Preferential interaction of MHC class I with TAPBPR in the absence of glycosylation.
cam.issuedOnline | 2018-08 | |
dc.contributor.author | Neerincx, Andreas | |
dc.contributor.author | Boyle, Louise H | |
dc.contributor.orcid | Boyle, Louise [0000-0002-3105-6555] | |
dc.date.accessioned | 2018-09-10T22:15:52Z | |
dc.date.available | 2018-09-10T22:15:52Z | |
dc.date.issued | 2019-09 | |
dc.description.abstract | We 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.medium | Print-Electronic | |
dc.identifier.doi | 10.17863/CAM.27396 | |
dc.identifier.eissn | 1872-9142 | |
dc.identifier.issn | 0161-5890 | |
dc.identifier.uri | https://www.repository.cam.ac.uk/handle/1810/280032 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | Elsevier BV | |
dc.publisher.url | http://dx.doi.org/10.1016/j.molimm.2018.06.269 | |
dc.rights | Attribution 4.0 International (CC BY 4.0) | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.subject | Antigen processing and presentation | |
dc.subject | MHC | |
dc.subject | N-linked glycosylation | |
dc.subject | TAPBPR/TAPBPL | |
dc.subject | Tapasin | |
dc.subject | Calreticulin | |
dc.subject | Cell Line, Tumor | |
dc.subject | Endoplasmic Reticulum | |
dc.subject | Genes, MHC Class I | |
dc.subject | Glycosylation | |
dc.subject | HeLa Cells | |
dc.subject | Histocompatibility Antigens Class I | |
dc.subject | Humans | |
dc.subject | Immunoglobulins | |
dc.subject | Membrane Proteins | |
dc.subject | Membrane Transport Proteins | |
dc.subject | Peptides | |
dc.subject | Protein Disulfide-Isomerases | |
dc.title | Preferential interaction of MHC class I with TAPBPR in the absence of glycosylation. | |
dc.type | Article | |
dcterms.dateAccepted | 2018-06-14 | |
prism.endingPage | 66 | |
prism.publicationDate | 2019 | |
prism.publicationName | Mol Immunol | |
prism.startingPage | 58 | |
prism.volume | 113 | |
pubs.funder-project-id | Wellcome Trust (104647/Z/14/Z) | |
rioxxterms.licenseref.startdate | 2019-09 | |
rioxxterms.licenseref.uri | http://www.rioxx.net/licenses/all-rights-reserved | |
rioxxterms.type | Journal Article/Review | |
rioxxterms.version | VoR | |
rioxxterms.versionofrecord | 10.1016/j.molimm.2018.06.269 |
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