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Journal articles on the topic 'Major histocompatibility complex I (MHCI)'

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Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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1

Matte-Martone, Catherine, Jinli Liu, Dhanpat Jain, Jennifer McNiff, and Warren D. Shlomchik. "CD8+ but not CD4+ T cells require cognate interactions with target tissues to mediate GVHD across only minor H antigens, whereas both CD4+ and CD8+ T cells require direct leukemic contact to mediate GVL." Blood 111, no. 7 (April 1, 2008): 3884–92. http://dx.doi.org/10.1182/blood-2007-11-125294.

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Abstract Whether T-cell antigen receptors (TCR) on donor T cells require direct interactions with major histocompatibility complex class I or class II (MHCI/MHCII) molecules on target cells to mediate graft-versus-host disease (GVHD) and graft-versus-leukemia (GVL) is a fundamental question in allogeneic stem-cell transplantation (alloSCT). In MHC-mismatched mouse models, these contacts were not required for GVHD. However, this conclusion may not apply to MHC-matched, multiple minor histocompatibility antigen-mismatched alloSCT, the most common type performed clinically. To address this, we used wild-type (wt)→MHCI−/− or wt→MHCII−/− bone marrow chimeras as recipients in GVHD experiments. For GVL experiments, we used MHCI−/− or MHCII−/− chronic-phase CML cells created by expressing the BCR-ABL cDNA in bone marrow from MHCI−/− or MHCII−/− mice. TCR/MHCI contact was obligatory for both CD8-mediated GVHD and GVL. In contrast, CD4 cells induced GVHD in wt→MHCII−/− chimeras, whereas MHCII−/− mCP-CML was GVL-resistant. Donor CD4 cells infiltrated affected skin and bowel in wt→MHCII−/− recipients, indicating that they mediated GVHD by acting locally. Thus, CD4 cells use distinct effector mechanisms in GVHD and GVL: direct cytolytic action is required for GVL but not for GVHD. If these noncytolytic pathways can be inhibited, then GVHD might be ameliorated while preserving GVL.
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2

de la Calle, Claire M., Sarah A. Holzman, Umer Sheikh, Jonathan H. Huang, Haydn T. Kissick, Adeboya O. Osunkoya, Brian P. Pollack, Dattatraya Patil, Kenneth Ogan, and Viraj A. Master. "Evaluation of major histocompatibility complex class I expression in clear cell renal cell carcinoma as a prognostic tool." Journal of Clinical Oncology 33, no. 7_suppl (March 1, 2015): 469. http://dx.doi.org/10.1200/jco.2015.33.7_suppl.469.

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469 Background: After nephrectomy for clear cell renal cell carcinoma (ccRCC) approximately one-third of patients develop metastases. Yet, with currently used prognostic tools such as the TNM staging and the Fuhrman nuclear grade (FNG) system, it is difficult to accurately assess prognosis for each patient. Here, we evaluated Major Histocompatibility Complex Class I (MHCI) expression as a potential prognostic immune marker in ccRCC. Methods: Fifty-five post-nephrectomy patients that presented with localized ccRCC were included. All patients had four or more years of follow up. MHCI was stained in the tumor sections via immunohistochemistry. Then, via an automated image analysis algorithm MHCI expression was quantitated with the Positivity score, the ratio of positively stained pixels over the total number of pixels. Results: Mean MHCI positivity score of the cohort was 0.75 (SE= ±0.20). At the end of the follow-up period, the patients who were alive had higher MHCI expression (0.80 positivity score; SE ±0.14) than those who died of disease (0.62 positivity score; SE= ±0.16; t test, p<0.0001). MHCI positivity scores above the mean were associated with increased cancer specific survival (Mantel-Cox, p=0.0021). MHCI expression was higher among patients with no recurrence (0.80; SE= ±0.16) compared to those that recurred during the study period (0.70; SE= ±0.22; t test, p=0.017); and time-to-recurrence was longer in patients with above mean MHCI positivity scores (Mantel-Cox, p=0.017). Patients who were alive with recurrence had increased MHCI expression (0.81; SE= ±0.10) compared to those who succumbed to disease recurrence (0.62; SE= ±0.25; t-test, p=0.0009). No correlation was detected between FNG and tumor expression of MHCI (ANOVA, p=0.655, F=0.423) or between stage at presentation and MHCI tumor expression (ANOVA, p=0.734, F=0.311). Conclusions: With an automated high-throughput image analysis, this cohort shows that increased MHCI expression in ccRCC is associated with improved prognosis after curative nephrectomy.
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3

Master, Viraj A., Sarah Holzman, Brian Pollack, and Adeboya O. Osunkoya. "Major histocompatibility complex class I (MHC 1) expression in clear cell renal cell carcinoma: Correlation with clinical outcome." Journal of Clinical Oncology 32, no. 4_suppl (February 1, 2014): 541. http://dx.doi.org/10.1200/jco.2014.32.4_suppl.541.

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541 Background: Most patients with clear cell renal cell carcinoma (ccRCC) initially present with localized disease but a fraction subsequently develop metastases. Current predictive models of ccRCC recurrence are imperfect, suggesting a need for additional predictors. Metastatic ccRCC may be modulated by the immune system, suggesting that the immune system plays a role in tumor progression. Major histocompatibility complex class I (MHC I) expression on tumor cells is critical for immune system recognition. Here, we analyzed MHC I expression in ccRCC and its correlation with clinical outcomes. Methods: ccRCC patients who underwent radical nephrectomy with a ≥4 years of follow-up, without T4 disease or metastasis at presentation were included. All slides were re-reviewed by a single Urologic Pathologist and blocks with tumor and adjacent renal parenchyma were selected for each case for immunohistochemical staining for MHC I . Whole slide scanning and automated image analysis was used; representative areas of tumor and normal kidney were selected and averaged with Aperio image analysis software (positive pixel count v. 9). Unpaired t-test and one-way ANOVA were performed in GraphPad Prism. Results: 34 patients were analyzed. Fuhrman nuclear grades (FNG) were: FNG 2 10/34 (29%), FNG 3 20/34 (59%) and FNG 4 4/34 (11%). Although there was no correlation with FNG and MHC1 (ANOVA, p=0.800), patients who were alive at follow up had increased MHCI expression (80.1% average positivity score) than those who died (53% average positivity score; t-test, p<0.0001). Patients living with recurrence had increased MHCI expression (81.3% positivity score) compared to those who succumbed to their disease (53.2% positivity score; t-test, p<0.0001). Conclusions: MHCI expression may be an important prognostic factor in ccRCC for recurrence free survival, and also for prognosis of those patients with recurrence. This is the first study to show that increased MHCI expression is a favorable prognostic indicator in metastatic ccRCC. These results suggest that MHCI expression plays an important role in tumor-host immune system interaction of ccRCC and merits further study.
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4

Holzman, Sarah A., Claire M. de la Calle, Haydn T. Kissick, Adeboye O. Osunkoya, Brian P. Pollack, Dattatraya Patil, Kenneth Ogan, and Viraj A. Master. "High Expression of Major Histocompatibility Complex Class I in Clear Cell Renal Cell Carcinoma Is Associated with Improved Prognosis." Urologia Internationalis 95, no. 1 (2015): 72–78. http://dx.doi.org/10.1159/000370164.

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Introduction: In this study we analyzed major histocompatibility complex class I (MHCI) expression as a potential prognostic immune marker for patients with clear cell renal cell carcinoma (ccRCC). Patients and Methods: 34 patients with localized ccRCC (pT1-pT3) who had undergone nephrectomy and had at least 4 years of clinical follow-up data were included in the study. Immunohistochemical staining for MHCI was performed on tumor sections. An automated image analysis algorithm was applied to representative tumor areas to quantitate the proportion of stained pixels (positivity score = positive pixels/total pixels) on scanned digital slides. Results: At the end of the study, the patients who were alive had increased MHCI expression (mean positivity score 0.80) compared to those who died of the disease (mean positivity score 0.53; p < 0.0001, t test). Patients who were alive with recurrence had increased MHCI expression (positivity score 0.81) compared to those who succumbed to their disease recurrence (positivity score 0.53; p < 0.0001, t test). Survival was higher among patients with high MHCI expression compared to patients with low MHCI expression (p < 0.0001, Mantel-Cox). Conclusions: With an automated high-throughput image analysis technique, this study shows that higher tumor cell MHCI expression promotes increased survival and reduced incidence of recurrence compared to patients with lower tumor cell MHCI expression.
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5

Mavridis, George, Richa Arya, Alexander Domnick, Jerome Zoidakis, Manousos Makridakis, Antonia Vlahou, Anastasia Mpakali, et al. "A systematic re-examination of processing of MHCI-bound antigenic peptide precursors by endoplasmic reticulum aminopeptidase 1." Journal of Biological Chemistry 295, no. 21 (March 17, 2020): 7193–210. http://dx.doi.org/10.1074/jbc.ra120.012976.

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Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims antigenic peptide precursors to generate mature antigenic peptides for presentation by major histocompatibility complex class I (MHCI) molecules and regulates adaptive immune responses. ERAP1 has been proposed to trim peptide precursors both in solution and in preformed MHCI-peptide complexes, but which mode is more relevant to its biological function remains controversial. Here, we compared ERAP1-mediated trimming of antigenic peptide precursors in solution or when bound to three MHCI alleles, HLA-B*58, HLA-B*08, and HLA-A*02. For all MHCI-peptide combinations, peptide binding onto MHCI protected against ERAP1-mediated trimming. In only a single MHCI-peptide combination, trimming of an HLA-B*08-bound 12-mer progressed at a considerable rate, albeit still slower than in solution. Results from thermodynamic, kinetic, and computational analyses suggested that this 12-mer is highly labile and that apparent on-MHC trimming rates are always slower than that of MHCI-peptide dissociation. Both ERAP2 and leucine aminopeptidase, an enzyme unrelated to antigen processing, could trim this labile peptide from preformed MHCI complexes as efficiently as ERAP1. A pseudopeptide analogue with high affinity for both HLA-B*08 and the ERAP1 active site could not promote the formation of a ternary ERAP1/MHCI/peptide complex. Similarly, no interactions between ERAP1 and purified peptide-loading complex were detected in the absence or presence of a pseudopeptide trap. We conclude that MHCI binding protects peptides from ERAP1 degradation and that trimming in solution along with the dynamic nature of peptide binding to MHCI are sufficient to explain ERAP1 processing of antigenic peptide precursors.
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6

Lilley, Brendan N., Domenico Tortorella, and Hidde L. Ploegh. "Dislocation of a Type I Membrane Protein Requires Interactions between Membrane-spanning Segments within the Lipid Bilayer." Molecular Biology of the Cell 14, no. 9 (September 2003): 3690–98. http://dx.doi.org/10.1091/mbc.e03-03-0192.

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The human cytomegalovirus gene product US11 causes rapid degradation of class I major histocompatibility complex (MHCI) heavy chains by inducing their dislocation from the endoplasmic reticulum (ER) and subsequent degradation by the proteasome. This set of reactions resembles the endogenous cellular quality control pathway that removes misfolded or unassembled proteins from the ER. We show that the transmembrane domain (TMD) of US11 is essential for MHCI heavy chain dislocation, but dispensable for MHCI binding. A Gln residue at position 192 in the US11 TMD is crucial for the ubiquitination and degradation of MHCI heavy chains. Cells that express US11 TMD mutants allow formation of MHCI-β2m complexes, but their rate of egress from the ER is significantly impaired. Further mutagenesis data are consistent with the presence of an alpha-helical structure in the US11 TMD essential for MHCI heavy chain dislocation. The failure of US11 TMD mutants to catalyze dislocation is a unique instance in which a polar residue in the TMD of a type I membrane protein is required for that protein's function. Targeting of MHCI heavy chains for dislocation by US11 thus requires the formation of interhelical hydrogen bonds within the ER membrane.
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7

Weigert, Roberto, Albert Chi Yeung, Jean Li, and Julie G. Donaldson. "Rab22a Regulates the Recycling of Membrane Proteins Internalized Independently of Clathrin." Molecular Biology of the Cell 15, no. 8 (August 2004): 3758–70. http://dx.doi.org/10.1091/mbc.e04-04-0342.

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Plasma membrane proteins that are internalized independently of clathrin, such as major histocompatibility complex class I (MHCI), are internalized in vesicles that fuse with the early endosomes containing clathrin-derived cargo. From there, MHCI is either transported to the late endosome for degradation or is recycled back to the plasma membrane via tubular structures that lack clathrin-dependent recycling cargo, e.g., transferrin. Here, we show that the small GTPase Rab22a is associated with these tubular recycling intermediates containing MHCI. Expression of a dominant negative mutant of Rab22a or small interfering RNA-mediated depletion of Rab22a inhibited both formation of the recycling tubules and MHCI recycling. By contrast, cells expressing the constitutively active mutant of Rab22a exhibited prominent recycling tubules and accumulated vesicles at the periphery, but MHCI recycling was still blocked. These results suggest that Rab22a activation is required for tubule formation and Rab22a inactivation for final fusion of recycling membranes with the surface. The trafficking of transferrin was only modestly affected by these treatments. Dominant negative mutant of Rab11a also inhibited recycling of MHCI but not the formation of recycling tubules, suggesting that Rab22a and Rab11a might coordinate different steps of MHCI recycling.
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8

Clement, Mathew, Lea Knezevic, Tamsin Dockree, James E. McLaren, Kristin Ladell, Kelly L. Miners, Sian Llewellyn-Lacey, et al. "CD8 coreceptor-mediated focusing can reorder the agonist hierarchy of peptide ligands recognized via the T cell receptor." Proceedings of the National Academy of Sciences 118, no. 29 (July 16, 2021): e2019639118. http://dx.doi.org/10.1073/pnas.2019639118.

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CD8+ T cells are inherently cross-reactive and recognize numerous peptide antigens in the context of a given major histocompatibility complex class I (MHCI) molecule via the clonotypically expressed T cell receptor (TCR). The lineally expressed coreceptor CD8 interacts coordinately with MHCI at a distinct and largely invariant site to slow the TCR/peptide-MHCI (pMHCI) dissociation rate and enhance antigen sensitivity. However, this biological effect is not necessarily uniform, and theoretical models suggest that antigen sensitivity can be modulated in a differential manner by CD8. We used two intrinsically controlled systems to determine how the relationship between the TCR/pMHCI interaction and the pMHCI/CD8 interaction affects the functional sensitivity of antigen recognition. Our data show that modulation of the pMHCI/CD8 interaction can reorder the agonist hierarchy of peptide ligands across a spectrum of affinities for the TCR.
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9

Pommier, Arnaud, Naishitha Anaparthy, Nicoletta Memos, Z. Larkin Kelley, Alizée Gouronnec, Ran Yan, Cédric Auffray, et al. "Unresolved endoplasmic reticulum stress engenders immune-resistant, latent pancreatic cancer metastases." Science 360, no. 6394 (May 17, 2018): eaao4908. http://dx.doi.org/10.1126/science.aao4908.

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The majority of patients with pancreatic ductal adenocarcinoma (PDA) develop metastatic disease after resection of their primary tumor. We found that livers from patients and mice with PDA harbor single disseminated cancer cells (DCCs) lacking expression of cytokeratin 19 (CK19) and major histocompatibility complex class I (MHCI). We created a mouse model to determine how these DCCs develop. Intraportal injection of immunogenic PDA cells into preimmunized mice seeded livers only with single, nonreplicating DCCs that were CK19– and MHCI–. The DCCs exhibited an endoplasmic reticulum (ER) stress response but paradoxically lacked both inositol-requiring enzyme 1α activation and expression of the spliced form of transcription factor XBP1 (XBP1s). Inducible expression of XBP1s in DCCs, in combination with T cell depletion, stimulated the outgrowth of macrometastatic lesions that expressed CK19 and MHCI. Thus, unresolved ER stress enables DCCs to escape immunity and establish latent metastases.
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10

Parrish, Heather L., Neha R. Deshpande, Jelena Vasic, and Michael S. Kuhns. "Functional evidence for TCR-intrinsic specificity for MHCII." Proceedings of the National Academy of Sciences 113, no. 11 (February 1, 2016): 3000–3005. http://dx.doi.org/10.1073/pnas.1518499113.

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How T cells become restricted to binding antigenic peptides within class I or class II major histocompatibility complex molecules (pMHCI or pMHCII, respectively) via clonotypic T-cell receptors (TCRs) remains debated. During development, if TCR–pMHC interactions exceed an affinity threshold, a signal is generated that positively selects the thymocyte to become a mature CD4+ or CD8+ T cell that can recognize foreign peptides within MHCII or MHCI, respectively. But whether TCRs possess an intrinsic, subthreshold specificity for MHC that facilitates sampling of the peptides within MHC during positive selection or T-cell activation is undefined. Here we asked if increasing the frequency of lymphocyte-specific protein tyrosine kinase (Lck)-associated CD4 molecules in T-cell hybridomas would allow for the detection of subthreshold TCR–MHC interactions. The reactivity of 10 distinct TCRs was assessed in response to selecting and nonselecting MHCII bearing cognate, null, or “shaved” peptides with alanine substitutions at known TCR contact residues: Three of the TCRs were selected on MHCII and have defined peptide specificity, two were selected on MHCI and have a known pMHC specificity, and five were generated in vitro without defined selecting or cognate pMHC. Our central finding is that IL-2 was made when each TCR interacted with selecting or nonselecting MHCII presenting shaved peptides. These responses were abrogated by anti-CD4 antibodies and mutagenesis of CD4. They were also inhibited by anti-MHC antibodies that block TCR–MHCII interactions. We interpret these data as functional evidence for TCR-intrinsic specificity for MHCII.
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11

Naslavsky, Naava, Roberto Weigert, and Julie G. Donaldson. "Convergence of Non-clathrin- and Clathrin-derived Endosomes Involves Arf6 Inactivation and Changes in Phosphoinositides." Molecular Biology of the Cell 14, no. 2 (February 2003): 417–31. http://dx.doi.org/10.1091/mbc.02-04-0053.

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The trafficking of two plasma membrane (PM) proteins that lack clathrin internalization sequences, major histocompatibility complex class I (MHCI), and interleukin 2 receptor α subunit (Tac) was compared with that of PM proteins internalized via clathrin. MHCI and Tac were internalized into endosomes that were distinct from those containing clathrin cargo. At later times, a fraction of these internalized membranes were observed in Arf6-associated, tubular recycling endosomes whereas another fraction acquired early endosomal autoantigen 1 (EEA1) before fusion with the “classical” early endosomes containing the clathrin-dependent cargo, LDL. After convergence, cargo molecules from both pathways eventually arrived, in a Rab7-dependent manner, at late endosomes and were degraded. Expression of a constitutively active mutant of Arf6, Q67L, caused MHCI and Tac to accumulate in enlarged PIP2-enriched vacuoles, devoid of EEA1 and inhibited their fusion with clathrin cargo-containing endosomes and hence blocked degradation. By contrast, trafficking and degradation of clathrin-cargo was not affected. A similar block in transport of MHCI and Tac was reversibly induced by a PI3-kinase inhibitor, implying that inactivation of Arf6 and acquisition of PI3P are required for convergence of endosomes arising from these two pathways.
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12

Eken, Ahmet, Vivian Ortiz, and Jack R. Wands. "Ethanol Inhibits Antigen Presentation by Dendritic Cells." Clinical and Vaccine Immunology 18, no. 7 (May 11, 2011): 1157–66. http://dx.doi.org/10.1128/cvi.05029-11.

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ABSTRACTPrevious studies suggest that altered virus-specific T-cell responses observed during chronic ethanol exposure may be due to abnormal functioning of dendritic cells (DCs). Here we explored the effects of ethanol on exogenous antigen presentation by DCs. BALB/c, C57BL/6, and CBA/caj mice were fed ethanol or an isocaloric control diet for 8 weeks. The splenic DC population was expanded using an Flt3L expression plasmid via tail vein injection. DCs were purified and assessed for antigen presentation and processing and for peptide-major histocompatibility complex class I and II (MHCI and MHCII) formation on the cell surface. Interleukin-2 (IL-2) was measured as an indicator of antigen-specific T-cell activation by DCs in coculture. Antigen processing and peptide-MHCII complexes were evaluated by flow cytometry. We observed that ethanol not only suppressed allogeneic peptide presentation to T cells by DCs but also altered presentation of exogenous ovalbumin (OVA) peptide 323-339 to an OVA-specific DO11 T-cell line as well as to OVA-sensitized primary T cells. Smaller amounts of peptide-MHCII complexes were found on the DCs isolated from the spleens of ethanol-fed mice. In contrast to MHCII presentation, cross-presentation of exogenous OVA peptide via MHCI by DCs remained intact. More importantly, ethanol-exposed DCs had reduced B7-DC and enhanced ICOS-L (inhibitory) costimulatory molecule expression. Ethanol inhibits exogenous and allogeneic antigen presentation and affects the formation of peptide-MHCII complexes, as well as altering costimulatory molecule expression on the cell surface. Therefore, DC presentation of peptides in a favorable costimulatory protein environment is required to subsequently activate T cells and appears to be a critical target for the immunosuppressive effects of ethanol.
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13

Warre-Cornish, Katherine, Leo Perfect, Roland Nagy, Rodrigo R. R. Duarte, Matthew J. Reid, Pooja Raval, Annett Mueller, et al. "Interferon-γ signaling in human iPSC–derived neurons recapitulates neurodevelopmental disorder phenotypes." Science Advances 6, no. 34 (August 2020): eaay9506. http://dx.doi.org/10.1126/sciadv.aay9506.

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Maternal immune activation increases the risk of neurodevelopmental disorders. Elevated cytokines, such as interferon-γ (IFN-γ), in offspring’s brains play a central role. IFN-γ activates an antiviral cellular state, limiting viral entry and replication. Moreover, IFN-γ is implicated in brain development. We tested the hypothesis that IFN-γ signaling contributes to molecular and cellular phenotypes associated with neurodevelopmental disorders. Transient IFN-γ treatment of neural progenitors derived from human induced pluripotent stem cells increased neurite outgrowth. RNA sequencing analysis revealed that major histocompatibility complex class I (MHCI) genes were persistently up-regulated through neuronal differentiation—an effect that was mediated by IFN-γ-induced promyelocytic leukemia protein (PML) nuclear bodies. Critically, IFN-γ-induced neurite outgrowth required both PML and MHCI. We also found evidence that IFN-γ disproportionately altered the expression of genes associated with schizophrenia and autism, suggesting convergence between genetic and environmental risk factors. Together, these data implicate IFN-γ signaling in neurodevelopmental disorder etiology.
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14

Piskurich, Janet F., and Vladimir I. Mayorov. "B Lymphocyte-Induced Maturation Protein-1/Positive Regulatory Domain I-Binding Factor 1 regulates two amino peptidases associated with antigen processing (78.9)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 78.9. http://dx.doi.org/10.4049/jimmunol.182.supp.78.9.

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Abstract A diverse repertoire of specifically-trimmed peptides is presented by the Major Histocompatibility Complex Class I (MHCI) pathway of antigen presentation for immune surveillance by CD8+ cytotoxic T cells. These peptides are generated in the cytosol, then trimmed by amino peptidases to meet the binding requirements of MHCI. Two endoplasmic reticulum amino peptidases, ERAP1 and ERAP2, perform this function in human cells. Positive Regulatory Domain I-Binding Factor 1 (PRDI-BF1) called B Lymphocyte Induced Maturation Protein-1 (BLIMP-1) in mice drives the differentiation of B lymphocytes into plasma cells. We demonstrated that PRDI-BF1/BLIMP-1 regulates the MHCII pathway of antigen presentation by repressing MHC class II transactivator (CIITA) transcription. We now show that PRDI-BF1/BLIMP-1 plays a key role in modulating the MHCI pathway. Functional promoter analyses and protein/DNA binding studies demonstrate that both full-length PRDI-BF1/BLIMP-1 and a truncated form of this transcription factor called PRDI-BF1β, expressed in myeloma cells and associated with resistance to chemotherapy in diffuse large B-cell and T-cell lymphoma, mediate repression of ERAP1 and ERAP2. Repression occurs through a site nearly identical in sequence to a site for repression of CIITA. IFN-γ or ectopic expression of IRF-1 up regulates ERAP expression even in PRDI-BF1/BLIMP-1-expressing cells. The goal of this work is to uncover pathways useful in therapeutic approaches to improve the ability of the immune system to recognize and destroy PRDI-BF1-expressing tumors. Supported by grants from the National Cancer Institute (RO1CA102203) and MEDCEN Community Health Foundation of Central Georgia.
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Wang, Yang, Tomasz Sosinowski, Andrey Novikov, Frances Crawford, Janice White, Niyun Jin, Zikou Liu, et al. "How C-terminal additions to insulin B-chain fragments create superagonists for T cells in mouse and human type 1 diabetes." Science Immunology 4, no. 34 (April 5, 2019): eaav7517. http://dx.doi.org/10.1126/sciimmunol.aav7517.

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In type 1 diabetes (T1D), proinsulin is a major autoantigen and the insulin B:9-23 peptide contains epitopes for CD4+ T cells in both mice and humans. This peptide requires carboxyl-terminal mutations for uniform binding in the proper position within the mouse IAg7 or human DQ8 major histocompatibility complex (MHC) class II (MHCII) peptide grooves and for strong CD4+ T cell stimulation. Here, we present crystal structures showing how these mutations control CD4+ T cell receptor (TCR) binding to these MHCII-peptide complexes. Our data reveal stricking similarities between mouse and human CD4+ TCRs in their interactions with these ligands. We also show how fusions between fragments of B:9-23 and of proinsulin C-peptide create chimeric peptides with activities as strong or stronger than the mutated insulin peptides. We propose transpeptidation in the lysosome as a mechanism that could accomplish these fusions in vivo, similar to the creation of fused peptide epitopes for MHCI presentation shown to occur by transpeptidation in the proteasome. Were this mechanism limited to the pancreas and absent in the thymus, it could provide an explanation for how diabetogenic T cells escape negative selection during development but find their modified target antigens in the pancreas to cause T1D.
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16

Ujvari, Beata, and Katherine Belov. "Major Histocompatibility Complex (MHC) Markers in Conservation Biology." International Journal of Molecular Sciences 12, no. 8 (August 15, 2011): 5168–86. http://dx.doi.org/10.3390/ijms12085168.

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17

Farag, M. A., A.-H. Saad, A. F. Wahby, and R. El Ridi. "The major histocompatibility complex (MHC) of the snake,." Developmental & Comparative Immunology 10, no. 1 (December 1986): 96. http://dx.doi.org/10.1016/0145-305x(86)90050-9.

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18

Constantin, Carolyn M., Elizabeth E. Bonney, John D. Altman, and Ora L. Strickland. "Major Histocompatibility Complex (MHC) Tetramer Technology: An Evaluation." Biological Research For Nursing 4, no. 2 (October 2002): 115–27. http://dx.doi.org/10.1177/1099800402238332.

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Single-cell assays are currently favored to quantitate T-cell responses. Staining antigen-specific T-cells with fluorescently labeled tetrameric major histocompatibility complex (MHC)/peptide complexes has greatly enhanced the ability to assess the cellular dynamics of an immune response at the single-cell level.This article reviews MHC tetramer technology, defining it, discussing how MHC tetramers are made, outlining the benefits of this technology, comparing and contrasting it to other methods for evaluating immune responses, and describing current applications.
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19

Zhu, Jie, Rama Madhurapantula, Aruna Kalyanasundaram, Tanya Sabharwal, Olga Antipova, Sandra Bishnoi, and Joseph Orgel. "Ultrastructural Location and Interactions of the Immunoglobulin Receptor Binding Sequence within Fibrillar Type I Collagen." International Journal of Molecular Sciences 21, no. 11 (June 11, 2020): 4166. http://dx.doi.org/10.3390/ijms21114166.

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Collagen type I is a major constituent of animal bodies. It is found in large quantities in tendon, bone, skin, cartilage, blood vessels, bronchi, and the lung interstitium. It is also produced and accumulates in large amounts in response to certain inflammations such as lung fibrosis. Our understanding of the molecular organization of fibrillar collagen and cellular interaction motifs, such as those involved with immune-associated molecules, continues to be refined. In this study, antibodies raised against type I collagen were used to label intact D-periodic type I collagen fibrils and observed with atomic force microscopy (AFM), and X-ray diffraction (XRD) and immunolabeling positions were observed with both methods. The antibodies bind close to the C-terminal telopeptide which verifies the location and accessibility of both the major histocompatibility complex (MHC) class I (MHCI) binding domain and C-terminal telopeptide on the outside of the collagen fibril. The close proximity of the C-telopeptide and the MHC1 domain of type I collagen to fibronectin, discoidin domain receptor (DDR), and collagenase cleavage domains likely facilitate the interaction of ligands and receptors related to cellular immunity and the collagen-based Extracellular Matrix.
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Radaelli, E., F. Del Piero, L. Aresu, F. Sciarrone, N. Vicari, S. Mattiello, S. Tagliabue, M. Fabbi, and E. Scanziani. "Expression of Major Histocompatibility Complex Class II Antigens in Porcine Leptospiral Nephritis." Veterinary Pathology 46, no. 5 (January 29, 2009): 800–809. http://dx.doi.org/10.1354/vp.08-vp-0078-r-fl.

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Class II major histocompatibility complex (MHCII) is required for the presentation of antigens to CD4 helper T cells. During nephritis, not only primary antigen presenting cells such as histiocytes and lymphocytes, but also cytokine-stimulated tubular epithelial cells express MHCII. Leptospirosis in fattening pigs is characterized by several degrees of nephritis, from absence of lesions to severe multifocal tubulo-interstitial inflammation. Renal tissue from 20 8-month-old pigs with spontaneous nephritis and 6 control pigs without renal lesions were investigated for leptospirosis by indirect immunohistochemistry (IHC) and polymerase chain reaction (PCR). IHC for MHCII also was performed on renal samples. Serum samples were tested for different serovars of Leptospira interrogans. Control pigs were free of interstitial nephritis and negative for leptospirosis by all tests. In pigs with nephritis, serology was positive for serovar Pomona in 19/20 pigs. In 16 of these 19 pigs, leptospiral renal infection was confirmed by PCR and/or indirect IHC. Nephritic lesions were classified histologically into perivascular lymphocytic (4 pigs), lymphofollicular (6 pigs), lymphohistiocytic (8 pigs), and neutrophilic (2 pigs) pattern. MHCII expression by histiocytes and lymphocytes was observed in all lesions. Prominent MHCII expression in regenerating tubular epithelium was observed in lymphofollicular and lymphohistiocytic nephritis. No tubular colocalization between leptospiral and MHCII antigen was observed. Results suggest that during leptospiral nephritis, MHCII contributes to the intensity of the inflammatory response. Furthermore de novo MHCII expression in regenerating tubules may play a role in the defence mechanism against leptospiral tubular colonization.
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Eyster, Craig A., Nelson B. Cole, Shariska Petersen, Kasinath Viswanathan, Klaus Früh, and Julie G. Donaldson. "MARCH ubiquitin ligases alter the itinerary of clathrin-independent cargo from recycling to degradation." Molecular Biology of the Cell 22, no. 17 (September 2011): 3218–30. http://dx.doi.org/10.1091/mbc.e10-11-0874.

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Following endocytosis, internalized plasma membrane proteins can be recycled back to the cell surface or trafficked to late endosomes/lysosomes for degradation. Here we report on the trafficking of multiple proteins that enter cells by clathrin-independent endocytosis (CIE) and determine that a set of proteins (CD44, CD98, and CD147) found primarily in recycling tubules largely failed to reach late endosomes in HeLa cells, whereas other CIE cargo proteins, including major histocompatibility complex class I protein (MHCI), trafficked to both early endosome antigen 1 (EEA1) and late endosomal compartments in addition to recycling tubules. Expression of the membrane-associated RING-CH 8 (MARCH8) E3 ubiquitin ligase completely shifted the trafficking of CD44 and CD98 proteins away from recycling tubules to EEA1 compartments and late endosomes, resulting in reduced surface levels. Cargo affected by MARCH expression, including CD44, CD98, and MHCI, still entered cells by CIE, suggesting that the routing of ubiquitinated cargo occurs after endocytosis. MARCH8 expression led to direct ubiquitination of CD98 and routing of CD98 to late endosomes/lysosomes.
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KENNEDY, P. G. E., and J. GAIRNS. "Major histocompatibility complex (MHC) antigen expression in HIV encephalitis." Neuropathology and Applied Neurobiology 18, no. 5 (October 1992): 515–22. http://dx.doi.org/10.1111/j.1365-2990.1992.tb00818.x.

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Nonaka, Masaru, Kiyoshi Naruse, Megumi Matsuo, and Akihiro Shima. "Comparative Genomics of Medaka: The Major Histocompatibility Complex (MHC)." Marine Biotechnology 3 (November 1, 2001): S141—S144. http://dx.doi.org/10.1007/s10126-001-0035-0.

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Liang, Chunguang, Elena Bencurova, Eric Psota, Priya Neurgaonkar, Martina Prelog, Carsten Scheller, and Thomas Dandekar. "Population-Predicted MHC Class II Epitope Presentation of SARS-CoV-2 Structural Proteins Correlates to the Case Fatality Rates of COVID-19 in Different Countries." International Journal of Molecular Sciences 22, no. 5 (March 5, 2021): 2630. http://dx.doi.org/10.3390/ijms22052630.

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We observed substantial differences in predicted Major Histocompatibility Complex II (MHCII) epitope presentation of SARS-CoV-2 proteins for different populations but only minor differences in predicted MHCI epitope presentation. A comparison of this predicted epitope MHC-coverage revealed for the early phase of infection spread (till day 15 after reaching 128 observed infection cases) highly significant negative correlations with the case fatality rate. Specifically, this was observed in different populations for MHC class II presentation of the viral spike protein (p-value: 0.0733 for linear regression), the envelope protein (p-value: 0.023), and the membrane protein (p-value: 0.00053), indicating that the high case fatality rates of COVID-19 observed in some countries seem to be related with poor MHC class II presentation and hence weak adaptive immune response against these viral envelope proteins. Our results highlight the general importance of the SARS-CoV-2 structural proteins in immunological control in early infection spread looking at a global census in various countries and taking case fatality rate into account. Other factors such as health system and control measures become more important after the early spread. Our study should encourage further studies on MHCII alleles as potential risk factors in COVID-19 including assessment of local populations and specific allele distributions.
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Castro, Michael, Bence Sipos, Natalia Pieper, and Saskia Biskup. "Major histocompatibility complex class 1 (MHC1) loss among patients with glioblastoma (GBM)." Journal of Clinical Oncology 38, no. 15_suppl (May 20, 2020): e14523-e14523. http://dx.doi.org/10.1200/jco.2020.38.15_suppl.e14523.

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e14523 Background: Immune evasion represents a hallmark behavior of cancer and may occur through many mechanisms. Among these, intact tumor antigen presentation at the cell surface is a fundamental prerequisite to achieving successful adaptive immunotherapy. The loss of MHC1 expression due to molecular events, including mutation, deletion, or epigenetic silencing of B2M is commonly acquired during immunotherapy. On the other hand, molecular events affecting antigen presentation machinery may be present prior to immunotherapy administration. Among these, TP53 mutations causing loss of ERAP1 and TAP1 expression compromise transport of MHC1 molecules from the endoplasmic reticulum to the cell surface and mutant peptide integration into the HLA context resulting in absent antigen presentation. Thus far, clinical trials of PD-1/L1 agents have failed to demonstrate a benefit for GBM patients and responses are seen only among a minority. Hence, we set out to assess the integrity of MHC1 expression by using immunohistochemistry. Methods: Immunohistochemical (IHC) stains for HLA, B and C were developed and validated with internal controls. Staining intensity and location (membrane-bound or cytoplasmic) was evaluated semi-quantitatively. The first 10 consecutive patients with GBM who were referred for neoepitope vaccine were evaluated. Results: Absent staining was seen among 6/10, negligible, or faint staining was present in 2, and only 2 tumors demonstrated intact membrane-bound expression. Conclusions: In addition to low tumor mutation burden and an immunosuppressive tumor microenvironment, MHC1 loss is a frequent event among patients with GBM, and may be a dominant cause of immunotherapy failure for as many as 80% of patients. Thus, development of strategies to reverse this loss may be an essential component of successful adaptive immunotherapy for this disease. These data suggest that routine assessment of MHC1 should become a component of eligibility checking for GBM patients being considered for an MHC-restricted approaches. [Table: see text]
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Nakayama, Masafumi, Arisa Hori, Saori Toyoura, and Shin-Ichiro Yamaguchi. "Shaping of T Cell Functions by Trogocytosis." Cells 10, no. 5 (May 10, 2021): 1155. http://dx.doi.org/10.3390/cells10051155.

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Trogocytosis is an active process whereby plasma membrane proteins are transferred from one cell to the other cell in a cell-cell contact-dependent manner. Since the discovery of the intercellular transfer of major histocompatibility complex (MHC) molecules in the 1970s, trogocytosis of MHC molecules between various immune cells has been frequently observed. For instance, antigen-presenting cells (APCs) acquire MHC class I (MHCI) from allografts, tumors, and virally infected cells, and these APCs are subsequently able to prime CD8+ T cells without antigen processing via the preformed antigen-MHCI complexes, in a process called cross-dressing. T cells also acquire MHC molecules from APCs or other target cells via the immunological synapse formed at the cell-cell contact area, and this phenomenon impacts T cell activation. Compared with naïve and effector T cells, T regulatory cells have increased trogocytosis activity in order to remove MHC class II and costimulatory molecules from APCs, resulting in the induction of tolerance. Accumulating evidence suggests that trogocytosis shapes T cell functions in cancer, transplantation, and during microbial infections. In this review, we focus on T cell trogocytosis and the related inflammatory diseases.
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Wooldridge, Linda, Emily Edwards, Julia Ekeruche, John Miles, Hugo van den Berg, Mathew Clement, and Andrew Sewell. "Combinatorial peptide library scans of multiple HLA A*0201 restricted CTL reveal high levels of degeneracy at MHCI anchor positions (100.12)." Journal of Immunology 186, no. 1_Supplement (April 1, 2011): 100.12. http://dx.doi.org/10.4049/jimmunol.186.supp.100.12.

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Abstract CD8+ cytotoxic T lymphocytes (CTLs) hold the key to the successful prevention and eradication of infectious and neoplastic disease. T-cells recognize ‘foreign’ peptide fragments often referred to as epitopes, in the context of ‘self’ major histocompatibility complex class I (MHCI) molecules. Epitope identification is essential to define targets for the effective control of disease. Peptides bind to MHCI molecules by anchoring at position 2 and the C-terminus of the peptide ligand. Techniques such as pool sequencing have been hugely instrumental in revealing HLA allele-specific peptide binding motifs. However, this approach only reveals the most dominant MHC anchor residues. The preferred binding motif identified by pool sequencing for the most common MHCI, HLA A*0201, is L/M at position 2 and V/I/L/A at the C-terminus. Here, we use an extremely sensitive combinatorial library screening approach to show that in the context of HLA A*0201, degeneracy at anchor residue positions is much higher than previously appreciated. We also examined the recognition of peptides with substitutions of all 20 amino acids at both anchor positions in three different clonal systems which confirm these observations. Indeed, in one clonal system, 9-mer peptides containing A, C, F, I, K, L, M, Q, S, T, V in position 2 and A, C, F, I, L, M, T, V at position 9 were recognized efficiently. These observations have implications for T-cell epitope prediction and future vaccine design.
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Jung, Kie-Chul, Md Rashedul Hoque, Dong-Won Seo, Byung-Kwon Park, Kang-Duk Choi, and Jun-Heon Lee. "Genotype Analysis of the Major Histocompatibility Complex Region in Korean Native Chicken." Korean Journal of Poultry Science 36, no. 4 (December 31, 2009): 317–22. http://dx.doi.org/10.5536/kjps.2009.36.4.317.

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Yamaguchi and Dijkstra. "Major Histocompatibility Complex (MHC) Genes and Disease Resistance in Fish." Cells 8, no. 4 (April 25, 2019): 378. http://dx.doi.org/10.3390/cells8040378.

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Fascinating about classical major histocompatibility complex (MHC) molecules is their polymorphism. The present study is a review and discussion of the fish MHC situation. The basic pattern of MHC variation in fish is similar to mammals, with MHC class I versus class II, and polymorphic classical versus nonpolymorphic nonclassical. However, in many or all teleost fishes, important differences with mammalian or human MHC were observed: (1) The allelic/haplotype diversification levels of classical MHC class I tend to be much higher than in mammals and involve structural positions within but also outside the peptide binding groove; (2) Teleost fish classical MHC class I and class II loci are not linked. The present article summarizes previous studies that performed quantitative trait loci (QTL) analysis for mapping differences in teleost fish disease resistance, and discusses them from MHC point of view. Overall, those QTL studies suggest the possible importance of genomic regions including classical MHC class II and nonclassical MHC class I genes, whereas similar observations were not made for the genomic regions with the highly diversified classical MHC class I alleles. It must be concluded that despite decades of knowing MHC polymorphism in jawed vertebrate species including fish, firm conclusions (as opposed to appealing hypotheses) on the reasons for MHC polymorphism cannot be made, and that the types of polymorphism observed in fish may not be explained by disease-resistance models alone.
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Caron, Etienne, Daniel J. Kowalewski, Ching Chiek Koh, Theo Sturm, Heiko Schuster, and Ruedi Aebersold. "Analysis of Major Histocompatibility Complex (MHC) Immunopeptidomes Using Mass Spectrometry." Molecular & Cellular Proteomics 14, no. 12 (October 19, 2015): 3105–17. http://dx.doi.org/10.1074/mcp.o115.052431.

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Caron, Etienne, Daniel J. Kowalewski, Ching Chiek Koh, Theo Sturm, Heiko Schuster, and Ruedi Aebersold. "Analysis of Major Histocompatibility Complex (MHC) Immunopeptidomes Using Mass Spectrometry." Molecular & Cellular Proteomics 14, no. 12 (December 2015): 3105–17. http://dx.doi.org/10.1074/mcp.m115.052431.

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32

Margiotta, Azzurra, Dominik M. Frei, Ingrid Hegnes Sendstad, Lennert Janssen, Jacques Neefjes, and Oddmund Bakke. "Invariant chain regulates endosomal fusion and maturation through an interaction with the SNARE Vti1b." Journal of Cell Science 133, no. 19 (September 9, 2020): jcs244624. http://dx.doi.org/10.1242/jcs.244624.

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ABSTRACTThe invariant chain (Ii, also known as CD74) is a multifunctional regulator of adaptive immune responses and is responsible for sorting major histocompatibility complex class I and class II (MHCI and MHCII, respectively) molecules, as well as other Ii-associated molecules, to a specific endosomal pathway. When Ii is expressed, endosomal maturation and proteolytic degradation of proteins are delayed and, in non-antigen presenting cells, the endosomal size increases, but the molecular mechanisms underlying this are not known. We identified that a SNARE, Vti1b, is essential for regulating these Ii-induced effects. Vti1b binds to Ii and is localized at the contact sites of fusing Ii-positive endosomes. Furthermore, truncated Ii lacking the cytoplasmic tail, which is not internalized from the plasma membrane, relocates Vti1b to the plasma membrane. Knockout of Ii in an antigen-presenting cell line was found to speed up endosomal maturation, whereas silencing of Vti1b inhibits the Ii-induced maturation delay. Our results suggest that Ii, by interacting with the SNARE Vti1b in antigen-presenting cells, directs specific Ii-associated SNARE-mediated fusion in the early part of the endosomal pathway that leads to a slower endosomal maturation for efficient antigen processing and MHC antigen loading.
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33

Plaeger-Marshall, Susan, Albert Haas, Loran T. Clement, Janis V. Giorgi, Irvin S. Y. Chen, Shirley G. Quan, Richard A. Gatti, and E. Richard Stiehm. "Interferon-induced expression of class II major histocompatibility antigens in the major histocompatibility complex (MHC) class II deficiency syndrome." Journal of Clinical Immunology 8, no. 4 (July 1988): 285–95. http://dx.doi.org/10.1007/bf00916557.

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34

Dohring, Christian, and Marco Colonna. "Major Histocompatibility Complex (MHC) Class I Recognition by Natural Killer Cells." Critical Reviews™ in Immunology 17, no. 3-4 (1997): 285–99. http://dx.doi.org/10.1615/critrevimmunol.v17.i3-4.20.

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35

Nesse, L. L., G. Paulsen, M. Syed, and G. Ruff. "A Human Major Histocompatibility Complex (MHC) DNA Probe Recognizes Goat Genes." Acta Veterinaria Scandinavica 29, no. 2 (June 1988): 193–98. http://dx.doi.org/10.1186/bf03548370.

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36

Karell, K., N. Klinger, P. Holopainen, A. Levo, and J. Partanen. "Major histocompatibility complex (MHC)- linked microsatellite markers in a founder population." Tissue Antigens 56, no. 1 (July 2000): 45–51. http://dx.doi.org/10.1034/j.1399-0039.2000.560106.x.

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37

Markey, A. C., L. J. Churchill, and D. M. MacDonald. "Altered expression of major histocompatibility complex (MHC) antigens by epidermal tumours." Journal of Cutaneous Pathology 17, no. 2 (April 1990): 65–71. http://dx.doi.org/10.1111/j.1600-0560.1990.tb00058.x.

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38

Wu, Ming-Shiuan, Kenzaburo Tani, Hajime Sugiyama, Hitoshi Hibino, Kiyoko Izawa, Tsuyoshi Tanabe, Yukoh Nakazaki, et al. "MHC (Major Histocompatibility Complex)-DRB Genes and Polymorphisms in Common Marmoset." Journal of Molecular Evolution 51, no. 3 (September 2000): 214–22. http://dx.doi.org/10.1007/s002390010083.

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39

Ogoshi, Kyoji, and Kaichi Isono. "HETEROZYGOTE ADVANTAGE AT MAJOR HISTOCOMPATIBILITY COMPLEX (MHC) MOLECULES AND CANCER RISK." Annals of Cancer Research and Therapy 9, no. 1-2 (2001): 73–86. http://dx.doi.org/10.4993/acrt1992.9.73.

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40

何, 银忠. "The Research of Major Histocompatibility Complex (MHC) Gene in Small Mammals." Bioprocess 06, no. 03 (2016): 48–52. http://dx.doi.org/10.12677/bp.2016.63007.

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41

Stenbjerg, S., and K. Mygind. "MIGRATION INHIBITORY FACTOR (MIF) AND THE HUMAN MAJOR HISTOCOMPATIBILITY COMPLEX (MHC)." Acta Pathologica Microbiologica Scandinavica Section C Immunology 83C, no. 2 (August 15, 2009): 157–64. http://dx.doi.org/10.1111/j.1699-0463.1975.tb01620.x.

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42

BLOOM, S. E., W. E. BRILES, R. W. BRILES, M. E. DELANY, and R. R. DIETERT. "Chromosomal Localization of the Major Histocompatibility (B) Complex (MHC) and Its Expression in Chickens Aneuploid for the Major Histocompatibility Complex/Ribosomal Deoxyribonucleic Acid Microchromosome." Poultry Science 66, no. 5 (May 1987): 782–89. http://dx.doi.org/10.3382/ps.0660782.

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43

SHENG, HU, YANG QUAN CHEN, and TIANSHUANG QIU. "HEAVY-TAILED DISTRIBUTION AND LOCAL LONG MEMORY IN TIME SERIES OF MOLECULAR MOTION ON THE CELL MEMBRANE." Fluctuation and Noise Letters 10, no. 01 (March 2011): 93–119. http://dx.doi.org/10.1142/s0219477511000429.

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The joint presence of heavy-tailed distribution and long memory in time series always leads to certain trouble in correctly obtaining the statistical characteristics for time series modeling. These two properties i.e., heavy-tailed distribution and long memory, cannot be neglected in time series analysis, because the tail thickness of the distribution and long memory property of the time series are critical in characterizing the essence of the resulting natural or man-made phenomenon of the time series. Meanwhile, the fluctuation of the varying local long memory parameter may be used to capture the internal changes which underlie the externally observed phenomenon. Therefore, in this paper, we proposed to use the variance trend, heavy-tailed distribution, long memory, and local long memory characteristics to analyze a time series recorded as in [1] from tracking the jumps of individual molecules on cell membranes. The tracked molecules are Class I major histocompatibility complex (MHCI) expressed on rat hepatoma cells. The analysis results show that the jump time series of molecular motion on the cell membrane obviously has both heavy-tailed distribution and local long memory characteristics. The tail heaviness parameters, long memory parameters, and the local long memory parameters of ten MHCI molecular jump time series are all summarized with tables and figures in the paper. These reported tables and figures are not only interesting but also important in terms of additional novel insights and characterization of the time series under investigation.
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Kim, Hyungsoo, Heejung Kim, Yongmei Feng, Yan Li, Hironari Tamiya, Stefania Tocci, and Ze’ev A. Ronai. "PRMT5 control of cGAS/STING and NLRC5 pathways defines melanoma response to antitumor immunity." Science Translational Medicine 12, no. 551 (July 8, 2020): eaaz5683. http://dx.doi.org/10.1126/scitranslmed.aaz5683.

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Protein arginine methyltransferase 5 (PRMT5) controls diverse cellular processes and is implicated in cancer development and progression. Here, we report an inverse correlation between PRMT5 function and antitumor immunity. PRMT5 expression was associated with an antitumor immune gene signature in human melanoma tissue. Reducing PRMT5 activity antagonized melanoma growth in immunocompetent but not immunocompromised mice. PRMT5 methylation of IFI16 [interferon-γ (IFN-γ)–inducible protein 16] or its murine homolog IFI204, which are components of the cGAS/STING (stimulator of IFN genes) pathway, attenuated cytosolic DNA–induced IFN and chemokine expression in melanoma cells. PRMT5 also inhibited transcription of the gene encoding NLRC5 (nucleotide-binding oligomerization domain-like receptor family caspase recruitment domain containing 5), a protein that promotes the expression of genes implicated in major histocompatibility complex class I (MHCI) antigen presentation. PRMT5 knockdown augmented IFN and chemokine production and increased MHCI abundance in melanoma. Increased expression of IFI204 and NLRC5 was associated with decreased melanoma growth in murine models, and increased expression of IFI16 and NLRC5 correlated with prolonged survival of patients with melanoma. Combination of pharmacological (GSK3326595) or genetic (shRNA) inhibition of PRMT5 with immune checkpoint therapy limited growth of murine melanoma tumors (B16F10 and YUMM1.7) and enhanced therapeutic efficacy, compared with the effect of either treatment alone. Overall, our findings provide a rationale to test PRMT5 inhibitors in immunotherapy-based clinical trials as a means to enhance an antitumor immune response.
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Wooldridge, Linda, Kristin Ladell, David Price, Andrew Sewell, and Mathew Clement. "Anti-CD8 antibodies can trigger T-cell effector function in the absence of TCR engagement and improve pMHCI tetramer staining (113.28)." Journal of Immunology 186, no. 1_Supplement (April 1, 2011): 113.28. http://dx.doi.org/10.4049/jimmunol.186.supp.113.28.

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Abstract Cytotoxic T lymphocytes (CTLs) recognize foreign peptides presented at the cell surface bound to major histocompatibility complex class I (MHCI) molecules. Antigen recognition involves the binding of both T-cell receptor (TCR) and CD8 co-receptor to the same peptide-MHCI (pMHCI) ligand. Specificity is determined by the TCR, whereas CD8 mediates an effect on antigen sensitivity. Anti-CD8 antibodies have been used extensively in previous studies to examine the role of CD8 in CTL activation. However, it is unclear from the literature whether anti-CD8 antibodies per se are capable of inducing effector function. Here, we report on the ability of seven monoclonal anti-human CD8 antibodies to activate six human CTL clones with a total of five different specificities. Six out of seven anti-human CD8 antibodies tested did not activate CTLs. In contrast, one anti-human CD8 antibody, OKT8, induced effector function in all CTLs examined. Moreover, OKT8 was found to enhance TCR/pMHCI on-rates and, as a consequence, could be used to improve pMHCI tetramer staining. The observed heterogeneity in the ability of anti-CD8 antibodies to trigger T-cell effector function provides an explanation for the apparent incongruity observed in previous studies and should be taken into consideration when interpreting results generated with these reagents. Furthermore, the ability of antibody-mediated CD8 engagement to deliver an activation signal underscores the importance of CD8 in CTL signalling.
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Lazary, S., M. L. Dubath, Ch Luder, and H. Gerber. "EQUINE LEUCOCYTE ANTIGEN SYSTEM. IV. RECOMBINATION WITHIN THE MAJOR HISTOCOMPATIBILITY COMPLEX (MHC)." European Journal of Immunogenetics 13, no. 4 (August 1986): 315–26. http://dx.doi.org/10.1111/j.1744-313x.1986.tb01116.x.

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JARVI, SUSAN I., CHERYL L. TARR, CARL E. MCINTOSH, CARTER T. ATKINSON, and ROBERT C. FLEISCHER. "Natural selection of the major histocompatibility complex (Mhc) in Hawaiian honeycreepers (Drepanidinae)." Molecular Ecology 13, no. 8 (June 16, 2004): 2157–68. http://dx.doi.org/10.1111/j.1365-294x.2004.02228.x.

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48

Ejsmond, Maciej Jan, and Jacek Radwan. "Red Queen Processes Drive Positive Selection on Major Histocompatibility Complex (MHC) Genes." PLOS Computational Biology 11, no. 11 (November 24, 2015): e1004627. http://dx.doi.org/10.1371/journal.pcbi.1004627.

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49

Carmichael, Paul, John Copier, Alex So, and Robert Lechler. "Allele-Specific Variation in the Degeneracy of Major Histocompatibility Complex (MHC) Restriction." Human Immunology 54, no. 1 (April 1997): 21–29. http://dx.doi.org/10.1016/s0198-8859(97)00014-1.

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50

Keyserlingk, H. v., K. P. Dieckmann, U. Angelides, U. Geidner, B. Kirschbaum, N. Wöllert, and H. W. Bauer. "Testicular cancer — influence of the major histocompatibility complex (MHC) on pure seminoma." European Journal of Cancer and Clinical Oncology 23, no. 11 (November 1987): 1767. http://dx.doi.org/10.1016/0277-5379(87)90606-7.

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