Allele- and temperature-dependency of in vitro HLA class I assembly

Chersi, Alberto; Garzillo, Carmine; Butler, Richard H.; Tanigaki, Nobuyuki

doi:10.1016/s0198-8859(01)00273-7

Cited by 4 publications

(3 citation statements)

References 29 publications

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“…Histidine 171 effects a substantial change in the position of the amino‐terminal residue, which causes the peptide to be drawn more deeply into the binding groove. Maenaka et al also attributed the slow in vitro assembly of HLA‐B*51:01 to the presence of histidine at position 171.…”

Section: Discussionmentioning

confidence: 54%

“…These same properties may also be responsible for the role of HLA‐B*51:01 in causing Behçet's disease. One characteristic of HLA‐B*51:01 is that it assembles more slowly in vitro than other HLA‐B allotypes , and this is reflected in vivo, where HLA‐B*51:01 is highly dependent on tapasin for its exit from the endoplasmic reticulum and translocation to the cell surface . When the three dimensional structure of HLA‐B*51:01 was compared with structures of the serologically related HLA‐B*35:01 and HLA‐B*53:01 allotypes, the substitution of histidine for tyrosine at position 171 was seen to have a dramatic effect on the conformation of the bound peptide .…”

Section: Discussionmentioning

confidence: 99%

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HLA class I variation in Iranian Lur and Kurd populations: high haplotype and allotype diversity with an abundance of KIR ligands

Ashouri

Norman

Guethlein

et al. 2016

HLA

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HLA-A , -B and -C alleles of 285 individuals, representing three Iranian Lur populations and one Iranian Kurd population were sequenced completely, yielding HLA class I genotypes at high resolution and filling four fields of the official HLA nomenclature. Each population has 87–99 alleles, evenly distributed between the three HLA class I genes, 145 alleles being identified in total. These alleles were already known, named and deposited in the HLA database. The alleles form 316 different HLA A-B-C haplotypes, with each population having between 80 and 112 haplotypes. The four Iranian populations form a related group that is distinguished from other populations, including other Iranians. All four KIR ligands - the A3/11, Bw4, C1 and C2 epitopes - are well represented, particularly Bw4, which is carried by three high-frequency allotypes: HLA-A*24:02, HLA-A*32:01 and HLA-B*51:01. In the Lur and Kurd populations, between 82% and 94% of individuals have the Bw4 epitope, the ligand for KIR3DL1. HLA-B*51:01 is likely of Neandertal origin and associated with Behcet’s disease, also known as the Silk Road disease. The Lordegan Lur have the highest frequency of HLA-B*51:01 in the world. This allele is present on 46 Lur and Kurd haplotypes. Present at lower frequency is HLA-B*51:08, which is also associated with Behcet’s disease. In the four Iranian populations, 31 haplotypes encode both Bw4+HLA-A and Bw4+HLA-B, a dual combination of Bw4 epitopes that is relatively rare in other populations, worldwide. This study both demonstrates and emphasizes the value of studying HLA class I polymorphism at highest resolution in anthropologically well-defined populations.

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Section: Discussionmentioning

confidence: 54%

Section: Discussionmentioning

confidence: 99%

HLA class I variation in Iranian Lur and Kurd populations: high haplotype and allotype diversity with an abundance of KIR ligands

Ashouri

Norman

Guethlein

et al. 2016

HLA

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“…We were not able to establish the MHC ELISA method for HLA‐B*35:01 owing to a very high background signal. This could be indicative for enhanced stability of the HLA‐B*35:01 molecule after conditional ligand cleavage under these experimental conditions although previous data relating to the assembly efficiency for HLA‐B*35 do not support this . It could be speculated if the remaining six amino acids after UV light induced cleavage would stabilize the HLA‐B*35:01 to retain the conformation even when no exchange peptide is added.…”

Section: Discussionmentioning

confidence: 76%

Design and validation of conditional ligands for HLA‐B08:01, HLA‐B15:01, HLA‐B35:01, and HLA‐B44:05

et al. 2015

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We designed conditional ligands restricted to HLA-B*08:01, 2B*35:01, and 2B*44:05 and proved the use of a conditional ligand previously designed for HLA-B*15:02 together with HLA-B*15:01. Furthermore, we compared the detection capabilities of specific HLA-B*15:01-restricted T cells using the HLA-B*15:01 and HLA-B*15:02 major histocompatibility complex (MHC) multimers and found remarkable differences in the staining patterns detected by flow cytometry. These new conditional ligands greatly add to the application of MHC-based technologies in the analyses of T-cell recognition as they represent frequently expressed HLA-B molecules. This expansion of conditional ligands is important to allow T-cell detection over a wide range of HLA restrictions, and provide comprehensive understanding of the T-cell recognition in a given context. V C 2015 International Society for Advancement of Cytometry Key terms CD8 T cells; MHC multimer; HLA-B molecules; flow cytometry; conditional ligands THE tracking of specific T cells by use of fluorochrome-conjugated major histocompatibility complex (MHC) multimers for flow cytometry has increased our understanding in all areas of T-cell immunology (1-3). Staining of cells for binding to MHC multimers, combined with a set of antibodies to identify the CD8 T-cell population, represents an attractive way to quantitatively and phenotypically measure the CD8 T cells with certain specificities in a complex cell sample. It is thus possible to directly investigate the frequency and phenotype of these peptide-MHC (pMHC) multimer-specific T cells. The design and use of conditional ligands for the generation of MHC monomers was introduced in 2006 and revolutionized our ability to generate MHC reagents in a high-throughput fashion (4). These are HLA-binding peptides containing an UV-labile bond next to a 2-nitrophenylglycine or 3-amino-3-(2-nitrophenyl)-propionic acid residue (denoted "J") in their amino acid sequence, and can be integrated into the standard refolding procedure. Upon short-term UV light (366 nm) exposure, the amide bond next to the "J" residue is cleaved, and the fragmented peptide can be substituted with another ligand. The rescue of the MHC Class I complex after UV light exposure is dependent on the binding affinity between the ligand and the MHC molecule. Thus, this technique allows high-throughput affinity estimation using an MHC ELISA (5,6) and the generation of large libraries of pMHC complexes for the determinations of antigen-specific T cells using MHC Class I multimers in flow (7,8) and mass cytometry (9). The UV exchange technology has been extended to several MHC Class I variants (2,6,10), but conditional ligands has previously not been defined for some of the most frequently expressed HLA-B alleles.

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Responses of peptide-specific T cells to stimulation with polystyrene beads carrying HLA class I molecules loaded with single peptides

Chersi¹,

Galati²,

Accapezzato

et al. 2004

Journal of Immunological Methods

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Allele- and temperature-dependency of in vitro HLA class I assembly

Cited by 4 publications

References 29 publications

HLA class I variation in Iranian Lur and Kurd populations: high haplotype and allotype diversity with an abundance of KIR ligands

HLA class I variation in Iranian Lur and Kurd populations: high haplotype and allotype diversity with an abundance of KIR ligands

Design and validation of conditional ligands for HLA‐B08:01, HLA‐B15:01, HLA‐B35:01, and HLA‐B44:05

Responses of peptide-specific T cells to stimulation with polystyrene beads carrying HLA class I molecules loaded with single peptides

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Allele- and temperature-dependency of in vitro HLA class I assembly

Cited by 4 publications

References 29 publications

HLA class I variation in Iranian Lur and Kurd populations: high haplotype and allotype diversity with an abundance of KIR ligands

HLA class I variation in Iranian Lur and Kurd populations: high haplotype and allotype diversity with an abundance of KIR ligands

Design and validation of conditional ligands for HLA‐B*08:01, HLA‐B*15:01, HLA‐B*35:01, and HLA‐B*44:05

Responses of peptide-specific T cells to stimulation with polystyrene beads carrying HLA class I molecules loaded with single peptides

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Design and validation of conditional ligands for HLA‐B08:01, HLA‐B15:01, HLA‐B35:01, and HLA‐B44:05