A mechanistic basis for the co-evolution of chicken tapasin and major histocompatibility complex class I (MHC I) proteins
A mechanistic basis for the co-evolution of chicken tapasin and major histocompatibility complex class I (MHC I) proteins
MHC class I molecules display peptides at the cell surface to cytotoxic T cells. The co-factor tapasin functions to ensure MHC I become loaded with high affinity peptides. In most mammals, the tapasin gene appears to have little sequence diversity and few alleles and is located distal to several classical MHC I loci, so tapasin appears to function in a universal way to assist MHC I peptide loading. In contrast the chicken tapasin gene is tightly linked to the single dominantly expressed MHC I locus, is highly polymorphic and moderately diverse in sequence. Therefore tapasin-assisted loading of MHC I in chickens may occur in a haplotype-specific way, via the co-evolution of chicken tapasin and MHC I. Here we demonstrate a mechanistic basis for this co-evolution, revealing differences in the ability of two chicken MHC I alleles to bind and release peptides in the presence or absence of tapasin, where like in mammals efficient self-loading is negatively correlated with tapasin-assisted loading. We found that a polymorphic residue in the MHC I ?3 domain thought to bind tapasin influenced both tapasin function as well as intrinsic peptide-binding properties. Differences were also evident between the MHC alleles in their interactions with tapasin. Lastly we show that a mismatched combination of tapasin and MHC alleles exhibit significantly impaired MHC I maturation in vivo, and that polymorphic MHC residues thought to contact tapasin influence maturation efficiency. Collectively this supports the possibility that tapasin and BF2 proteins have co-evolved resulting in allele-specific peptide-loading in vivo.
antigen presentation, evolution, immunology, major histocompatibility complex (mhc), protein-protein interactions, chicken mhc, co-evolution, peptide selection, tapasin
n/a
Van Hateren, A.
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Carter, R.
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Bailey, A.
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Kontouli, N.
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Williams, A.P.
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Kaufman, J.
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Elliott, T.J.
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Van Hateren, A.
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Carter, R.
840a775a-867e-42ba-a7cb-d131c9fdb9c6
Bailey, A.
541e2cd9-ac72-4058-9293-def64fc2c284
Kontouli, N.
63602628-7753-421d-817e-071cd752b848
Williams, A.P.
973ff46f-46f1-4d7c-b27d-0f53221e4c44
Kaufman, J.
3efdcaaf-f10f-4b98-944f-3fc88f5508c7
Elliott, T.J.
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Van Hateren, A., Carter, R., Bailey, A., Kontouli, N., Williams, A.P., Kaufman, J. and Elliott, T.J.
(2013)
A mechanistic basis for the co-evolution of chicken tapasin and major histocompatibility complex class I (MHC I) proteins.
The Journal of Biological Chemistry, n/a, .
(doi:10.1074/jbc.M113.474031).
(PMID:24078633)
Abstract
MHC class I molecules display peptides at the cell surface to cytotoxic T cells. The co-factor tapasin functions to ensure MHC I become loaded with high affinity peptides. In most mammals, the tapasin gene appears to have little sequence diversity and few alleles and is located distal to several classical MHC I loci, so tapasin appears to function in a universal way to assist MHC I peptide loading. In contrast the chicken tapasin gene is tightly linked to the single dominantly expressed MHC I locus, is highly polymorphic and moderately diverse in sequence. Therefore tapasin-assisted loading of MHC I in chickens may occur in a haplotype-specific way, via the co-evolution of chicken tapasin and MHC I. Here we demonstrate a mechanistic basis for this co-evolution, revealing differences in the ability of two chicken MHC I alleles to bind and release peptides in the presence or absence of tapasin, where like in mammals efficient self-loading is negatively correlated with tapasin-assisted loading. We found that a polymorphic residue in the MHC I ?3 domain thought to bind tapasin influenced both tapasin function as well as intrinsic peptide-binding properties. Differences were also evident between the MHC alleles in their interactions with tapasin. Lastly we show that a mismatched combination of tapasin and MHC alleles exhibit significantly impaired MHC I maturation in vivo, and that polymorphic MHC residues thought to contact tapasin influence maturation efficiency. Collectively this supports the possibility that tapasin and BF2 proteins have co-evolved resulting in allele-specific peptide-loading in vivo.
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e-pub ahead of print date: 27 September 2013
Keywords:
antigen presentation, evolution, immunology, major histocompatibility complex (mhc), protein-protein interactions, chicken mhc, co-evolution, peptide selection, tapasin
Organisations:
Cancer Sciences
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Local EPrints ID: 358904
URI: http://eprints.soton.ac.uk/id/eprint/358904
ISSN: 0021-9258
PURE UUID: c55c2c2b-efca-40ad-8018-5883f173212d
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Date deposited: 21 Oct 2013 13:23
Last modified: 15 Mar 2024 03:47
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Author:
R. Carter
Author:
A. Bailey
Author:
N. Kontouli
Author:
J. Kaufman
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