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dc.contributor.authorIles, Jason
dc.contributor.authorZmuidinaite, Raminta
dc.contributor.authorSadee, Christoph
dc.contributor.authorGardiner, Anna
dc.contributor.authorLacey, Jonathan
dc.contributor.authorHarding, Stephen
dc.contributor.authorUle, Jernej
dc.contributor.authorRoblett, Debra
dc.contributor.authorHeeney, Jonathan
dc.contributor.authorBaxendale, Helen
dc.contributor.authorIles, Ray K
dc.date.accessioned2022-05-25T01:04:48Z
dc.date.available2022-05-25T01:04:48Z
dc.date.issued2022-04-08
dc.identifier.issn1661-6596
dc.identifier.other35456942
dc.identifier.otherPMC9030890
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/337451
dc.description.abstractThe immune response to SARS-CoV-2 infection requires antibody recognition of the spike protein. In a study designed to examine the molecular features of anti-spike and anti-nucleocapsid antibodies, patient plasma proteins binding to pre-fusion stabilised complete spike and nucleocapsid proteins were isolated and analysed by matrix-assisted laser desorption ionisation-time of flight (MALDI-ToF) mass spectrometry. Amongst the immunoglobulins, a high affinity for human serum albumin was evident in the anti-spike preparations. Careful mass comparison revealed the preferential capture of advanced glycation end product (AGE) forms of glycated human serum albumin by the pre-fusion spike protein. The ability of bacteria and viruses to surround themselves with serum proteins is a recognised immune evasion and pathogenic process. The preference of SARS-CoV-2 for AGE forms of glycated serum albumin may in part explain the severity and pathology of acute respiratory distress and the bias towards the elderly and those with (pre)diabetic and atherosclerotic/metabolic disease.
dc.languageeng
dc.publisherMDPI AG
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourcenlmid: 101092791
dc.sourceessn: 1422-0067
dc.subjectHumans
dc.subjectDiabetes Mellitus, Type 2
dc.subjectPrediabetic State
dc.subjectSerum Albumin
dc.subjectAntibodies, Viral
dc.subjectAged
dc.subjectSpike Glycoprotein, Coronavirus
dc.subjectSerum Albumin, Human
dc.subjectCOVID-19
dc.subjectSARS-CoV-2
dc.titleSARS-CoV-2 Spike Protein Binding of Glycated Serum Albumin-Its Potential Role in the Pathogenesis of the COVID-19 Clinical Syndromes and Bias towards Individuals with Pre-Diabetes/Type 2 Diabetes and Metabolic Diseases.
dc.typeArticle
dc.date.updated2022-05-25T01:04:48Z
prism.issueIdentifier8
prism.publicationNameInt J Mol Sci
prism.volume23
dc.identifier.doi10.17863/CAM.84864
dcterms.dateAccepted2022-04-06
rioxxterms.versionofrecord10.3390/ijms23084126
rioxxterms.versionVoR
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidZmuidinaite, Raminta [0000-0001-7728-6623]
dc.contributor.orcidSadee, Christoph [0000-0001-7416-1470]
dc.contributor.orcidIles, Ray K [0000-0003-0573-9739]
dc.identifier.eissn1422-0067
cam.issuedOnline2022-04-08


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International