An essential role for HLA-DM in antigen presentation by class II major histocompatibility molecules

Morris, P. J.

doi:10.1016/0168-9525(94)90246-1

Cited by 89 publications

(130 citation statements)

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“…These results were consistent with observations obtained using human DC [159]. In contrast, after a 60-min incubation of BMDC with ECD HER2 complexed to anti-HER2/neu IgG3-(IL-2), 69% of co-localization was with LAMP-1, and 32% of co-localization was with H2-DM (equivalent to human HLA-DM; a marker of class II compartments [161]) indicated that ECD HER2 complexed with anti-HER2/neu IgG3-(IL-2) is redirected to antigen processing compartments [160]. These studies demonstrate that the complex ECD HER2 with anti-HER2/neu IgG3-(IL-2) promotes the uptake and presentation of the specific antigen by BMDC to T cells.…”

Section: Antibody-cytokine Fusion Proteins As Adjuvants Of Antitumor supporting

confidence: 81%

Antibody–cytokine fusion proteins: applications in cancer therapy

Ortíz‐Sánchez

Helguera

Daniels

et al. 2008

Expert Opinion on Biological Therapy

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Background-Antibody-cytokine fusion proteins consist of cytokines fused to an antibody to improve antibody-targeted cancer immunotherapy. These molecules have the capacity to enhance the tumoricidal activity of the antibodies and/or activate a secondary antitumor immune response.Objective-To review the strategies used to develop antibody-cytokine fusion proteins and their in vitro and in vivo properties, including preclinical and clinical studies focusing on IL-2, IL-12 and GM-CSF. Methods-Articles were found by searching databases such as PubMed and Clinical Trials of the US National Institutes of Health.Results/conclusion-Multiple antibody-cytokine fusion proteins have demonstrated significant antitumor activity as direct therapeutics or as adjuvants of cancer vaccines in preclinical studies, paving the way for their clinical evaluation.

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Section: Antibody-cytokine Fusion Proteins As Adjuvants Of Antitumor supporting

confidence: 81%

Antibody–cytokine fusion proteins: applications in cancer therapy

Ortíz‐Sánchez

Helguera

Daniels

et al. 2008

Expert Opinion on Biological Therapy

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“…Removal of CLIP and the addition of antigenic peptides are important for SDS stability of HLA class II proteins (7)(8)(9)(10)(11)(12)(13)(14)(15). The unique stability of DQ0602 in the HLA-DM-deficient cell line BLS-1 suggested the possibility that DQ0602 interacted with CLIP in a unique way that resulted in SDS stability.…”

Section: Discussionmentioning

confidence: 99%

“…This process is dependent on HLA-DM such that in HLA-DM-deficient cells, the SDS-resistant property of various HLA-DR, -DQ, and -DP molecules is generally lost (5,(7)(8)(9). Peptides eluted from DR3 on HLA-DM-deficient cells are predominantly derived from invariant chain (10,11).…”

mentioning

confidence: 99%

β57-Asp Plays an Essential Role in the Unique SDS Stability of HLA-DQA10102/DQB10602 αβ Protein Dimer, the Class II MHC Allele Associated with Protection from Insulin-Dependent Diabetes Mellitus

Ettinger

Liu

Nepom

et al. 2000

The Journal of Immunology

103

160

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Studies of the stability of HLA-DQ have revealed a correlation between SDS stability of MHC class II αβ dimers and insulin-dependent diabetes mellitus (IDDM) susceptibility. The MHC class II αβ dimer encoded by HLA-DQA1*0102/DQB1*0602 (DQ0602), which is a dominant protective allele in IDDM, exhibits the greatest SDS stability among HLA-DQ molecules in EBV-transformed B-lymphoblastoid cells and PBLs. DQ0602 is also uniquely SDS stable in the HLA-DM-deficient cell line, BLS-1. We addressed the molecular mechanism of the stability of DQ0602 in BLS-1. A panel of mutants based on the polymorphic differences between HLA-DQA1*0102/DQB1*0602 and HLA-DQA1*0102/DQB1*0604 were generated and expressed in BLS-1. An Asp at β57 was found to be critical for SDS stability, whereas Tyr at β30, Gly at β70, and Ala at β86 played secondary roles. Furthermore, the level of class II-associated invariant chain peptide bound to HLA-DQ did not correlate with SDS stability, suggesting that class II-associated invariant chain peptide does not play a direct role in the unique SDS stability of DQ0602. These results support a role for DQB1 codon 57 in HLA-DQ αβ dimer stability and IDDM susceptibility.

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“…The non-classical class II proteins, HLA-DM and -DO, assume the same structure described above for classical class II but lacks the ability to bind peptides. Their heterodimer molecules are also expressed by alpha and beta chain genes, HLA-DMA1 and -DMB1 for -DM molecules, and HLA-DOA1 and -DOB1 for -DO molecules [55,56] . However, in these non-classical loci, alpha and beta chain genes polymorphisms asymmetry are not evident and both show a very low number of alleles.…”

Section: The Hla Systemmentioning

confidence: 99%

HLA Loci and Respiratory Infectious Diseases

Spínola

2016

Journal of Respiratory Research

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The HLA system harbour a wide set of genes that plays an important role in the regulation and action of the immune system against invading pathogens, making them natural candidates for research on the genetic susceptibility for respiratory infections. Thus, along past decades, this topic has been subject to intense research and, consequently, several alleles of those loci have been implicated in the ability, more or less effective, to tackle and control invading pathogens in the respiratory system. Current editorial introduce, revise, summarize and comment the major advances in the role of HLA genes for the development of, and protection against, respiratory infectious disease. A general picture is drawn and new challenges on the field are relocated, especially those that might enlighten respiratory diseases aetiology and, thus, contribute in advances for diagnosis and treatment.

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An essential role for HLA-DM in antigen presentation by class II major histocompatibility molecules

Cited by 89 publications

References 0 publications

Antibody–cytokine fusion proteins: applications in cancer therapy

Antibody–cytokine fusion proteins: applications in cancer therapy

β57-Asp Plays an Essential Role in the Unique SDS Stability of HLA-DQA10102/DQB10602 αβ Protein Dimer, the Class II MHC Allele Associated with Protection from Insulin-Dependent Diabetes Mellitus

HLA Loci and Respiratory Infectious Diseases

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An essential role for HLA-DM in antigen presentation by class II major histocompatibility molecules

Cited by 89 publications

References 0 publications

Antibody–cytokine fusion proteins: applications in cancer therapy

Antibody–cytokine fusion proteins: applications in cancer therapy

β57-Asp Plays an Essential Role in the Unique SDS Stability of HLA-DQA1*0102/DQB1*0602 αβ Protein Dimer, the Class II MHC Allele Associated with Protection from Insulin-Dependent Diabetes Mellitus

HLA Loci and Respiratory Infectious Diseases

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β57-Asp Plays an Essential Role in the Unique SDS Stability of HLA-DQA10102/DQB10602 αβ Protein Dimer, the Class II MHC Allele Associated with Protection from Insulin-Dependent Diabetes Mellitus