ArticleThe Journal of biological chemistry2013
A mechanistic basis for the co-evolution of chicken tapasin and major histocompatibility complex class I (MHC I) proteins.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 49 citations in OpenAlex.
- Genetic characterization of the TAPBP and its allelic association with BF2 in the chicken major histocompatibility complex.Immunogenetics · 2026Article
- A Chicken Tapasin ortholog can chaperone empty HLA-B∗37:01 molecules independent of other peptide-loading components.The Journal of biological chemistry · 2023Article
- A Wider and Deeper Peptide-Binding Groove for the Class I Molecules from B15 Compared with B19 Chickens Correlates with Relative Resistance to Marek's Disease.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- New vistas unfold: Chicken MHC molecules reveal unexpected ways to present peptides to the immune system.Frontiers in immunology · 2022Review
- Coevolution between MHC Class I and Antigen-Processing Genes in Salamanders.Molecular biology and evolution · 2021Article
- Chickens as a simple system for scientific discovery: The example of the MHC.Molecular immunology · 2021Article
- Conformational sensing of major histocompatibility complex (MHC) class I molecules by immune receptors and intracellular assembly factors.Current opinion in immunology · 2021Review
- Molecular Evolution of Antigen-Processing Genes in Salamanders: Do They Coevolve with MHC Class I Genes?Genome biology and evolution · 2021Article
- A potential nomenclature for the Immuno Polymorphism Database (IPD) of chicken MHC genes: progress and problems.Immunogenetics · 2020Review
- Selective Stimulation of Duplicated Atlantic Salmon MHC Pathway Genes by Interferon-Gamma.Frontiers in immunology · 2020Article
- From Chickens to Humans: The Importance of Peptide Repertoires for MHC Class I Alleles.Frontiers in immunology · 2020Review
- Development and optimization of a hybridization technique to type the classical class I and class II B genes of the chicken MHC.Immunogenetics · 2019Article
- Review
- Dynamically Driven Allostery in MHC Proteins: Peptide-Dependent Tuning of Class I MHC Global Flexibility.Frontiers in immunology · 2019Article
- Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle.Nature chemical biology · 2018Article
- Article
- Generalists and Specialists: A New View of How MHC Class I Molecules Fight Infectious Pathogens.Trends in immunology · 2018Review
- Whole genome duplications have provided teleosts with many roads to peptide loaded MHC class I molecules.BMC evolutionary biology · 2018Article
- Direct evidence for conformational dynamics in major histocompatibility complex class I molecules.The Journal of biological chemistry · 2017Article
- Recent advances in Major Histocompatibility Complex (MHC) class I antigen presentation: Plastic MHC molecules and TAPBPR-mediated quality control.F1000Research · 2017Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
MHC class I molecules display peptides at the cell surface to cytotoxic T cells. The co-factor tapasin functions to ensure that MHC I becomes 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 and 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, as in mammals, efficient self-loading is negatively correlated with tapasin-assisted loading. We found that a polymorphic residue in the MHC I α3 domain thought to bind tapasin influenced both tapasin function and intrinsic peptide binding properties. Differences were also evident between the MHC alleles in their interactions with tapasin. Last, 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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.