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Artykuły w czasopismach na temat „Presentation of peptides”

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Data publikacji: 30 listopada 2024

Data aktualizacji: 31 lipca 2025

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1

Wen, R., G. A. Cole, S. Surman, M. A. Blackman, and D. L. Woodland. "Major histocompatibility complex class II-associated peptides control the presentation of bacterial superantigens to T cells." Journal of Experimental Medicine 183, no. 3 (1996): 1083–92. http://dx.doi.org/10.1084/jem.183.3.1083.

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Recent studies have shown that only a subset of major histocompatibility complex (MHC) class II molecules are able to present bacterial superantigens to T cells, leading to the suggestion that class-II associated peptides may influence superantigen presentation. Here, we have assessed the potential role of peptides on superantigen presentation by (a) analyzing the ability of superantigens to block peptide-specific T cell responses and (b) analyzing the ability of individual peptides to promote superantigen presentation on I-Ab-expressing T2 cells that have a quantitative defect in antigen proc

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2

Utz, U., S. Koenig, J. E. Coligan, and W. E. Biddison. "Presentation of three different viral peptides, HTLV-1 Tax, HCMV gB, and influenza virus M1, is determined by common structural features of the HLA-A2.1 molecule." Journal of Immunology 149, no. 1 (1992): 214–21. http://dx.doi.org/10.4049/jimmunol.149.1.214.

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Abstract To determine whether similar or dissimilar molecular features of class I molecules are involved in the presentation of structurally distinct peptides, we have investigated the influence of different pockets of the HLA-A2.1 molecule on the presentation of three different viral peptides. HTLV-I Tax peptide 12-19, HCMV gB 619-628, and influenza M1 58-66 are minimal peptides that induce HLA-A2.1-restricted noncross-reactive CTL. A detailed analysis of the structural features of HLA-A2.1 that are involved in peptide presentation was undertaken using a panel of 11 HLA-A2 mutants with single

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3

Zandvliet, Maarten L., J. H. Frederik Falkenburg, Michel G. D. Kester, et al. "Sequence Dependent Efficiency of Cross-Presentation in MHC Class I Requires Rational Design of Long Synthetic Peptides for Vaccination or Ex Vivo Activation." Blood 112, no. 11 (2008): 3904. http://dx.doi.org/10.1182/blood.v112.11.3904.3904.

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Abstract For the induction or boosting of antigen-specific CD8+ T cell responses, long synthetic peptides have been used in vaccination studies. Superior in vivo CD8+ T cell responses have been reported following vaccination with long peptides compared with minimal peptides, which was attributed to selective uptake and cross-presentation by professional antigen-presenting cells. Furthermore, to generate antigen-specific T cell lines for adoptive immunotherapy or to measure antigen-specific T cell responses, protein-spanning pools of overlapping long synthetic peptides can be used to simultaneo

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4

Neisig, A., J. Roelse, A. J. Sijts, et al. "Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences." Journal of Immunology 154, no. 3 (1995): 1273–79. http://dx.doi.org/10.4049/jimmunol.154.3.1273.

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Abstract The MHC-encoded transporter associated with Ag presentation (TAP) translocates peptides from the cytosol to the ER lumen, where association with MHC class I molecules occurs. The MHC class I/peptide complex is subsequently transported to the cell surface for presentation to CD8+T cells. We studied TAP-dependent translocation of defined MHC class I presentable murine peptides by competition for translocation of a radiolabeled model peptide, to address whether efficient peptide presentation by MHC class I molecules is preceded by equal efficient peptide translocation by TAP. Surprisingl

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5

Fremont, Daved H., Shaodong Dai, Herbert Chiang, Frances Crawford, Philippa Marrack, and John Kappler. "Structural Basis of Cytochrome c Presentation by IEk." Journal of Experimental Medicine 195, no. 8 (2002): 1043–52. http://dx.doi.org/10.1084/jem.20011971.

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The COOH-terminal peptides of pigeon and moth cytochrome c, bound to mouse IEk, are two of the most thoroughly studied T cell antigens. We have solved the crystal structures of the moth peptide and a weak agonist–antagonist variant of the pigeon peptide bound to IEk. The moth peptide and all other peptides whose structures have been solved bound to IEk, have a lysine filling the p9 pocket of IEk. However, the pigeon peptide has an alanine at p9 shifting the lysine to p10. Rather than kinking to place the lysine in the anchor pocket, the pigeon peptide takes the extended course through the bind

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6

Hombach, J., H. Pircher, S. Tonegawa, and R. M. Zinkernagel. "Strictly transporter of antigen presentation (TAP)-dependent presentation of an immunodominant cytotoxic T lymphocyte epitope in the signal sequence of a virus protein." Journal of Experimental Medicine 182, no. 5 (1995): 1615–19. http://dx.doi.org/10.1084/jem.182.5.1615.

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Peptides presented by major histocompatibility complex (MHC) class I molecules are derived from intracellularly synthesized proteins. Cytosolic proteins are fragmented into peptides, which are subsequently transported via the transporter of antigen presentation (TAP) into the endoplasmic reticulum (ER), where they bind to MHC class I molecules. We have investigated the requirements for MHC class I presentation of the immunodominant gp33 cytotoxic T lymphocyte epitope of the lymphocytic choriomeningitis virus. This epitope is located within the leader peptide of the virus glycoprotein. Such an

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7

Daniel, Soizic, Vladimir Brusic, Sophie Caillat-Zucman, et al. "Relationship Between Peptide Selectivities of Human Transporters Associated with Antigen Processing and HLA Class I Molecules." Journal of Immunology 161, no. 2 (1998): 617–24. http://dx.doi.org/10.4049/jimmunol.161.2.617.

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Abstract Efficiency of presentation of a peptide epitope by a MHC class I molecule depends on two parameters: its binding to the MHC molecule and its generation by intracellular Ag processing. In contrast to the former parameter, the mechanisms underlying peptide selection in Ag processing are poorly understood. Peptide translocation by the TAP transporter is required for presentation of most epitopes and may modulate peptide supply to MHC class I molecules. To study the role of human TAP for peptide presentation by individual HLA class I molecules, we generated artificial neural networks capa

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8

Mo, X. Y., Paolo Cascio, Kristen Lemerise, Alfred L. Goldberg, and Kenneth Rock. "Distinct Proteolytic Processes Generate the C and N Termini of MHC Class I-Binding Peptides." Journal of Immunology 163, no. 11 (1999): 5851–59. http://dx.doi.org/10.4049/jimmunol.163.11.5851.

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Abstract Most of the MHC class I peptides presented to the immune system are generated during the course of protein breakdown by the proteasome. However, the precise role of the proteasome, e.g., whether this particle or some other protease generates the carboxyl (C) and amino (N) termini of the presented 8- to 10-residue peptides, is not clear. Here, we show that presentation on Db of ASNENMETM, a peptide from influenza nucleoprotein, and on Kb of FAPGNYPAL, a peptide from Sendai virus nucleoprotein, was blocked by the proteasome inhibitor, lactacystin. Using plasmid minigene constructs encod

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9

Monji, T., and D. Pious. "Exogenously provided peptides fail to complex with intracellular class II molecules for presentation by antigen-presenting cells." Journal of Immunology 158, no. 7 (1997): 3155–64. http://dx.doi.org/10.4049/jimmunol.158.7.3155.

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Abstract Exogenously supplied antigenic peptides can bind to and be presented by cell surface class II molecules of APCs without prior processing. However, it has been unclear whether peptide Ags exogenously supplied to APCs can also form complexes with nascent intracellular class II molecules that contribute to Ag presentation. We found that exogenously provided peptide Ags, unlike whole protein Ags, are presented as efficiently by fixed as by unfixed B lymphoblastoid APCs, suggesting that intracellular processes do not contribute to the presentation of exogenously supplied peptides by unfixe

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10

Stryhn, A., L. O. Pedersen, T. Romme, et al. "pH dependence of MHC class I-restricted peptide presentation." Journal of Immunology 156, no. 11 (1996): 4191–97. http://dx.doi.org/10.4049/jimmunol.156.11.4191.

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Abstract The function of MHC class I molecules is to bind and present antigenic peptides to cytotoxic T cells. Here, we report that class I-restricted peptide presentation is strongly pH dependent. The presentation of some peptides was enhanced at acidic pH, whereas the presentation of others was inhibited. Biochemical peptide-MHC class I binding assays demonstrated that peptide-MHC class I complexes are more stable at neutral pH than at acidic pH. We suggest that acid-dependent peptide dissociation can generate empty class I molecules and that the resulting binding potential can be exploited

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11

Boucau, Julie, Julien Madouasse, Christopher Carlin, et al. "Effect of cellular activation on the antigen processing machinery of primary CD4 T cells. (P5029)." Journal of Immunology 190, no. 1_Supplement (2013): 110.15. http://dx.doi.org/10.4049/jimmunol.190.supp.110.15.

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Abstract The killing of HIV-infected CD4 T cells by specific CD8 T cells (CTL) requires the presentation of peptide-MHC-I complexes produced during the intracellular degradation of viral proteins by the proteasome and other peptidases, to their cognate T cell receptors. HIV infection induces general cellular activation, which renders cells more susceptible to infection. Whether the activation state of cells alters the expression and activity of the antigen processing machinery and the kinetics and nature of epitopes displayed by MHC-I is not known despite its potential role in altering the eff

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12

Garstka, Malgorzata A., Alexander Fish, Patrick H. N. Celie, et al. "The first step of peptide selection in antigen presentation by MHC class I molecules." Proceedings of the National Academy of Sciences 112, no. 5 (2015): 1505–10. http://dx.doi.org/10.1073/pnas.1416543112.

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MHC class I molecules present a variable but limited repertoire of antigenic peptides for T-cell recognition. Understanding how peptide selection is achieved requires mechanistic insights into the interactions between the MHC I and candidate peptides. We find that, at first encounter, MHC I H-2Kb considers a wide range of peptides, including those with expanded N termini and unfitting anchor residues. Discrimination occurs in the second step, when noncanonical peptides dissociate with faster exchange rates. This second step exhibits remarkable temperature sensitivity, as illustrated by numerou

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13

Yin, Liusong, Mauricio Calvo-Calle, and Lawrence Stern. "Characterization of HLA-DM susceptibility of MHC II-peptide complex in antigen presentation and epitope selection (100.54)." Journal of Immunology 186, no. 1_Supplement (2011): 100.54. http://dx.doi.org/10.4049/jimmunol.186.supp.100.54.

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Abstract HLA-DM (DM) is a non-classic major histocompatibility complex II (MHC II), which mediates the exchange of peptides loading to MHC II during antigen presentation. However, the role of DM-mediated peptide exchange in epitope selection is still unclear. In this study, we addressed this question systematically using overlapping peptides from vaccinia virus protein A10L. We measured the binding affinity, intrinsic half life, DM-mediated half life and immunogenecity of 126 A10L peptides bound to HLA-DR1. Correlation coefficient analysis shows that immunogenecity of peptides is very weakly c

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14

Anton, L. C., J. W. Yewdell, and J. R. Bennink. "MHC class I-associated peptides produced from endogenous gene products with vastly different efficiencies." Journal of Immunology 158, no. 6 (1997): 2535–42. http://dx.doi.org/10.4049/jimmunol.158.6.2535.

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Abstract We compared the efficiency of generating antigenic peptides from various polypeptide contexts expressed by recombinant vaccinia viruses. These included full-length influenza virus nucleoprotein (NP(1-498)), two truncated forms, and cytosolic and endoplasmic reticulum-targeted minimal peptides. Two peptides were studied, NP(50-57) (Kk-restricted) and NP(147-155) (Kd-restricted). The efficiency of peptide generation was measured in cytotoxicity assays by determining 1) the kinetics of presentation following infection using brefeldin A to block additional presentation and 2) the concentr

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15

Legge, Kevin L., Booki Min, Christopher Pack, Jacque Caprio, and Habib Zaghouani. "Differential Presentation of an Altered Peptide Within Fetal Central and Peripheral Organs Supports an Avidity Model for Thymic T Cell Development and Implies a Peripheral Readjustment for Activation." Journal of Immunology 162, no. 10 (1999): 5738–46. http://dx.doi.org/10.4049/jimmunol.162.10.5738.

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Abstract Altered self peptides may drive T cell development by providing avidity of interactions low enough to potentiate positive selection but not powerful enough to trigger programmed cell death. Since the peptide repertoire in both central and peripheral organs is nearly the same, interactions of these peptides with T cells in the thymus would have to be different from those taking place in the periphery; otherwise, T cell development and maturation would result in either autoimmunity or T cell deficiency. Herein, a self and an altered self peptide were delivered to fetuses, and their pres

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16

Barouch, D., T. Friede, S. Stevanović, et al. "HLA-A2 subtypes are functionally distinct in peptide binding and presentation." Journal of Experimental Medicine 182, no. 6 (1995): 1847–56. http://dx.doi.org/10.1084/jem.182.6.1847.

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Nearly half of HLA-A2-positive individuals in African populations have a subtype of HLA-A2 other than the A*0201 allele. We have isolated the common African HLA-A2 subtype genes from Epstein-Barr virus-transformed B cell lines and have established stable class I reduced transfectants expressing these alleles. We have studied the peptide binding and presentation properties of A*0201, A*0202, A*0205, A*0214, and A*6901 by a combination of approaches: assaying direct binding of labeled synthetic peptides, studying the ability of antigen-specific cytotoxic T lymphocytes to recognize peptide-pulsed

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17

Prasad, Sharanya, Shelley Starck, and Nilabh Shastri. "Presentation of cryptic peptides by MHC I molecules is enhanced by inflammatory stimuli. (P5003)." Journal of Immunology 190, no. 1_Supplement (2013): 110.2. http://dx.doi.org/10.4049/jimmunol.190.supp.110.2.

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Abstract Cytolytic T cells eliminate infected cells by recognizing intracellular peptides presented by MHC class I molecules. The antigenic peptides are derived primarily from newly synthesized proteins including those produced by cryptic translation. Previous studies have shown that in addition to the canonical AUG codon, translation can be initiated at non-AUG codons . Furthermore, translation initiation at non-AUG codons such as CUG is mechanistically distinct from canonical translation initiation as it is resistant to protein synthesis inhibitors that cause global translation shutdown. Her

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18

Lind, Kristin, Hernando Escobar, Eduardo Reyes-Vargas, Julio Delgado, and Nilabh Shastri. "ERAAP-deficiency differentially affects peptide presentation across multiple MHC I (100.15)." Journal of Immunology 186, no. 1_Supplement (2011): 100.15. http://dx.doi.org/10.4049/jimmunol.186.supp.100.15.

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Abstract Genome-wide association studies in humans have linked polymorphisms in the ER aminopeptidase associated with antigen processing (ERAAP) as well as particular MHC class I molecules to autoimmune diseases. How ERAAP polymorphisms affect function of different MHC I molecules is not known. ERAAP normally trims antigenic precursor peptides to generate potential peptide-MHC I ligands that can be recognized by CD8 T cells. To detect changes in the peptide repertoires displayed by different MHC I molecules, we immunized wild-type B10.D2 (H-2d) mice with ERAAP-deficient (ERAAP-KO) cells and an

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Bacik, I., J. H. Cox, R. Anderson, J. W. Yewdell, and J. R. Bennink. "TAP (transporter associated with antigen processing)-independent presentation of endogenously synthesized peptides is enhanced by endoplasmic reticulum insertion sequences located at the amino- but not carboxyl-terminus of the peptide." Journal of Immunology 152, no. 2 (1994): 381–87. http://dx.doi.org/10.4049/jimmunol.152.2.381.

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Abstract Under most circumstances, cell surface MHC class I molecules display peptides derived from a cytosolic pool of proteins. The efficient presentation of such peptides requires the functioning of two MHC gene products [TAP1 and TAP2 (transporter-associated with Ag processing 1 and 2)] that form a complex that facilitates transmembrane movement of peptides from the cytosol to the endoplasmic reticulum, the site of peptide association with class I molecules. It has been previously shown that peptides can be presented in a TAP-independent manner in association with HLA A2.1 or H-2 Kd if the

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Khodadoust, Michael, Niclas Olsson, Lisa Wagar, et al. "Antigen Presentation Profiling Reveals T-Cell Recognition of Lymphoma Immunoglobulin Neoantigens." Blood 128, no. 22 (2016): 915. http://dx.doi.org/10.1182/blood.v128.22.915.915.

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Abstract Neoantigens arising through somatic mutations are increasingly recognized as key tumor antigens driving clinical immune responses. We sought to identify human lymphoma neoantigens through a genomic and proteomic characterization of peptide ligands of major histocompatibility complex class I (MHC-I) and class II (MHC-II) of a cohort of patients with untreated mantle cell lymphoma. Peptide identification was performed through analysis of MHC-I and MHC-II peptide ligands using liquid chromatography and tandem mass spectrometry (LC/MS-MS), and augmented by generating patient-specific prot

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Vijayasimha, Kartikeya, Amy Leigh Leestemaker-Palmer, James Gibb, Jonathan W. Yewdell, and Brian P. Dolan. "Targeted protein degradation via NEDD8 conjugation does not enhance direct MHC class I antigen presentation." Journal of Immunology 206, no. 1_Supplement (2021): 93.01. http://dx.doi.org/10.4049/jimmunol.206.supp.93.01.

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Abstract Knowledge of different pathways contributing to peptide generation for direct MHC class I antigen presentation is important to the field of immunotherapy. Here we investigated the role of the ubiquitin-like protein NEDD8 in antigen presentation. We show that proteins tagged N-terminally with NEDD8 undergo rapid degradation via the proteasomal, and autophagy-lysosomal pathways. To determine if protein NEDDylation increased peptide presentation, we fused NEDD8 to the N-terminus of a cytosolic form of ovalbumin (OVA) and measured presentation of the SIINFEKL peptide via the murine MHC cl

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Zajonc, Dirk M. "Unconventional Peptide Presentation by Classical MHC Class I and Implications for T and NK Cell Activation." International Journal of Molecular Sciences 21, no. 20 (2020): 7561. http://dx.doi.org/10.3390/ijms21207561.

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T cell-mediated immune recognition of peptides is initiated upon binding of the antigen receptor on T cells (TCR) to the peptide-MHC complex. TCRs are typically restricted by a particular MHC allele, while polymorphism within the MHC molecule can affect the spectrum of peptides that are bound and presented to the TCR. Classical MHC Class I molecules have a confined binding groove that restricts the length of the presented peptides to typically 8–11 amino acids. Both N- and C-termini of the peptide are bound within binding pockets, allowing the TCR to dock in a diagonal orientation above the MH

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23

Lo-Man, Richard, Jan P. M. Langeveld, Pierre Martineau, Maurice Hofnung, Robert H. Meloen, and Claude Leclerc. "Immunodominance Does Not Result from Peptide Competition for MHC Class II Presentation." Journal of Immunology 160, no. 4 (1998): 1759–66. http://dx.doi.org/10.4049/jimmunol.160.4.1759.

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Abstract Competition for binding to MHC class II molecules between processed peptides derived from a single protein Ag is considered an important parameter leading to the presentation of a limited set of peptides by APCs. We tested the relevance of this competition process in a model Ag, the MalE protein, by deleting T cell epitopes or by introducing a competitor T cell peptide. We identified in DBA/1 (I-Aq) mice six immunodominant T cell determinants in the MalE sequence, 89–95, 116–123, 198–205, 211–219, 274–281, and 335–341. Synthetic peptides carrying these determinants were classified in

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Rimer, Jamie, and Emil Unanue. "Presentation of citrullinated peptides by class II histocompatibility molecules is associated with autophagy. (100.19)." Journal of Immunology 186, no. 1_Supplement (2011): 100.19. http://dx.doi.org/10.4049/jimmunol.186.supp.100.19.

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Abstract Autoimmune responses to citrullinated proteins are associated with rheumatoid arthritis; however, little is known of the mechanism of citrullination by the antigen presenting cells (APC) of the immune system. Using T cell hybridomas as probes, we found constitutive presentation by class II-Major Histocompatibility Complex (MHC) molecules of a dominant citrullinated peptide from hen egg-white lysozyme (HEL) by either macrophages or dendritic cells. Treatment of APC with 3-Methyladenine (3MA) blocked presentation of the citrullinated peptides after processing unmodified HEL, but present

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Balasubramani, Anand. "Stitching peptides for presentation." Science 362, no. 6412 (2018): 300.20–302. http://dx.doi.org/10.1126/science.362.6412.300-t.

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Heemels, Marie-Thérèse, and Hidde Ploegh. "Antigen presentation: Untapped peptides." Current Biology 3, no. 6 (1993): 380–83. http://dx.doi.org/10.1016/0960-9822(93)90208-6.

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Bell, Elaine. "Trimming peptides for presentation." Nature Reviews Immunology 6, no. 1 (2006): 7. http://dx.doi.org/10.1038/nri1765.

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Samson Li, Chi Han, Hong Wang, Kin Tak Chan, et al. "Abstract 3538: The development of neoantigen-derived peptide vaccine driven by AI epitope design and computer assisted epitope enhancement." Cancer Research 85, no. 8_Supplement_1 (2025): 3538. https://doi.org/10.1158/1538-7445.am2025-3538.

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Abstract Background and objective: Neoantigens are the ideal targets for developing cancer vaccine for cancer treatment. However, the development of cancer vaccines is often hindered by poor antigen presentation of the vaccine peptide by major histocompatibility complex (MHC) molecules. Our AI epitope prediction model showed prediction accuracy superior to several state-of-the-art algorithms for MHC-I antigen presentation. As studies showed that amino acid substitution in key positions of MHC-I epitope provides strong activating signals to cytotoxic T cells, we aimed to develop MHC-I restricte

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Fox, Robert I., and Ho-Il Kang. "Mechanism of Action of Antimalarial Drugs: Inhibition of Antigen Processing and Presentation." Lupus 2, no. 1_suppl (1993): 9–12. http://dx.doi.org/10.1177/0961203393002001031.

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Recent studies have elucidated the steps involved in the association of antigenic peptides with major histocompatibility complex (MHC) encoded proteins and have suggested how antimalarial compounds might influence this important site of immune activation. These steps of antigen presentation in the macrophage (or other antigen-presenting cells) include: (a) the partial proteolytic degradation of endogenous and exogenous proteins into peptides within the lysosome; (b) the synthesis of MHC class II (i.e. HLA-D associated) α, β, and invariant (Ii) chains in the endoplasmic reticulum; (c) the initi

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Cram, Erik D., Ryan S. Simmons, Amy L. Palmer, William H. Hildebrand, Daniel D. Rockey, and Brian P. Dolan. "Enhanced Direct Major Histocompatibility Complex Class I Self-Antigen Presentation Induced by Chlamydia Infection." Infection and Immunity 84, no. 2 (2015): 480–90. http://dx.doi.org/10.1128/iai.01254-15.

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The direct major histocompatibility complex (MHC) class I antigen presentation pathway ensures intracellular peptides are displayed at the cellular surface for recognition of infected or transformed cells by CD8+cytotoxic T lymphocytes.Chlamydiaspp. are obligate intracellular bacteria and, as such, should be targeted by CD8+T cells. It is likely thatChlamydiaspp. have evolved mechanisms to avoid the CD8+killer T cell responses by interfering with MHC class I antigen presentation. Using a model system of self-peptide presentation which allows for posttranslational control of the model protein's

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Shawar, S. M., J. M. Vyas, E. Shen, J. R. Rodgers, and R. R. Rich. "Differential amino-terminal anchors for peptide binding to H-2M3a or H-2Kb and H-2Db." Journal of Immunology 151, no. 1 (1993): 201–10. http://dx.doi.org/10.4049/jimmunol.151.1.201.

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Abstract We previously established that H-2M3a, the H chain of the maternally transmitted Ag (Mta), is specialized for presentation of N-formylated peptides. We hypothesized that the N-formyl group might prevent or limit the presentation of peptide Ag by H-2K and H-2D molecules. We now show by Mta- and OVA-specific CTL assays, peptide competition, and immunofluorescence analyses that N-formyl modification of four antigenic peptides inhibited their binding by either H-2Kb (OVAMet258-264, VSVNP52-59, and SVNP324-332) or H2-Db (SVNP324-332, and IVNP366-374). In contrast, N-formyl-OVAMet258-264 di

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Legge, Kevin L., Booki Min, Nicholas T. Potter, and Habib Zaghouani. "Presentation of a T Cell Receptor Antagonist Peptide by Immunoglobulins Ablates Activation of T Cells by a Synthetic Peptide or Proteins Requiring Endocytic Processing." Journal of Experimental Medicine 185, no. 6 (1997): 1043–54. http://dx.doi.org/10.1084/jem.185.6.1043.

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T cell receptor (TCR) antagonism is being considered for inactivation of aggressive T cells and reversal of T cell–mediated autoimmune diseases. TCR antagonist peptides silence aggressive T cells and reverse experimental allergic encephalomyelitis induced with free peptides. However, it is not clear whether free antagonist peptides could reverse natural disease where the antigen is presumably available for endocytic processing and peptides gain access to newly synthesized class II MHC molecules. Using an efficient endocytic presentation system, we demonstrate that a proteolipid protein (PLP) T

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van Ham, Marieke, Marcel van Lith, Björn Lillemeier, et al. "Modulation of the Major Histocompatibility Complex Class II–Associated Peptide Repertoire by Human Histocompatibility Leukocyte Antigen (Hla)-Do." Journal of Experimental Medicine 191, no. 7 (2000): 1127–36. http://dx.doi.org/10.1084/jem.191.7.1127.

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Antigen presentation by major histocompatibility complex class II molecules is essential for antibody production and T cell activation. For most class II alleles, peptide binding depends on the catalytic action of human histocompatibility leukocyte antigens (HLA)-DM. HLA-DO is selectively expressed in B cells and impedes the activity of DM, yet its physiological role remains unclear. Cell surface iodination assays and mass spectrometry of major histocompatibility complex class II–eluted peptides show that DO affects the antigenic peptide repertoire of class II. DO generates both quantitative a

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Sorvillo, Nicoletta, Simon D. van Haren, Paul H. Kaijen, et al. "Preferential HLA-DRB1*11 Dependent Presentation of CUB2 Derived Peptides by ADAMTS13 Pulsed Dendritic Cells." Blood 120, no. 21 (2012): 489. http://dx.doi.org/10.1182/blood.v120.21.489.489.

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Abstract Abstract 489 Autoantibodies directed against ADAMTS13 prohibit the processing of VWF multimers initiating a rare and life-threatening disorder called acquired thrombotic thrombocytopenic purpura (TTP). Recently, HLA-DRB1*11 has been identified as a risk factor for the development of acquired TTP. Here, we identified ADAMTS13-derived peptides presented on MHC class II alleles. Dendritic cells from a panel of both HLA-DRB1*11 positive and negative donors were pulsed with ADAMTS13 and the HLA-DR-presented peptide repertoire was analyzed by mass spectrometry. Interestingly, pulsing of den

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Chen, B. P., A. Madrigal, and P. Parham. "Cytotoxic T cell recognition of an endogenous class I HLA peptide presented by a class II HLA molecule." Journal of Experimental Medicine 172, no. 3 (1990): 779–88. http://dx.doi.org/10.1084/jem.172.3.779.

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Human leukocytes were stimulated in vitro with peptides corresponding in sequence to the highly variable helix of the alpha 1 domain of various HLA-B and -C molecules. A CD4+ CD8- cytotoxic T cell line, CTL-AV, that is specific for the HLA-B7 peptide presented by HLA-DR11.1 was obtained. The HLA-DR11.2 molecule, which only differs at three residues from HLA-DR11.1, did not present the HLA-B7 peptide to CTL-AV. Peptides from the alpha 1 domain helix of other HLA-A and HLA-B molecules, but not HLA-C molecules, competed with the HLA-B7 peptide for binding to HLA-DR11.1. A cell line (WT50) that co

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Nagamine, Brandy S., and Brian P. Dolan. "The unfolded protein response alters MHC class I antigen presentation in a mouse cell line." Journal of Immunology 200, no. 1_Supplement (2018): 99.9. http://dx.doi.org/10.4049/jimmunol.200.supp.99.9.

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Abstract Direct MHC class I antigen presentation is a necessary step to identify cells for elimination by cytotoxic CD8+ T cells. Antigenic peptides may originate from host-derived unnecessary or “retired” proteins as well as defective ribosomal products (DRiPs). DRiPs are newly synthesized polypeptides incapable of attaining a stable configuration and are thus rapidly degraded. The balance between protein synthesis and degradation, key processes to antigenic peptide generation, are likely influenced by the unfolded protein response (UPR). The UPR is a cellular response designed to alleviate t

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Garg, Manish, Margaret K. Callahan, and Pramod K. Srivastava. "Essential role of heat shock protein 90 in direct and cross-presentation (93.13)." Journal of Immunology 178, no. 1_Supplement (2007): S168. http://dx.doi.org/10.4049/jimmunol.178.supp.93.13.

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Abstract Direct antigen presentation involves the generation of peptides by proteasomes, ferrying of peptides from cytosol to endoplasmic reticulum and finally, formation and transport of peptide-MHC I complexes. Chaperones hsp90, hsp70, gp96 and TriC have previously been shown to associate with MHC class I epitopes and their precursors. Here, we have treated cells with hsp90 inhibitors Radicicol, 17-AAG or geldanamycin and observe that (i) treatment of cells with such inhibitors leads, in a dose-and time- dependent fashion, to a decrease in the levels of peptide-bound but not total cell surfa

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Lee, Daniel, Andy J. Minn, and Lexus R. Johnson. "CAR-T cells to deliver engineered peptide antigens and reprogram antigen specific T cell responses against solid tumors." Journal of Clinical Oncology 39, no. 15_suppl (2021): 2530. http://dx.doi.org/10.1200/jco.2021.39.15_suppl.2530.

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2530 Background: Neoantigen depleted malignancies such as colorectal cancer demonstrate primary resistance to immune checkpoint blockade, and solid tumors in general have shown resistance to chimeric antigen receptor (CAR) T cell therapy. However, CAR-T cells have been shown to be capable of delivering various therapeutic molecules in a targeted fashion to the tumor microenvironment, in some cases through extracellular vesicles (EVs). In vivo studies have shown that the presentation of foreign viral peptides by solid tumors can reprogram bystander virus-specific cytotoxic T cells (CTLs) agains

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Hall, Pamela R., Brian Hjelle, David C. Brown, et al. "Multivalent Presentation of Antihantavirus Peptides on Nanoparticles Enhances Infection Blockade." Antimicrobial Agents and Chemotherapy 52, no. 6 (2008): 2079–88. http://dx.doi.org/10.1128/aac.01415-07.

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ABSTRACT Viral entry into susceptible host cells typically results from multivalent interactions between viral surface proteins and host entry receptors. In the case of Sin Nombre virus (SNV), a New World hantavirus that causes hantavirus cardiopulmonary syndrome, infection involves the interaction between viral membrane surface glycoproteins and the human integrin αvβ3. Currently, there are no therapeutic agents available which specifically target SNV. To address this problem, we used phage display selection of cyclic nonapeptides to identify peptides that bound SNV and specifically prevented

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Rosloniec, E. F., L. J. Vitez, S. Buus, and J. H. Freed. "MHC class II-derived peptides can bind to class II molecules, including self molecules, and prevent antigen presentation." Journal of Experimental Medicine 171, no. 5 (1990): 1419–30. http://dx.doi.org/10.1084/jem.171.5.1419.

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Seven synthetic peptides corresponding to the polymorphic regions of the alpha and beta chains of the I-Ak molecule were examined for their ability to inhibit the presentation of foreign antigens to antigen-specific, I-A-restricted T cell hybridomas. Two of the peptides, representing the sequences found in the first and third polymorphic regions (PMR) of the A alpha k chain (alpha k-1 and alpha k-3) were capable of inhibiting the presentation of three different HEL-derived peptide antigens to their appropriate T cells. In addition, the alpha k-1 peptide inhibited the presentation of the OVA(32

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Adorini, L., J. Moreno, F. Momburg, et al. "Exogenous peptides compete for the presentation of endogenous antigens to major histocompatibility complex class II-restricted T cells." Journal of Experimental Medicine 174, no. 4 (1991): 945–48. http://dx.doi.org/10.1084/jem.174.4.945.

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Antigen-presenting cells (APC) transfected with a construct encoding the hen egg-white lysozyme (HEL) amino acid sequence 1-80 constitutively present HEL peptides complexed to major histocompatibility complex (MHC) class II molecules to specific T cell hybridomas, indicating that endogenous cellular antigens can be efficiently presented to class II-restricted T cells. Here we show that exogenous peptide competitors added to HEL-transfected APC can inhibit the presentation of endogenous HEL peptides to class II-restricted T cells. The inhibition is specific for the class II molecule binding the

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Haque, Syed Mahdee, Abdul-Rahman Salman, Hamdi Abdeen, et al. "Cancer immunotherapy: Identifying cancer testis antigen peptides to enhance antitumor response." Journal of Clinical Oncology 40, no. 16_suppl (2022): e20022-e20022. http://dx.doi.org/10.1200/jco.2022.40.16_suppl.e20022.

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e20022 Background: Cancer testis antigens (CTAs) are highly immunogenic, tissue-restricted proteins that may be over expressed in hematological malignancies. In this study, an in silico analysis of CTA-derived peptide presentation on HLA class I molecules is reported with an aim to identify putative CTA peptides with a high estimated binding affinity to known HLA class I molecules. Methods: Eighty unique HLA Class I alleles (HLA-A, B, and C), across 78 hematopoietic cell transplant recipients were computationally studied for their ability to bind peptides derived from three CTAs. The amino aci

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Mellins, E., P. Cameron, M. Amaya, et al. "A mutant human histocompatibility leukocyte antigen DR molecule associated with invariant chain peptides." Journal of Experimental Medicine 179, no. 2 (1994): 541–49. http://dx.doi.org/10.1084/jem.179.2.541.

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From a human histocompatibility leukocyte antigen (HLA)-DR/DQ hemizygous, B lymphoblastoid progenitor, we isolated a cell line, 10.24.6, with a DR alpha missense mutation (96P--&gt;96S), which results in an N-linked carbohydrate addition at position 94 in the DR alpha 2 domain. Several features of 10.24.6 cells suggest that the mutation disrupts normal intracellular formation of peptide/DR complexes. The mutant HLA-DR dimers, though expressed at the cell surface, lack the conformation of the mature, peptide-loaded class II molecules of the progenitor cell, as assessed by their loss of bind

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Dörfel, Daniela, Silke Appel, Frank Grünebach, et al. "Processing and presentation of HLA class I and II epitopes by dendritic cells after transfection with in vitro–transcribed MUC1 RNA." Blood 105, no. 8 (2005): 3199–205. http://dx.doi.org/10.1182/blood-2004-09-3556.

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AbstractRNA transfection of dendritic cells (DCs) was shown to be highly efficient in eliciting CD8+ and CD4+ T-cell responses. However, antigen presentation pathways involved in generation of human leukocyte antigen (HLA) class I and class II peptides have remained elusive. To analyze this we incubated mucin 1 (MUC1) RNA-transfected DCs with compounds known to inhibit HLA class I presentation and used these cells in chromium 51 (51Cr)–release assays. As effectors, we used cytotoxic T lymphocyte (CTL) lines specific for the MUC1 peptides M1.1 and M1.2. We observed that the presentation of HLA-

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Lazarski, Christopher A., Francisco A. Chaves, and Andrea J. Sant. "The impact of DM on MHC class II–restricted antigen presentation can be altered by manipulation of MHC–peptide kinetic stability." Journal of Experimental Medicine 203, no. 5 (2006): 1319–28. http://dx.doi.org/10.1084/jem.20060058.

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DM edits the peptide repertoire presented by major histocompatibility complex class II molecules by professional antigen-presenting cells (APCs), favoring presentation of some peptides over others. Despite considerable research by many laboratories, there is still significant uncertainty regarding the biochemical attributes of class II–peptide complexes that govern their susceptibility to DM editing. Here, using APCs that either do or do not express DM and a set of unrelated antigens, we found that the intrinsic kinetic stability of class II–peptide complexes is tightly correlated with the eff

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Ma, Yue, and Yoko Yamakoshi. "(Invited, Digital Presentation) Aggregation Switchable Fullerene-Peptides Conjugates." ECS Meeting Abstracts MA2022-01, no. 11 (2022): 810. http://dx.doi.org/10.1149/ma2022-0111810mtgabs.

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Intensive research has been applied on chemical functionalization of fullerenes over the past decades, aiming at utilizing their broad availabilities in chemical biology field. Chemical moieties was induced to improve their water solubility and thus enhance their properties or interaction with biomolecules. In our previous study, we reported the synthesis of fullerene-PEG conjugates and demonstrated their ability for photoinduced DNA damage and ROS generation under visible light irradiation. In this work, we report a water-soluble fullerene derivative by constructing a fullerene-peptide conjug

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van Ham, S. M., U. Grüneberg, G. Malcherek, I. Bröker, A. Melms, and J. Trowsdale. "Human histocompatibility leukocyte antigen (HLA)-DM edits peptides presented by HLA-DR according to their ligand binding motifs." Journal of Experimental Medicine 184, no. 5 (1996): 2019–24. http://dx.doi.org/10.1084/jem.184.5.2019.

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Human histocompatibility leukocyte antigen (HLA)-DM is a facilitator of antigen presentation via major histocompatibility complex (MHC) class II molecules. In the absence of HLA-DM, MHC class II molecules do not present natural peptides, but tend to remain associated with class II-associated invariant chain peptides (CLIP). Recently, DM was shown to catalyze the release of CLIP from HLA-DR. We have investigated which peptides bound to HLA-DR are vulnerable to release upon encountering DM. By directed substitution of allele-specific anchor residues between CLIP and DR3-cognate peptides and the

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Kropp, Laura, Manish Garg, and Robert Binder. "Ovalbumin-derived precursor peptides are transferred sequentially from gp96 and calreticulin to MHC I in the endoplasmic reticulum (130.26)." Journal of Immunology 184, no. 1_Supplement (2010): 130.26. http://dx.doi.org/10.4049/jimmunol.184.supp.130.26.

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Abstract Cellular peptides generated by proteasomal degradation of proteins in the cytosol and destined for presentation by MHC I are associated with several chaperones. Hsp70, hsp90, and the TCP1-ring complex have been implicated as important cytosolic players for chaperoning these peptides. In this study we report that gp96 and calreticulin are essential for chaperoning peptides in the endoplasmic reticulum. Importantly we demonstrate that cellular peptides are transferred sequentially from gp96 to calreticulin and then to MHC I forming a relay line. Disruption of this relay line by removal

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Shimojo, N., W. L. Maloy, R. W. Anderson, W. E. Biddison, and J. E. Coligan. "Specificity of peptide binding by the HLA-A2.1 molecule." Journal of Immunology 143, no. 9 (1989): 2939–47. http://dx.doi.org/10.4049/jimmunol.143.9.2939.

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Abstract The HLA-A2 molecule contains a putative peptide binding site that is bounded by two alpha-helices and a beta-pleated sheet floor. Previous studies have demonstrated that the influenza virus matrix peptide M1 55-73 can sensitize target cells for lysis by HLA-A2.1-restricted virus-immune CTL and can induce CTL that can lyse virus-infected target cells. To assess the specificity of peptide binding by the HLA-A2.1 molecule, we examined the ability of seven variant M1 peptides to be recognized by a panel of M1 55-73 peptide-specific HLA-A2.1-restricted CTL lines. The results demonstrate th

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Zügel, U., B. Schoel, and S. H. Kaufmann. "Beta 2-microglobulin independent presentation of exogenously added foreign peptide and endogenous self-epitope by MHC class I alpha-chain to a cross-reactive CD8+ CTL clone." Journal of Immunology 153, no. 9 (1994): 4070–80. http://dx.doi.org/10.4049/jimmunol.153.9.4070.

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Abstract CD8+ T cells recognize antigenic peptides in the context of MHC class I molecules that encompass two distinct polypeptide chains, the MHC-encoded alpha-chain and the non-MHC-encoded beta 2-microglobulin (beta 2-m). The beta 2-m is considered essential for the stability and function of the MHC class I peptide complex and, hence, for peptide presentation to CD8+ T cells. In this study, we describe peptide presentation by macrophages from beta 2-m-deficient mice to a CD8+ CTL clone tht cross-recognizes an H-2Db-restricted peptide of the mycobacterial heat shock protein 60 (hsp60) and a s

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