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n3:pmcid: PMC0
bibo:doi: 10.1038%2Fncomms15924
n2:contains: _:vb65028479 _:vb65028498 _:vb65028522

Subject Item: _:vb65028479
rdf:type: n2:Section
dc:title: results
n2:contains: _:vb65028496 _:vb65028497 _:vb65028488 _:vb65028489 _:vb65028490 _:vb65028491 _:vb65028492 _:vb65028493 _:vb65028494 _:vb65028495 _:vb65028480 _:vb65028481 _:vb65028482 _:vb65028483 _:vb65028484 _:vb65028485 _:vb65028486 _:vb65028487

Subject Item: _:vb65028480
rdf:type: n3:Context
rdf:value: Importantly, similar hybrid constructs for other HLA class I genes have been described before, and shown to retain the peptide-binding specificity of the HLA allele>>19<<. The C*05 and C*07 hybrid constructs were transfected into HLA class I-negative 721.221 cells along with a GFP plasmid to control for transfection efficiency, and the level of HLA-C surface expression on transfected cells was determined
n3:mentions: n4:10946256

Subject Item: _:vb65028481
rdf:type: n3:Context
rdf:value: C*05 and C*07 transfected cells was physiologically relevant as it was comparable to the relative difference in expression between HLA-C*05 and HLA-C*07 on human peripheral blood lymphocytes, which is reported to be between 1.5 and 2-fold>>4<<. This was of particular interest considering that both our hybrid constructs had an identical 3′UTR, as well as a region starting from a part of intron 3 until, and including, exon 8.
n3:mentions: n4:23559252

Subject Item: _:vb65028482
rdf:type: n3:Context
rdf:value: promoter/5′UTR of C*07 on luciferase expression has been evidenced in a previous study, that included the region of its core promoter, and reported that the core promoter of C*07 was significantly more active than its C*06 counterpart>>20<<. To assess how the promoter directly influenced expression of the HLA-C molecules, we swapped the promoter/5′UTR of C*05 and C*07, and generated new hybrid constructs (Fig.
n3:mentions: n4:22113476

Subject Item: _:vb65028483
rdf:type: n3:Context
rdf:value: Although the anti-HLA antibody (W6/32) that we used to stain for HLA-C expression has monomorphic specificity and binds fully assembled HLA class I molecules with equal affinity>>21<<22, we included an N-terminal hemagglutinin (HA) tag in these constructs as an additional control.
n3:mentions: n4:19368562

Subject Item: _:vb65028484
rdf:type: n3:Context
rdf:value: Although the anti-HLA antibody (W6/32) that we used to stain for HLA-C expression has monomorphic specificity and binds fully assembled HLA class I molecules with equal affinity>>2122<<, we included an N-terminal hemagglutinin (HA) tag in these constructs as an additional control.
n3:mentions: n4:23510417

Subject Item: _:vb65028485
rdf:type: n3:Context
rdf:value: and non-tagged HLA-C constructs, suggesting that the HA tag, itself, does not change the HLA-C expression pattern or cellular characteristics, also shown by a previous study comparing HA-tagged and non-tagged HLA class I molecules>>23<<. To then test whether variation in α1 and α2 domains of the HLA-C molecules was responsible for the differential expression, we generated modified lentiviral expression constructs that contained only exons 1–3 of the C*05 and C*07 alleles
n3:mentions: n4:19917696

Subject Item: _:vb65028486
rdf:type: n3:Context
rdf:value: of HLA-C folding intermediates inside the cell, before successful peptide loading and export to the cell surface, such that total protein expression is unaffected but there is a differential expression level at the plasma membrane>>24<<25. Taken together, these data demonstrate that variation in the coding region of HLA-C, specifically the α1 and α2 domains, can drive differential HLA-C expression at the cell surface.
n3:mentions: n4:9551969

Subject Item: _:vb65028487
rdf:type: n3:Context
rdf:value: of HLA-C folding intermediates inside the cell, before successful peptide loading and export to the cell surface, such that total protein expression is unaffected but there is a differential expression level at the plasma membrane>>2425<<. Taken together, these data demonstrate that variation in the coding region of HLA-C, specifically the α1 and α2 domains, can drive differential HLA-C expression at the cell surface.
n3:mentions: n4:17956861

Subject Item: _:vb65028488
rdf:type: n3:Context
rdf:value: To elucidate the role of α1/α2 domains and the peptide-binding cleft of HLA-C on differential expression, we solved the structure of HLA-C*05 in complex with a HLA-C*05 specific peptide, SAEPVPLQL (SAE)>>26<<, and HLA-C*07 in complex with a HLA-C*07 specific peptide, RYRPGTVAL (RYR)27 (Supplementary Table 1).
n3:mentions: n4:11172028

Subject Item: _:vb65028489
rdf:type: n3:Context
rdf:value: the peptide-binding cleft of HLA-C on differential expression, we solved the structure of HLA-C*05 in complex with a HLA-C*05 specific peptide, SAEPVPLQL (SAE)26, and HLA-C*07 in complex with a HLA-C*07 specific peptide, RYRPGTVAL (RYR)>>27<< (Supplementary Table 1).
n3:mentions: n4:9768753

Subject Item: _:vb65028490
rdf:type: n3:Context
rdf:value: The presence of these smaller residues and Asp9 in HLA-C*07 is consistent with the preference of P2 Arg/Tyr for HLA-C*07-restricted peptides, as previously reported>>28<<. Similarly, the F pocket of HLA-C*05 was ‘filled’ by large aromatic residues (Phe116 and Trp147), which were absent from HLA-C*07 (Ser116 and Leu147) (Fig. 6b). In addition to the larger Trp147, the hinge of the α2-helix of HLA-C*05
n3:mentions: n4:25311805

Subject Item: _:vb65028491
rdf:type: n3:Context
rdf:value: To test this, we refolded both HLA-C*05 and HLA-C*07 with four different peptides, including two HLA-C*05 peptides (a self-peptide, ITASRFKEL (ITA)>>29<<, and the viral peptide SAE26 and two HLA-C*07 peptides (two self peptides, RYRPGTVAL (RYR)27 and KYFDEHYEY (KYF)30), and compared the thermal stability of these peptide-HLA-C complexes.
n3:mentions: n4:16112985

Subject Item: _:vb65028492
rdf:type: n3:Context
rdf:value: To test this, we refolded both HLA-C*05 and HLA-C*07 with four different peptides, including two HLA-C*05 peptides (a self-peptide, ITASRFKEL (ITA)29, and the viral peptide SAE>>26<< and two HLA-C*07 peptides (two self peptides, RYRPGTVAL (RYR)27 and KYFDEHYEY (KYF)30), and compared the thermal stability of these peptide-HLA-C complexes.
n3:mentions: n4:11172028

Subject Item: _:vb65028493
rdf:type: n3:Context
rdf:value: test this, we refolded both HLA-C*05 and HLA-C*07 with four different peptides, including two HLA-C*05 peptides (a self-peptide, ITASRFKEL (ITA)29, and the viral peptide SAE26 and two HLA-C*07 peptides (two self peptides, RYRPGTVAL (RYR)>>27<< and KYFDEHYEY (KYF)30), and compared the thermal stability of these peptide-HLA-C complexes.
n3:mentions: n4:9768753

Subject Item: _:vb65028494
rdf:type: n3:Context
rdf:value: both HLA-C*05 and HLA-C*07 with four different peptides, including two HLA-C*05 peptides (a self-peptide, ITASRFKEL (ITA)29, and the viral peptide SAE26 and two HLA-C*07 peptides (two self peptides, RYRPGTVAL (RYR)27 and KYFDEHYEY (KYF)>>30<<), and compared the thermal stability of these peptide-HLA-C complexes.
n3:mentions: n4:8265661

Subject Item: _:vb65028495
rdf:type: n3:Context
rdf:value: Our study, combined with previous work>>13<<, suggests that there are three regions of HLA-C that have the ability to regulate differential HLA-C expression, that is, the promoter/5′UTR, exons 2 and 3, and the 3′UTR.
n3:mentions: n4:21499264

Subject Item: _:vb65028496
rdf:type: n3:Context
rdf:value: For example, C*04 alleles, which have been shown to be expressed at high levels at the cell surface>>4<<, appear to be more similar to C*05 than to C*07 in the promoter/5′UTR, and exons 2 and 3 sequence.
n3:mentions: n4:23559252

Subject Item: _:vb65028497
rdf:type: n3:Context
rdf:value: This is particularly interesting for C*04, as, based on binding of miR-148a in the 3′UTR of its mRNA>>13<<, and its similarity to C*07 in the 3′UTR, it would have been predicted to be a low-expresser (Fig.
n3:mentions: n4:21499264

Subject Item: _:vb65028498
rdf:type: n2:Section
dc:title: methods
n2:contains: _:vb65028520 _:vb65028521 _:vb65028516 _:vb65028517 _:vb65028518 _:vb65028519 _:vb65028512 _:vb65028513 _:vb65028514 _:vb65028515 _:vb65028508 _:vb65028509 _:vb65028510 _:vb65028511 _:vb65028504 _:vb65028505 _:vb65028506 _:vb65028507 _:vb65028500 _:vb65028501 _:vb65028502 _:vb65028503 _:vb65028499

Subject Item: _:vb65028499
rdf:type: n3:Context
rdf:value: Soluble class I heterodimers of HLA-C*05 and HLA-C*07 heavy chain and full-length β2-microglobulin (β2m) were expressed in Escherichia coli as inclusion bodies as previously described>>43<<. Both HLA molecules were refolded with four peptides ITASRFKEL, SAEPVPLQL, RYRPGTVAL and KYFDEHYEY and thermal stability assay was performed.
n3:mentions: n4:19167249

Subject Item: _:vb65028500
rdf:type: n3:Context
rdf:value: The data were collected on the MX1 beamline at the Australian Synchrotron>>44<<, using the ADSC-Quantum 210 CCD detector (at 100 K).
n3:mentions: n4:25537608

Subject Item: _:vb65028501
rdf:type: n3:Context
rdf:value: Data were processed using the XDS>>45<< and scaled using SCALA software46 from the CCP4 suite47.
n3:mentions: n4:20124692

Subject Item: _:vb65028502
rdf:type: n3:Context
rdf:value: Data were processed using the XDS45 and scaled using SCALA software>>46<< from the CCP4 suite47.
n3:mentions: n4:16369096

Subject Item: _:vb65028503
rdf:type: n3:Context
rdf:value: Data were processed using the XDS45 and scaled using SCALA software46 from the CCP4 suite>>47<<. The structures were determined by molecular replacement using the PHASER48 program with the HLA-C*08 for the MHC model without the peptide (Protein Data Base accession number, 4NT6 (ref. 49)). Manual model building was conducted using
n3:mentions: n4:15299374

Subject Item: _:vb65028504
rdf:type: n3:Context
rdf:value: The structures were determined by molecular replacement using the PHASER>>48<< program with the HLA-C*08 for the MHC model without the peptide (Protein Data Base accession number, 4NT6 (ref.
n3:mentions: n4:11567148

Subject Item: _:vb65028505
rdf:type: n3:Context
rdf:value: using SCALA software46 from the CCP4 suite47. The structures were determined by molecular replacement using the PHASER48 program with the HLA-C*08 for the MHC model without the peptide (Protein Data Base accession number, 4NT6 (ref. >>49<<)). Manual model building was conducted using the Coot software50 followed by maximum-likelihood refinement with the Buster program51 or Refmac form the CCP4 suite47.
n3:mentions: n4:24990997

Subject Item: _:vb65028506
rdf:type: n3:Context
rdf:value: Manual model building was conducted using the Coot software>>50<< followed by maximum-likelihood refinement with the Buster program51 or Refmac form the CCP4 suite47.
n3:mentions: n4:20383002

Subject Item: _:vb65028507
rdf:type: n3:Context
rdf:value: Manual model building was conducted using the Coot software50 followed by maximum-likelihood refinement with the Buster program>>51<< or Refmac form the CCP4 suite47.
n3:mentions: n4:21460447

Subject Item: _:vb65028508
rdf:type: n3:Context
rdf:value: Manual model building was conducted using the Coot software50 followed by maximum-likelihood refinement with the Buster program51 or Refmac form the CCP4 suite>>47<<. The final models have been validated using the Protein Data Base validation website and the final refinement statistics are summarized in supplementary table 1. All molecular graphics representations were created using PyMol52.
n3:mentions: n4:15299374

Subject Item: _:vb65028509
rdf:type: n3:Context
rdf:value: The HLA class-I negative 721.221 cells stably transfected with HLA-C*05:01 or HLA-C*07:02 were utilized to obtain the peptide repertoires in a previously described manner>>53<<54. In short, HLA class I were purified from a total 4 × 109 721.221 cells for each HLA-C using the pan class I antibody W6/32 immobilized and cross-linked to protein A resin.
n3:mentions: n4:24397554

Subject Item: _:vb65028510
rdf:type: n3:Context
rdf:value: The HLA class-I negative 721.221 cells stably transfected with HLA-C*05:01 or HLA-C*07:02 were utilized to obtain the peptide repertoires in a previously described manner>>5354<<. In short, HLA class I were purified from a total 4 × 109 721.221 cells for each HLA-C using the pan class I antibody W6/32 immobilized and cross-linked to protein A resin.
n3:mentions: n4:26700050

Subject Item: _:vb65028511
rdf:type: n3:Context
rdf:value: The dissociated complexes were further separated by Reversed-phase HPLC to isolate and fractionate the bound peptides before analysis with a Q Exactive Hybrid Quadrupole-Orbitrap Mass Spectrometer (Thermo Scientific)>>54<<. Peptides were identified by database search using the human UniProtKB/SwissProt database (Feb 2016) with ProteinPilot V5.0 (SCIEX). A false discovery rate of 5% was applied and known contaminant peptides removed from the final list of
n3:mentions: n4:26700050

Subject Item: _:vb65028512
rdf:type: n3:Context
rdf:value: Nucleotide sequences for HLA-C and chimpanzee MHC-C alleles were obtained from the IMGT database>>55<<. All chimpanzee sequences in the database were considered and a subset of human sequences was selected in each allele subclass.
n3:mentions: n4:25414341

Subject Item: _:vb65028513
rdf:type: n3:Context
rdf:value: was selected in each allele subclass. The region of the sequences aligned included exons 2 and 3 region (without the intron) and spanned 546 bp for the C*05 and C*07 sequences. Sequences were aligned with MUSCLE (v3.8.31) (ref. >>56<<) and the exons 2 and 3 sequences were extracted from the alignment. MrBayes (v3.2.5) (ref.
n3:mentions: n4:15034147

Subject Item: _:vb65028514
rdf:type: n3:Context
rdf:value: 2 and 3 region (without the intron) and spanned 546 bp for the C*05 and C*07 sequences. Sequences were aligned with MUSCLE (v3.8.31) (ref. 56) and the exons 2 and 3 sequences were extracted from the alignment. MrBayes (v3.2.5) (ref. >>57<<) was used to infer the phylogenetic relationship between sequences using the GTR model of nucleotide evolution with rate gamma distributed, running parameters used were nruns=3, nchains=4, ngen=2000000 and samplefreq=1000.
n3:mentions: n4:22357727

Subject Item: _:vb65028515
rdf:type: n3:Context
rdf:value: For each complete sequence, we determined the HLA-C allele by aligning the individual sequence in the HLA-C IMGT data set>>55<< to the query sequence and assigning the most similar allele.
n3:mentions: n4:25414341

Subject Item: _:vb65028516
rdf:type: n3:Context
rdf:value: Fig. 8 for completion. For display on the heat map, one representative sequence of each allele type was chosen. Pairwise alignments were performed with the Needleman–Wunsch algorithm in the EMBOSS package (v. 6.6.0.0) (ref. >>59<<). Multiple sequence alignments were performed for each regulatory region (promoter and 5′UTR, exons 2–3, and 3′UTR) using MUSCLE (v3.8.31) (ref.
n3:mentions: n4:10827456

Subject Item: _:vb65028517
rdf:type: n3:Context
rdf:value: performed with the Needleman–Wunsch algorithm in the EMBOSS package (v. 6.6.0.0) (ref. 59). Multiple sequence alignments were performed for each regulatory region (promoter and 5′UTR, exons 2–3, and 3′UTR) using MUSCLE (v3.8.31) (ref. >>56<<) and phylogenetic trees were generated using MrBayes (v3.2.5) (ref. 57) with model parameters mentioned previously.
n3:mentions: n4:15034147

Subject Item: _:vb65028518
rdf:type: n3:Context
rdf:value: 56) and phylogenetic trees were generated using MrBayes (v3.2.5) (ref. >>57<<) with model parameters mentioned previously.
n3:mentions: n4:22357727

Subject Item: _:vb65028519
rdf:type: n3:Context
rdf:value: This was done in the following way: phylogenetic distances as branch lengths from the HLA-C allele to HLA-C*05 and to HLA-C*07 were extracted using the R package ape>>60<<, the similarity metric was then calculated as the ratio of the distance of the query HLA-C sequence to HLA-C*05 divided by the sum of the distances of the query HLA-C sequence to HLA-C*05 and HLA-C*07.
n3:mentions: n4:14734327

Subject Item: _:vb65028520
rdf:type: n3:Context
rdf:value: Structural information has been deposited in the Protein Data Bank>>61<< under accession numbers 5VGD (HLA-C*05:01-SAE) and 5VGE (HLA-C*07:02-RYR).
n3:mentions: n4:10592235

Subject Item: _:vb65028521
rdf:type: n3:Context
rdf:value: The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE>>62<< partner repository with the data set identifier PXD006455.
n3:mentions: n4:26527722

Subject Item: _:vb65028522
rdf:type: n2:Section
dc:title: discussion
n2:contains: _:vb65028548 _:vb65028549 _:vb65028550 _:vb65028551 _:vb65028544 _:vb65028545 _:vb65028546 _:vb65028547 _:vb65028524 _:vb65028525 _:vb65028526 _:vb65028527 _:vb65028523 _:vb65028540 _:vb65028541 _:vb65028542 _:vb65028543 _:vb65028536 _:vb65028537 _:vb65028538 _:vb65028539 _:vb65028532 _:vb65028533 _:vb65028534 _:vb65028535 _:vb65028528 _:vb65028529 _:vb65028530 _:vb65028531

Subject Item: _:vb65028523
rdf:type: n3:Context
rdf:value: suggested that an enhancer κB element in the core HLA-C promoter was responsible for its differential effect on the luciferase reporter; however, they did not investigate the direct effects of the core promoter on HLA-C expression levels>>20<<. We do not find any evidence that the region of the promoter/5′UTR of HLA-C tested in this study has any significant effect on HLA-C mRNA levels; however, it is feasible that elements outside of the tested sequence could impact mRNA
n3:mentions: n4:22113476

Subject Item: _:vb65028524
rdf:type: n3:Context
rdf:value: Small differences in expression level of MHC/HLA genes can influence response to pathogens, tumours, autoimmunity, as well as transplantation, potentially through both the acquired and innate immune response pathways>>4<<51131323334.
n3:mentions: n4:23559252

Subject Item: _:vb65028525
rdf:type: n3:Context
rdf:value: Small differences in expression level of MHC/HLA genes can influence response to pathogens, tumours, autoimmunity, as well as transplantation, potentially through both the acquired and innate immune response pathways>>45<<1131323334.
n3:mentions: n4:25323824

Subject Item: _:vb65028526
rdf:type: n3:Context
rdf:value: Small differences in expression level of MHC/HLA genes can influence response to pathogens, tumours, autoimmunity, as well as transplantation, potentially through both the acquired and innate immune response pathways>>4511<<31323334. Hence, even a two-fold difference that is observed between HLA-C allotypes, such as HLA-C*05 and HLA-C*07, is likely to have functional consequences in influencing the efficacy of the immune response. HLA-C is expressed at lower
n3:mentions: n4:24248364

Subject Item: _:vb65028527
rdf:type: n3:Context
rdf:value: Small differences in expression level of MHC/HLA genes can influence response to pathogens, tumours, autoimmunity, as well as transplantation, potentially through both the acquired and innate immune response pathways>>451131<<323334. Hence, even a two-fold difference that is observed between HLA-C allotypes, such as HLA-C*05 and HLA-C*07, is likely to have functional consequences in influencing the efficacy of the immune response. HLA-C is expressed at lower
n3:mentions: n4:25485681

Subject Item: _:vb65028528
rdf:type: n3:Context
rdf:value: Small differences in expression level of MHC/HLA genes can influence response to pathogens, tumours, autoimmunity, as well as transplantation, potentially through both the acquired and innate immune response pathways>>45113132<<3334. Hence, even a two-fold difference that is observed between HLA-C allotypes, such as HLA-C*05 and HLA-C*07, is likely to have functional consequences in influencing the efficacy of the immune response. HLA-C is expressed at lower
n3:mentions: n4:16636135

Subject Item: _:vb65028529
rdf:type: n3:Context
rdf:value: Small differences in expression level of MHC/HLA genes can influence response to pathogens, tumours, autoimmunity, as well as transplantation, potentially through both the acquired and innate immune response pathways>>4511313233<<34. Hence, even a two-fold difference that is observed between HLA-C allotypes, such as HLA-C*05 and HLA-C*07, is likely to have functional consequences in influencing the efficacy of the immune response.
n3:mentions: n4:14610278

Subject Item: _:vb65028530
rdf:type: n3:Context
rdf:value: Small differences in expression level of MHC/HLA genes can influence response to pathogens, tumours, autoimmunity, as well as transplantation, potentially through both the acquired and innate immune response pathways>>451131323334<<. Hence, even a two-fold difference that is observed between HLA-C allotypes, such as HLA-C*05 and HLA-C*07, is likely to have functional consequences in influencing the efficacy of the immune response.
n3:mentions: n4:22496224

Subject Item: _:vb65028531
rdf:type: n3:Context
rdf:value: HLA-C is expressed at lower levels and is limited in polymorphism compared to its counterparts, HLA-A and HLA-B>>7<<8910. However, HLA-C is a prototypical KIR ligand and is important in the regulation of NK cell activity7. Although KIRs are capable of binding multiple HLA-C allotypes, it is plausible that differences in expression of HLA-C allotypes
n3:mentions: n4:16824023

Subject Item: _:vb65028532
rdf:type: n3:Context
rdf:value: HLA-C is expressed at lower levels and is limited in polymorphism compared to its counterparts, HLA-A and HLA-B>>78<<910. However, HLA-C is a prototypical KIR ligand and is important in the regulation of NK cell activity7. Although KIRs are capable of binding multiple HLA-C allotypes, it is plausible that differences in expression of HLA-C allotypes have
n3:mentions: n4:332508

Subject Item: _:vb65028533
rdf:type: n3:Context
rdf:value: HLA-C is expressed at lower levels and is limited in polymorphism compared to its counterparts, HLA-A and HLA-B>>789<<10. However, HLA-C is a prototypical KIR ligand and is important in the regulation of NK cell activity7. Although KIRs are capable of binding multiple HLA-C allotypes, it is plausible that differences in expression of HLA-C allotypes have
n3:mentions: n4:1383381

Subject Item: _:vb65028534
rdf:type: n3:Context
rdf:value: HLA-C is expressed at lower levels and is limited in polymorphism compared to its counterparts, HLA-A and HLA-B>>78910<<. However, HLA-C is a prototypical KIR ligand and is important in the regulation of NK cell activity7. Although KIRs are capable of binding multiple HLA-C allotypes, it is plausible that differences in expression of HLA-C allotypes have a
n3:mentions: n4:25754738

Subject Item: _:vb65028535
rdf:type: n3:Context
rdf:value: However, HLA-C is a prototypical KIR ligand and is important in the regulation of NK cell activity>>7<<. Although KIRs are capable of binding multiple HLA-C allotypes, it is plausible that differences in expression of HLA-C allotypes have a downstream influence on KIR signalling and NK cell function. The broad peptide specificity of KIRs35
n3:mentions: n4:16824023

Subject Item: _:vb65028536
rdf:type: n3:Context
rdf:value: The broad peptide specificity of KIRs>>35<< raises the question of whether alleles such as HLA-C*05, whose stability is less reliant on the sequence of the bound peptide, are potentially better KIR ligands.
n3:mentions: n4:24744756

Subject Item: _:vb65028537
rdf:type: n3:Context
rdf:value: that attempted to understand the peptide-binding specificities of HLA-C molecules suggested that no conservation at P2 is observed for HLA-C*05-restricted peptides, hence allowing a greater diversity of amino acids to bind the B pocket>>28<<. However, the authors described that a HLA-C*05-specific peptide would have a preference for an Asp at position 3.
n3:mentions: n4:25311805

Subject Item: _:vb65028538
rdf:type: n3:Context
rdf:value: as inefficient peptide binding or association with chaperons such as TAP (transporter associated with peptide-loading) or tapasin have been proposed to contribute towards lower surface expression of HLA-C in comparison to HLA-A and HLA-B>>24<<2536; however, this has not yet been reported for differential surface expression of HLA-C alleles.
n3:mentions: n4:9551969

Subject Item: _:vb65028539
rdf:type: n3:Context
rdf:value: inefficient peptide binding or association with chaperons such as TAP (transporter associated with peptide-loading) or tapasin have been proposed to contribute towards lower surface expression of HLA-C in comparison to HLA-A and HLA-B>>2425<<36; however, this has not yet been reported for differential surface expression of HLA-C alleles.
n3:mentions: n4:17956861

Subject Item: _:vb65028540
rdf:type: n3:Context
rdf:value: peptide binding or association with chaperons such as TAP (transporter associated with peptide-loading) or tapasin have been proposed to contribute towards lower surface expression of HLA-C in comparison to HLA-A and HLA-B>>242536<<; however, this has not yet been reported for differential surface expression of HLA-C alleles.
n3:mentions: n4:21355865

Subject Item: _:vb65028541
rdf:type: n3:Context
rdf:value: Studies of chicken MHC have reported an inverse correlation between diversity of peptide repertoire and cell surface MHC class I expression, with low expression correlating with resistance to Marek’s disease>>37<<38. However, structural analyses of high- and low-expressing chicken MHC class I molecules importantly reveal that the width of the peptide-binding groove is large in low-expressing molecules, and narrow in high-expressing MHC class I
n3:mentions: n4:25860507

Subject Item: _:vb65028542
rdf:type: n3:Context
rdf:value: Studies of chicken MHC have reported an inverse correlation between diversity of peptide repertoire and cell surface MHC class I expression, with low expression correlating with resistance to Marek’s disease>>3738<<. However, structural analyses of high- and low-expressing chicken MHC class I molecules importantly reveal that the width of the peptide-binding groove is large in low-expressing molecules, and narrow in high-expressing MHC class I
n3:mentions: n4:18083574

Subject Item: _:vb65028543
rdf:type: n3:Context
rdf:value: structural analyses of high- and low-expressing chicken MHC class I molecules importantly reveal that the width of the peptide-binding groove is large in low-expressing molecules, and narrow in high-expressing MHC class I molecules>>37<<3839. Similarly, a difference in thermal stability is correlated to surface expression levels40.
n3:mentions: n4:25860507

Subject Item: _:vb65028544
rdf:type: n3:Context
rdf:value: structural analyses of high- and low-expressing chicken MHC class I molecules importantly reveal that the width of the peptide-binding groove is large in low-expressing molecules, and narrow in high-expressing MHC class I molecules>>3738<<39. Similarly, a difference in thermal stability is correlated to surface expression levels40.
n3:mentions: n4:18083574

Subject Item: _:vb65028545
rdf:type: n3:Context
rdf:value: structural analyses of high- and low-expressing chicken MHC class I molecules importantly reveal that the width of the peptide-binding groove is large in low-expressing molecules, and narrow in high-expressing MHC class I molecules>>373839<<. Similarly, a difference in thermal stability is correlated to surface expression levels40.
n3:mentions: n4:23041567

Subject Item: _:vb65028546
rdf:type: n3:Context
rdf:value: Similarly, a difference in thermal stability is correlated to surface expression levels>>40<<. The presentation of peptides on the cell surface of chicken MHC is reliant on the peptide-translocation specificity of TAP, which is known to vary between chicken haplotypes and by TAP polymorphism3940; such peptide-translocation
n3:mentions: n4:26699458

Subject Item: _:vb65028547
rdf:type: n3:Context
rdf:value: The presentation of peptides on the cell surface of chicken MHC is reliant on the peptide-translocation specificity of TAP, which is known to vary between chicken haplotypes and by TAP polymorphism>>39<<40; such peptide-translocation specificity of TAP is not found in humans41.
n3:mentions: n4:23041567

Subject Item: _:vb65028548
rdf:type: n3:Context
rdf:value: The presentation of peptides on the cell surface of chicken MHC is reliant on the peptide-translocation specificity of TAP, which is known to vary between chicken haplotypes and by TAP polymorphism>>3940<<; such peptide-translocation specificity of TAP is not found in humans41.
n3:mentions: n4:26699458

Subject Item: _:vb65028549
rdf:type: n3:Context
rdf:value: cell surface of chicken MHC is reliant on the peptide-translocation specificity of TAP, which is known to vary between chicken haplotypes and by TAP polymorphism3940; such peptide-translocation specificity of TAP is not found in humans>>41<<.
n3:mentions: n4:7664780

Subject Item: _:vb65028550
rdf:type: n3:Context
rdf:value: By contrast, the 3′ miRNA binding site polymorphism seems to have arisen since the split of the human and chimpanzee ancestors, through a gene conversion event from an HLA-B sequence>>16<<. Similarly, there seems to be no evidence for shared polymorphism in the promoter region, likewise indicating that these variants have also risen since the species diverged42. This complex evolutionary and regulatory landscape is
n3:mentions: n4:21907013

Subject Item: _:vb65028551
rdf:type: n3:Context
rdf:value: Similarly, there seems to be no evidence for shared polymorphism in the promoter region, likewise indicating that these variants have also risen since the species diverged>>42<<. This complex evolutionary and regulatory landscape is suggestive of an ever-changing selective regime, perhaps resulting from transient selection for up- or downregulation of specific groups of alleles with particular binding
n3:mentions: n4:22422862

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