TAPBPR uses the same residues as tapasin to associate with MHC class I

Abstract

Event Abstract Back to Event TAPBPR uses the same residues as tapasin to associate with MHC class I Clemens Hermann1*, Lisa M. Strittmatter1 and Louise H. Boyle1 1 Cambridge Institute of Medical Research, University of Cambridge, Department of Pathology, United Kingdom In order to induce an appropriate T cell response, MHC class I molecules must be loaded with high affinity peptide. The key player for peptide loading is the MHC class I dedicated chaperone tapasin. Recently we have found a tapasin related protein called TAPBPR which is an additional component of the antigen presentation system. Like tapasin, TAPBPR binds to a heterodimer of MHC class I heavy chain and β2m. In contrast to tapasin, TAPBPR is not a component of the peptide loading complex and is not required for peptide loading. However, it controls the ER export rate of MHC class I molecules. Here we have characterised the interaction between TAPBPR and MHC class I. Residues in the N-terminal and IgC domain of tapasin which are important for its association with MHC class I are highly conserved in TAPBPR. Site-directed mutagenesis of these residues followed by immunoprecipitation of TAPBPR revealed that mutation of I261 or E205, R207, Q209, Q272 in the N-terminal domain and R335, Q336 and S337 in the IgC domain abolishes binding of TAPBPR to MHC class I. Tapasin is known to associate with specific residues on MHC class I such as T134, D227 and E229. We have identified that these residues are also essential for TAPBPR binding to MHC class I. The identification of TAPBPR as an additional MHC class I specific chaperon which binds to MHC class I in a similar way as tapasin has significant implications on our understanding of MHC class I biology. Keywords: human, MHC, Antigen Presentation/Processing, MHC class I, MHC biology Conference: 15th International Congress of Immunology (ICI), Milan, Italy, 22 Aug - 27 Aug, 2013. Presentation Type: Abstract Topic: Adaptive Immunity Citation: Hermann C, Strittmatter LM and Boyle LH (2013). TAPBPR uses the same residues as tapasin to associate with MHC class I. Front. Immunol. Conference Abstract: 15th International Congress of Immunology (ICI). doi: 10.3389/conf.fimmu.2013.02.01042 Copyright: The abstracts in this collection have not been subject to any Frontiers peer review or checks, and are not endorsed by Frontiers. They are made available through the Frontiers publishing platform as a service to conference organizers and presenters. The copyright in the individual abstracts is owned by the author of each abstract or his/her employer unless otherwise stated. Each abstract, as well as the collection of abstracts, are published under a Creative Commons CC-BY 4.0 (attribution) licence (https://creativecommons.org/licenses/by/4.0/) and may thus be reproduced, translated, adapted and be the subject of derivative works provided the authors and Frontiers are attributed. For Frontiers’ terms and conditions please see https://www.frontiersin.org/legal/terms-and-conditions. Received: 29 Jun 2013; Published Online: 22 Aug 2013. * Correspondence: Mr. Clemens Hermann, Cambridge Institute of Medical Research, University of Cambridge, Department of Pathology, Cambridge, CB2 0XY, United Kingdom, cbbh3@cam.ac.uk Login Required This action requires you to be registered with Frontiers and logged in. To register or login click here. Abstract Info Abstract The Authors in Frontiers Clemens Hermann Lisa M Strittmatter Louise H Boyle Google Clemens Hermann Lisa M Strittmatter Louise H Boyle Google Scholar Clemens Hermann Lisa M Strittmatter Louise H Boyle PubMed Clemens Hermann Lisa M Strittmatter Louise H Boyle Related Article in Frontiers Google Scholar PubMed Abstract Close Back to top Javascript is disabled. Please enable Javascript in your browser settings in order to see all the content on this page.