Paired lines of C3H mouse fibroblasts transformed with murine sarcoma virus (Kirsten strain) were prepared that express high or low levels ofclass II major histocompatibility complex antigen after treatment with interferon y (IFN-y) . Here, we described a comparison of the tumorigenicity of these lines in euthymic syngeneic and thymus-deficient nu/nu mice and in mice depleted of IFN-y . The class II-inducible cells are clearly less tumorigenic than the noninducible cells in syngeneic mice, but of similar tumorigenicity in nu/nu mice and in mice treated with antibodies to deplete IFN-y . We propose that in this system, IFN-y induction of class II antigens on the tumor cell surface operates to limit tumor growth ; ras expression, which inhibits induction of class II antigens, prevents this and so allows tumor growth .
Looking for Major histocompatability complex? Find out information about Major histocompatability complex. In vertebrates, a family of genes that encode cell surface glycoproteins that regulate interactions among cells of the immune system, some components of the... Explanation of Major histocompatability complex
The first step in the induction of immune responses, whether humoral or cell mediated, requires the interaction between antigen-presenting cells and T lymphocytes restricted at the major histocompatibility complex (MHC). These cells invariably express MHC class II molecules (HLA-D region in man and Ia in mouse) which are recognized by T cells of the helper/inducer subset in association with antigen fragments. Interestingly, in certain pathological conditions, for example in autoimmune diseases such as thyroiditis and diabetic insulitis, class II molecules may be expressed on epithelial cells that normally do not express them. We speculated that these cells may be able to present their surface autoantigens to T cells, and that this process may be crucial to the induction and maintenance of autoimmunity. A critical test of this hypothesis would be to determine whether epithelial cells bearing MHC class II molecules (class II+ cells) can present antigen to T cells. We report here that class II+ thyroid
Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments.
Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments.
Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route; where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules; and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments; exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides; autophagosomes constitutively fuse with MHC class II loading ...
Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route; where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules; and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments; exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides; autophagosomes constitutively fuse with MHC class II loading ...
The expression of MHC class II molecules on β-cells of the pancreatic islet has been proposed to play a role in the genesis of insulin-dependent diabetes mellitus in the NOD mouse. We investigated this by immunofluorescent double labeling of islet cells with anti-MHC and anti-CD45 to identify cells of hematopoietic origin. MHC class I expression increased with age on CD45− islet cells. MHC class II expression was not observed on CD45− islet cells at any age; the only cells in the islet that were MHC class II positive were also CD45+. This indicates that all MHC class II-positive cells in the islet are lymphoid cells that infiltrate the islet, whereas the islet endocrine cells express no MHC class II molecules. However, an increase in MHC class I expression occurred on β-cells, and this may play a role in immunopathogenesis.. ...
The ability of the immune system to eliminate and shape the immunogenicity of tumours defines the process of cancer immunoediting1. Immunotherapies such as those that target immune checkpoint molecules can be used to augment immune-mediated elimination of tumours and have resulted in durable responses in patients with cancer that did not respond to previous treatments. However, only a subset of patients benefit from immunotherapy and more knowledge about what is required for successful treatment is needed2-4. Although the role of tumour neoantigen-specific CD8+ T cells in tumour rejection is well established5-9, the roles of other subsets of T cells have received less attention. Here we show that spontaneous and immunotherapy-induced anti-tumour responses require the activity of both tumour-antigen-specific CD8+ and CD4+ T cells, even in tumours that do not express major histocompatibility complex (MHC) class II molecules. In addition, the expression of MHC class II-restricted antigens by tumour cells
MHC Class II (I-A/I-E), PE-eFluor 610, clone: M5/114.15.2, eBioscience™ 25μg; PE-eFluor 610 MHC Class II (I-A/I-E), PE-eFluor 610, clone: M5/114.15.2,...
Anti-MHC Class II antibody conjugated to Biotin [ER-TR3] validated for IHC, Flow Cyt, ICC/IF and tested in Mouse. Referenced in 1 publication. Immunogen…
Helper T cells are stimulated to fight infections or diseases upon recognition of peptides from antigens that are processed and presented by the proteins of Major Histocompatibility Complex (MHC) Class II molecules. Degradation of a full protein into small peptide fragments is a lengthy process consisting of many steps and chaperones. Malfunctions during any step of antigen processing could lead to the development of self-reactive T cells or defective immune response to pathogens. Although much has been accomplished regarding how antigens are processed and presented to T cells, many questions still remain unanswered, preventing the design of therapeutics for direct intervention with antigen processing. Here, we review published work on the discovery and function of a MHC class II molecular chaperone, HLA-DO, in human, and its mouse analog H2-O, herein called DO. While DO was originally discovered decades ago, elucidating its function has proven challenging. DO was discovered in association with
MHC Class II RT1Bu/L antibody [OX-3] (FITC) for FACS. Anti-MHC Class II RT1Bu/L mAb (GTX43381) is tested in Mouse, Rat samples. 100% Ab-Assurance.
HLA class II histocompatibility antigen gamma chain also known as HLA-DR antigens-associated invariant chain or CD74 (Cluster of Differentiation 74), is a protein that in humans is encoded by the CD74 gene. The invariant chain (Abbreviated Ii) is a polypeptide involved in the formation and transport of MHC class II protein. The cell surface form of the invariant chain is known as CD74. The nascent MHC class II protein in the rough ER binds a segment of the invariant chain (Ii; a trimer) in order to shape the peptide binding groove and prevent formation of a closed conformation. Binding to Ii might also prevent binding of peptides from the endogenous pathway to the groove of MHC class II. The invariant chain also facilitates MHC class IIs export from the ER in a vesicle. The signal for endosomal targeting resides in the cytoplasmic tail of the invariant chain. This fuses with a late endosome containing the endocytosed proteins. It is then cleaved by cathepsin S (cathepsin L in cortical thymic ...
We used a hit and run gene targeting strategy to generate mice expressing only the p31 isoform of the conserved invariant (Ii) chain associated with major histocompatibility complex (MHC) class II molecules. Spleen cells from these mice appear indistinguishable from wild type with respect to class II subunit assembly, transport, peptide acquisition, surface expression, and the ability to present intact protein antigens. Moreover, these mutant mice have normal numbers of thymic and peripheral CD4+ T cells, and intact CD4+ T-dependent proliferative responses towards a soluble antigen. In short, MHC class II expression and function are surprisingly unaffected in mice lacking p41 invariant chain, implying that the p31 and p41 isoforms may be functionally redundant in the intact animal.
Accurate prediction of antigen presentation by human leukocyte antigen (HLA) class II molecules would be valuable for vaccine development and cancer immunotherapies. Current computational methods trained on in vitro binding data are limited by insufficient training data and algorithmic constraints. Here we describe MARIA (major histocompatibility complex analysis with recurrent integrated architecture; https://maria.stanford.edu/ ), a multimodal recurrent neural network for predicting the likelihood of antigen presentation from a gene of interest in the context of specific HLA class II alleles. In addition to in vitro binding measurements, MARIA is trained on peptide HLA ligand sequences identified by mass spectrometry, expression levels of antigen genes and protease cleavage signatures. Because it leverages these diverse training data and our improved machine learning framework, MARIA (area under the curve = 0.89-0.92) outperformed existing methods
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HLA class II histocompatibility antigen, DO beta chain is a protein that in humans is encoded by the HLA-DOB gene. HLA-DOB belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DOA) and a beta chain (DOB), both anchored in the membrane. It is located in intracellular vesicles. DO suppresses peptide loading of MHC class II molecules by inhibiting HLA-DM. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. ENSG00000241910, ENSG00000243612, ENSG00000239457, ENSG00000241386, ENSG00000241106 GRCh38: Ensembl release 89: ENSG00000243496, ENSG00000241910, ENSG00000243612, ENSG00000239457, ENSG00000241386, ENSG00000241106 - Ensembl, May 2017 ...
Antigen presentation requires intracellular processing of native antigens to produce immunogenic peptides that bind to major histocompatibility complex class II (MHC-II) molecules. In functional studies of antigen processing by elicited peritoneal macrophages, MHC-II-peptide complexes were formed intracellularly. Immunogenic peptides were not released to bind surface MHC-II molecules. Ultrastructural studies employing immunogold staining in ultrathin cryosections of these macrophages showed large amounts of MHC-II molecules in intracellular sac-like vacuoles in the peripheral cytoplasm; most of these were negative for the lamp 1 lysosomal/endosomal membrane protein and cathepsin D. MHC-II molecules were also present in endosomes containing cathepsin D and lamp 1 as well as previously internalized gold-transferrin. The intracellular pool of MHC-II molecules was only slightly decreased by treatment with cycloheximide for 3 hr, indicating that it consisted mainly of endocytosed, recycling molecules, as
Unlike B cells, CD8-positive and CD4-positive T cells of the adaptive immune system do not recognize intact foreign proteins but instead recognize polypeptide fragments of potential antigens. These antigenic peptides are expressed on the surface of antigen presenting cells bound to MHC class I and MHC class II proteins. Here, we review the basics of antigen acquisition by antigen presenting cells, antigen proteolysis into polypeptide fragments, antigenic peptide binding to MHC proteins, and surface display of both MHC class I-peptide and MHC class II-peptide complexes.
Background: The major histocompatibility complex (MHC) is responsible for presenting antigens (epitopes) on the surface of antigen-presenting cells (APCs). When pathogen-derived epitopes are presented by MHC class II on an APC surface, T cells may be able to trigger an specific immune response. Prediction of MHC-II epitopes is particularly challenging because the open binding cleft of the MHC-II molecule allows epitopes to bind beyond the peptide binding groove; therefore, the molecule is capable of accommodating peptides of variable length. Among the methods proposed to predict MHC-II epitopes, artificial neural networks (ANNs) and support vector machines (SVMs) are the most effective methods. We propose a novel classification algorithm to predict MHC-II called sparse representation via 1-minimization. Results: We obtained a collection of experimentally confirmed MHC-II epitopes from the Immune Epitope Database and Analysis Resource (IEDB) and applied our 1-minimization algorithm. To benchmark the
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Sage AP, Nus M, Murphy D, Finigan A, Baker L, Masters L and Mallat Z. Regulatory B cell specific interleukin-10 does not regulate atherosclerosis in mice. ATVB. 35(8):1770-3. doi: 10.1161/ATVBAHA.115.305568. Sage A, Murphy D, Sabir S, Grazia G, Maffia P, Masters L, Baker L, Finigan A, Harrison J, Ludewig B, Reith W, Hansson G, Reizis B, Hugues S, Mallat Z. (2014) MHC class II-restricted antigen presentation by plasmacytoid dendritic cells drives pro-atherogenic immunity. 14;130(16):1363-73. doi: 10.1161/CIRCULATIONAHA.114.011090.. Sage AP & Mallat Z. (2014). Multiple potential roles for B cells in atherosclerosis. Ann Med. doi:10.3109/07853890.2014.900272. Ait-Oufella H, Sage AP, Mallat Z, Tedgui A. (2014). Adaptive (T and B cells) immunity and control by dendritic cells in atherosclerosis. Circ Res, 114(10), 1640-1660. doi:10.1161/CIRCRESAHA.114.302761. Zouggari Y, Ait-Oufella H, Bonnin P, Simon T, Sage A, Guérin C, Vilar J, Caligiuri G, Tsiantoulas D, Laurans L, Dumeau E, Kotti S, Bruneval P, ...
The invariant chain (Ii) binds nascent major histocompatibility complex (MHC) class II molecules, blocking peptide binding until the complex dissociates in the endosomes. This may serve to differentiate the MHC class I and II antigen presentation pathways and enable class II molecules to efficiently bind peptides in the endosomes. This hypothesis was addressed by probing spleen cells from a combination of knock-out and transgenic mice with a large panel of T cell hybridomas. The Ii molecule blocked the presentation of a range of endogenously synthesized epitopes, but some epitopes actually required Ii. Thus, the influence of Ii on presentation does not follow simple rules. In addition, mice expressing Ii were not tolerant to epitopes unmasked in its absence, a finding with possible implications for autoimmunity. ...
Vaccination of colon cancer patients with X-irradiated autologous tumor cells and Bacillus Calmette-Guérin results in a significant reduction in tumor recurrence. A study was undertaken to determine whether the expression of tumor-associated antigens, expression of major histocompatibility complex molecules, or the cellular composition of the vaccine cells correlates with vaccine efficacy. A significant increase in the percentage of histocompatibility leukocyte antigen (HLA) class II molecule-expressing tumor cells was the only marker with a positive correlation. Because HLA class II molecule expression is not a prognostic marker in control patients, it was hypothesized that HLA class II molecules are involved in the induction of tumor immunity in patients treated with the autologous colon tumor vaccine. Enhancement of HLA class II molecule-expressing cells could be induced in X-irradiated colon tumor cells injected into the skin of mice when the cells were mixed with γ-interferon. Therefore, ...
FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II ...
Infection with L. major is a well-characterized model in which differentiation of class II-restricted T cells into the two mature helper subsets is required for expression of the resistant and susceptible disease phenotype. Ii is required for stable expression of surface class II molecules and, as predicted, cells from Ii −/− mice have substantially lower amounts of surface class II that do not assume the compact conformation that characterizes stable peptide binding ((17), (28), (29)). The major immunologic consequences are twofold: a severely compromised ability to present processed antigens via the class II pathway, and a quantitatively and qualitatively altered CD4+ population due to aberrant selection by thymic epithelial cells unable to present self peptides in a normal manner ((40), (41)). Despite this drastic effect on the class II-dependent immune response, we could discern little consequence to the host in generating either Th1 or Th2 responses to L. major. How might we explain ...
In both collagen-induced arthritis (CIA) and rheumatoid arthritis, T cells recognize a galactosylated peptide from type II collagen (CII). In this study, we demonstrate that the CII259-273 peptide, galactosylated at lysine 264, in complex with Aq molecules prevented development of CIA in mice and ameliorated chronic relapsing disease. In contrast, nonglycosylated CII259-273/Aq complexes had no such effect. CIA dependent on other MHC class II molecules (Ar/Er) was also down-regulated, indicating a bystander vaccination effect. T cells could transfer the amelioration of CIA, showing that the protection is an active process. Thus, a complex between MHC class II molecules and a posttranslationally modified peptide offers a new possibility for treatment of chronically active autoimmune inflammation such as rheumatoid arthritis.
We identified the EphA3 antigen by cotransfecting into 293-EBNA cells a cDNA library from the tumor and cDNA clones coding for CIITA and for the relevant HLA class β II chain. This genetic approach should be generally applicable to clone other genes coding for antigens presented by MHC class II molecules. Although we verified that CIITA induced the expression of Ii in 293-EBNA cells and endowed them with the capacity to present antigens on HLA class II molecules, we observed that the additional cotransfection of an Ii cDNA improved antigen presentation. This proved true for antigens encoded either by the Ii-MAGE-A3 or by the EphA3 cDNA clones (data not shown). A free pool of Ii has been observed in class II-positive cells (31 , 32) , suggesting that an excess of Ii in the endoplasmic reticulum may be important for class II function. This may explain our results.. The name Eph was given to a putative receptor cloned from a human erythropoietin-producing hepatocarcinoma cell line (33 , 34) . Eph ...
The major histocompatibility complex (MHC) is a collection of genes coding for MHC molecules found on the surface of all nucleated cells of the body. In humans, the MHC genes are also referred to as human leukocyte antigen (HLA) genes. Mature red blood cells, which lack a nucleus, are the only cells that do not express MHC molecules on their surface.. There are two classes of MHC molecules involved in adaptive immunity, MHC I and MHC II (Figure 14.11). MHC I molecules are found on all nucleated cells; they present normal self-antigens as well as abnormal or nonself pathogens to the effector T cells involved in cellular immunity. In contrast, MHC II molecules are only found on macrophages, dendritic cells, and B cells; they present abnormal or nonself pathogen antigens for the initial activation of T cells.. Both types of MHC molecules are transmembrane glycoproteins that assemble as dimers in the cytoplasmic membrane of cells, but their structures are quite different. MHC I molecules are ...
While the absence of genes directly encoding MHC class II molecules was similar to the situation in cod [6], the receptor encoding gene (CD8β), which is involved in MHC I recognition via the T-cell receptor (TCR) was absent in pipefish but not cod (table 1). Note that CD8β is not mandatory for a MHC I mediated immune response, as CD8α molecules may function as a homodimer [16]. The antigen recognizing TCR γ was also absent. Because the majority of TCRs consist of α/β-heterodimers, functionality of the TCR is still likely [17].. As opposed to cod, where the CD4+-receptor was truncated and non-functional, this gene could not be identified among pipefish transcripts. For the invariant-chain gene, our annotation returned two contigs that aligned almost perfectly to each other, suggesting the same transcript. When translated into the appropriate amino acid sequence, the putative gene model revealed a stop codon approximately 20 amino acid distant from the 3′-end of the gene in other teleosts ...
IMMUNREAKTION + IMMUNANTWORT (IMMUNOLOGIE); DENDRITISCHE ZELLEN (IMMUNOLOGIE); MHC-KLASSE-II-MOLEKÜLE (IMMUNOLOGIE); ZENTRALNERVENSYSTEM (NEUROLOGIE); IMMUNE REACTION + IMMUNE RESPONSE (IMMUNOLOGY); DENDRITIC CELLS (IMMUNOLOGY); MHC CLASS II MOLECULES (IMMUNOLOGY); CENTRAL NERVOUS SYSTEM (NEUROLOGY ...
MHC II glycoproteins are only present on specialised antigen-presenting cells (APCs), including macrophages that engulf foreign particles such as bacteria, dendritic cells that present antigen to T cells, and B cells that produce antibodies.. ...
Principal nameMHC Class II I-Ak antibodyAlternative names for MHC Class II I-Ak antibodyH2-Aa, H-2 class II histocompatibility antigen A-K alpha…
Antigen presented to CD4+ T cells by major histocompatibility complex class II molecules (MHCII) plays a key role in adaptive immunity. Antigen presentation is initiated by the proteolytic cleavage of pathogenic or self proteins and loading of resultant peptides to MHCII. The loading and exchange of peptides to MHCII is catalyzed by a nonclassical MHCII molecule, HLA-DM (DM). It is well established that DM promotes peptide exchange in vitro and in vivo. However, the mechanism of DM-catalyzed peptide association and dissociation, and how this would affect epitope selection in human responses to infectious disease remain unclear. The work presented in this thesis was directed towards the understanding of mechanism of DM-mediated peptide exchange and its role in epitope selection. In Chapter II, I measured the binding affinity, intrinsic dissociation half-life and DM-mediated dissociation half-life for a large set of peptides derived from vaccinia virus and compared these properties to the peptide-specific
cDCs link innate and adaptive immunity by sensing pathogens and initiating adaptive immune responses. Although the two physiological functions of cDCs are likely to play distinct roles in immune homeostasis, they have not previously been evaluated independently. In the gut, cDCs sense and capture gut microbes in part by extending their processes into the gut lumen (Macpherson and Uhr, 2004; Niess et al., 2005; Chieppa et al., 2006; Vallon-Eberhard et al., 2006). Microbial sensing induces cDCs to produce cytokines such as IL-23, which are required to activate innate lymphoid cells (Kinnebrew et al., 2012; Satpathy et al., 2013). In addition, the ingested microbes are carried to local lymphoid organs, such as the mLNs, processed, and presented to T cells to initiate adaptive immune responses (Macpherson and Uhr, 2004; Niess et al., 2005).. Ablation experiments using CD11cDTR mice, conditional deletion of genes (e.g., Irf4, Irf8, or Notch2) with CD11cCre mice, and Batf3-deficient mice result in ...
TY - JOUR. T1 - Structural Analysis of Invariant Chain Subsets as a Function of Their Association with MHC Class II Chains. AU - Nguyen, Q. V.. AU - Reyes, Victor. AU - Humphreys, R. E.. PY - 1995/2/20. Y1 - 1995/2/20. N2 - Respective subsets of human invariant chain (Ii), as identified with antibodies to two different epitopes, were characterized as a function of their associations with major histocompatibility complex (MHC) class II α,β chains and intracellular processing. E1 antiserum to Ii(183-193) and VIC-Y1 monoclonal antibody to an N-terminal determinant identified Ii(E1) and Ii(VIC) populations, respectively. Ii proteins comprise several species which have been defined with either genomic or post-translational processes: Ii itself; IpN and IpO, which represent the glycosylated forms on asparagine or threonine/serine, respectively; γ2 and γ3, which originate from an alternative initiation site for transcription; and p41, which has a 64-amino-acid insert which originated from an ...
2oje: Zinc induces dimerization of the class II major histocompatibility complex molecule that leads to cooperative binding to a superantigen.
The nascent MHC class II protein in the rough ER has its peptide-binding cleft blocked by the invariant chain (Ii; a trimer) to prevent it from binding cellular peptides or peptides from the endogenous pathway. The invariant chain also facilitates MHC class IIs export from the ER in a vesicle. This fuses with a late endosome containing the endocytosed, degraded proteins. It is then broken down in stages, leaving only a small fragment called CLIP which still blocks the peptide binding cleft. An MHC class II-like structure, HLA-DM, removes CLIP and replaces it with a peptide from the endosome. The stable MHC class-II is then presented on the cell surface ...
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Summary is not available for the mouse gene. This summary is for the human ortholog.] HLA-DRB5 belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DRA) and a beta (DRB) chain, both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DR molecule the beta chain contains all the polymorphisms specifying the peptide binding specificities. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. DRB1 is expressed at a level five times higher than its paralogues ...
Histocompatibility Antigens Class II information including symptoms, causes, diseases, symptoms, treatments, and other medical and health issues.
Expression of MHC Class II Antigens During Xenopus Development. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
My major interest is in antigen processing, defined as the combination of mechanisms that generate the complexes of class I and class II MHC molecules with peptides that are the targets for recognition by T lymphocytes. My colleagues and I have identified a number of proteins that collaborate in these processes. MHC class I peptide binding occurs in the context of a large complex that we have defined in the endoplasmic reticulum consisting of TAP, an ATP-dependent peptide transporter; tapasin, a protein that couples the transporter to assembling class I molecules; and two "house-keeping" chaperones, calreticulin and ERp57. How these accessory molecules combine to facilitate peptide binding is currently being intensively investigated. We have also studied MHC class II peptide binding through the mechanism of class II molecules being delivered into the endocytic pathway by an associated protein, the invariant chain. This has included study of the CLIP, a residual fragment of the invariant chain, ...
Human class II pMHC tetramers containing autoantigenic specificities have been used to study T cell responses in a variety of diseases, including type 1 diabetes (T1D), celiac disease, pemphigus vulgaris, rheumatoid arthritis, multiple sclerosis, and uveitis (37-47). These studies have highlighted a fundamental point: the avidity of the TCR interaction with its pMHC target is influenced by selection against high-affinity self-Ag recognition. Unlike tetramer analyses in the infectious pathogen and allergen studies cited above, in which most of the responding T cells have a high-avidity binding to appropriate pMHC tetramers, tetramer binding to peripheral T cells in the context of autoimmunity displays a much wider spectrum of relative strength of interaction. In addition, the frequency of autoreactive CD4 T cells specific for a particular pMHC-self-Ag complex is quite low in peripheral blood, often less than five per million lymphocytes, requiring large sample volumes and careful handling for ...
RefSeq Summary (NM_006120): HLA-DMA belongs to the HLA class II alpha chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DMA) and a beta chain (DMB), both anchored in the membrane. It is located in intracellular vesicles. DM plays a central role in the peptide loading of MHC class II molecules by helping to release the CLIP molecule from the peptide binding site. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The alpha chain is approximately 33-35 kDa and its gene contains 5 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and the cytoplasmic tail. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC011447.1, ...
Major histocompatibility complex class II (MHC-II) molecules are expressed on the surface of professional antigen-presenting cells where they display peptides to T helper cells, which orchestrate the onset and outcome of many host immune responses. Understanding which peptides will be presented by the MHC-II molecule is therefore important for understanding the activation of T helper cells and can be used to identify T-cell epitopes. We here present updated versions of two MHC-II-peptide binding affinity prediction methods, NetMHCII and NetMHCIIpan. These were constructed using an extended data set of quantitative MHC-peptide binding affinity data obtained from the Immune Epitope Database covering HLA-DR, HLA-DQ, HLA-DP and H-2 mouse molecules. We show that training with this extended data set improved the performance for peptide binding predictions for both methods. Both methods are publicly available at www.cbs.dtu.dk/services/NetMHCII-2.3 and www.cbs.dtu.dk/services/NetMHCIIpan-3.2. PMID: ...
Clone REAL362 is an antibody fragment derived from the full MHC Class II (I-Ab) antibody molecule. It displays no binding to Fc receptors. The recombinantly engineered antibody fragments are multimerized to form the REAlease Complex to bind markers with high avidity.Clone REAL362 recognizes the mouse MHC class II alloantigen I-Ab of H-2b bearing mouse strains. It also cross-reacts with the H-2k and H-2u haplotypes, but reactivity to other haplotypes like, for example, d, f, g7, p, q, r, and s has not been observed. MHC class II is expressed on antigen-presenting cells, such as dendritic cells, monocytes, macrophages, B cells in lymphoid and non-lymphoid tissue, thymic epithelial cells, and on subsets of hematopoietic progenitor cells in the bone marrow.The REAlease Kits consist of the respective fluorochrome-conjugated REAlease Complexes and the REAlease Support Kit for removal of the REAlease Complexes and optional relabeling with different fluorochrome-conjugated REAlease Complexes. - Österreich
The Nonconventional MHC Class II Molecule DM Governs Diabetes Susceptibility in NOD Mice. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
MHC Class II I-Ab Mouse anti-Mouse, APC, Clone: AF6-120.1, eBioscience™ 100μg; APC MHC Class II I-Ab Mouse anti-Mouse, APC, Clone: AF6-120.1,...