenseAtribución 4.0 Internacional*
dc.format.volume1es_ES
dc.format.number12es_ES
dc.format.page2100077es_ES
dc.identifier.doi10.1002/anbr.202100077es_ES
dc.contributor.funderKatholieke Universiteit Leuven (Bélgica) es_ES
dc.contributor.funderNational Fund for Research (Francia) es_ES
dc.contributor.funderUnión Europea. Comisión Europea. European Research Council (ERC) es_ES
dc.contributor.funderMinisterio de Economía y Competitividad (España) es_ES
dc.contributor.funderInstituto de Salud Carlos III es_ES
dc.contributor.funderUnión Europea. Comisión Europea. H2020 es_ES
dc.description.peerreviewedes_ES
dc.identifier.e-issn2699-9307es_ES
dc.relation.publisherversionhttps://doi.org/10.1002/anbr.202100077es_ES
dc.identifier.journalAdvanced NanoBiomed Researches_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/EC/H2020/758224/EUes_ES
dc.rights.accessRightsopen accesses_ES
dc.relation.projectFECYTinfo:eu-repo/grantAgreement/MINECO//BFU2013-43149-R/ES/VIROLOGIA ESTRUCTURAL DE ROTAVIRUS/ es_ES
dc.relation.projectFISinfo:eu-repo/grantAgreement/ES/PI20CIII/00014es_ES


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