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dc.contributor.authorNeerincx, Andreas
dc.contributor.authorBoyle, Louise
dc.date.accessioned2018-09-10T22:15:52Z
dc.date.available2018-09-10T22:15:52Z
dc.date.issued2019-09
dc.identifier.issn0161-5890
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/280032
dc.description.abstractWe recently discovered that TAPBPR promotes reglucosylation of the N-linked glycan on MHC class I molecules, a modification that restores their recognition by calreticulin and reincorporation into the peptide-loading complex. We wondered whether TAPBPR displayed some degree of glycan specificity, as is known to be the case for tapasin via its interaction with calreticulin & ERp57, or whether its interaction with MHC class I was glycan independent. Here, we explored this by comparing the ability of TAPBPR to bind to MHC class I containing either an intact or disrupted NxS/T glycosylation consensus sequence. In contrast to tapasin, TAPBPR bound strongly to MHC class I molecules that lacked N-linked glycosylation, suggesting that the TAPBPR:MHC class I interaction is glycan independent. Furthermore, we found that glycosylated HLA-A2 preferentially interacts with tapasin rather than TAPBPR, possibly explaining, in part, why MHC class I molecules bind efficiently to tapasin in the face of an alternative chaperone. The distinction in glycan specificity between the two peptide editors suggests that TAPBPR may bind to MHC class I molecules that are associated with a broader diversity of oligosaccharides attached compared with tapasin. This may explain, to some extent, the ability of TAPBPR to interact with MHC class I molecules outside of the ER.
dc.format.mediumPrint-Electronic
dc.languageeng
dc.publisherElsevier BV
dc.rightsAttribution 4.0 International (CC BY 4.0)
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectCell Line, Tumor
dc.subjectHela Cells
dc.subjectEndoplasmic Reticulum
dc.subjectHumans
dc.subjectPeptides
dc.subjectImmunoglobulins
dc.subjectCalreticulin
dc.subjectMembrane Transport Proteins
dc.subjectMembrane Proteins
dc.subjectHistocompatibility Antigens Class I
dc.subjectGenes, MHC Class I
dc.subjectGlycosylation
dc.subjectProtein Disulfide-Isomerases
dc.titlePreferential interaction of MHC class I with TAPBPR in the absence of glycosylation.
dc.typeArticle
prism.endingPage66
prism.publicationDate2019
prism.publicationNameMol Immunol
prism.startingPage58
prism.volume113
dc.identifier.doi10.17863/CAM.27396
dcterms.dateAccepted2018-06-14
rioxxterms.versionofrecord10.1016/j.molimm.2018.06.269
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2019-09
dc.contributor.orcidBoyle, Louise [0000-0002-3105-6555]
dc.identifier.eissn1872-9142
rioxxterms.typeJournal Article/Review
pubs.funder-project-idWellcome Trust (104647/Z/14/Z)


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