Relevance of residue 116 of HLA‐B27 in determining susceptibility to ankylosing spondylitis

Mauro D'amato, Maria Teresa Fiorillo, Carlo Carcassi, Alessandro Mathieu, Angelo Zuccarelli, Pier Paolo Bitti, Roberto Tosi, Rosa Sorrentino*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

174 Citations (Scopus)

Abstract

Ankylosing spondylitis (AS) is an autoimmune disorder strongly associated with HLA‐B27. A direct role of B27 molecules in the disease pathogenesis has been postulated, possibly by presenting to T cells an as‐yet unidentified arthritogenic peptide that triggers the autoimmune response. There are nine HLA‐B27 alleles differing from each other at one or more amino acid positions. It is important, for the identification of the arthritogenic peptide, to define which alleles, and therefore which polymorphic positions, predispose to the disease. Here, we report that HLA‐B2709 is not associated with AS, as it was not found in patients. HLA‐B2709 differs from the most frequent and disease‐associated HLA‐B2705 allele for a single substitution (His vs. Asp) at position 116. Amino acid 116 is located at the bottom of the groove where the antigenic peptide sits, and it has been proven to influence the peptide‐binding specificity of HLA class I molecules. The most likely interpretation of these data is that the differences in charge and size that accompany the His‐to‐Asp substitution exclude the acceptance of the arthritogenic peptide.

Original languageEnglish
Pages (from-to)3199-3201
Number of pages3
JournalEuropean Journal of Immunology
Volume25
Issue number11
DOIs
Publication statusPublished - 1 Jan 1995
Externally publishedYes

Keywords

  • Ankylosing spondylitis
  • Arthritogenic peptide
  • HLA‐B27

Cite this

D'amato, M., Fiorillo, M. T., Carcassi, C., Mathieu, A., Zuccarelli, A., Bitti, P. P., ... Sorrentino, R. (1995). Relevance of residue 116 of HLA‐B27 in determining susceptibility to ankylosing spondylitis. European Journal of Immunology, 25(11), 3199-3201. https://doi.org/10.1002/eji.1830251133
D'amato, Mauro ; Fiorillo, Maria Teresa ; Carcassi, Carlo ; Mathieu, Alessandro ; Zuccarelli, Angelo ; Bitti, Pier Paolo ; Tosi, Roberto ; Sorrentino, Rosa. / Relevance of residue 116 of HLA‐B27 in determining susceptibility to ankylosing spondylitis. In: European Journal of Immunology. 1995 ; Vol. 25, No. 11. pp. 3199-3201.
@article{40db89b21c134f7094b674e9d010a965,
title = "Relevance of residue 116 of HLA‐B27 in determining susceptibility to ankylosing spondylitis",
abstract = "Ankylosing spondylitis (AS) is an autoimmune disorder strongly associated with HLA‐B27. A direct role of B27 molecules in the disease pathogenesis has been postulated, possibly by presenting to T cells an as‐yet unidentified arthritogenic peptide that triggers the autoimmune response. There are nine HLA‐B27 alleles differing from each other at one or more amino acid positions. It is important, for the identification of the arthritogenic peptide, to define which alleles, and therefore which polymorphic positions, predispose to the disease. Here, we report that HLA‐B★2709 is not associated with AS, as it was not found in patients. HLA‐B★2709 differs from the most frequent and disease‐associated HLA‐B★2705 allele for a single substitution (His vs. Asp) at position 116. Amino acid 116 is located at the bottom of the groove where the antigenic peptide sits, and it has been proven to influence the peptide‐binding specificity of HLA class I molecules. The most likely interpretation of these data is that the differences in charge and size that accompany the His‐to‐Asp substitution exclude the acceptance of the arthritogenic peptide.",
keywords = "Ankylosing spondylitis, Arthritogenic peptide, HLA‐B27",
author = "Mauro D'amato and Fiorillo, {Maria Teresa} and Carlo Carcassi and Alessandro Mathieu and Angelo Zuccarelli and Bitti, {Pier Paolo} and Roberto Tosi and Rosa Sorrentino",
year = "1995",
month = "1",
day = "1",
doi = "10.1002/eji.1830251133",
language = "English",
volume = "25",
pages = "3199--3201",
journal = "European Journal of Immunology",
issn = "0014-2980",
publisher = "Wiley-VCH Verlag GmbH & Co. KGaA",
number = "11",

}

D'amato, M, Fiorillo, MT, Carcassi, C, Mathieu, A, Zuccarelli, A, Bitti, PP, Tosi, R & Sorrentino, R 1995, 'Relevance of residue 116 of HLA‐B27 in determining susceptibility to ankylosing spondylitis', European Journal of Immunology, vol. 25, no. 11, pp. 3199-3201. https://doi.org/10.1002/eji.1830251133

Relevance of residue 116 of HLA‐B27 in determining susceptibility to ankylosing spondylitis. / D'amato, Mauro; Fiorillo, Maria Teresa; Carcassi, Carlo; Mathieu, Alessandro; Zuccarelli, Angelo; Bitti, Pier Paolo; Tosi, Roberto; Sorrentino, Rosa.

In: European Journal of Immunology, Vol. 25, No. 11, 01.01.1995, p. 3199-3201.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Relevance of residue 116 of HLA‐B27 in determining susceptibility to ankylosing spondylitis

AU - D'amato, Mauro

AU - Fiorillo, Maria Teresa

AU - Carcassi, Carlo

AU - Mathieu, Alessandro

AU - Zuccarelli, Angelo

AU - Bitti, Pier Paolo

AU - Tosi, Roberto

AU - Sorrentino, Rosa

PY - 1995/1/1

Y1 - 1995/1/1

N2 - Ankylosing spondylitis (AS) is an autoimmune disorder strongly associated with HLA‐B27. A direct role of B27 molecules in the disease pathogenesis has been postulated, possibly by presenting to T cells an as‐yet unidentified arthritogenic peptide that triggers the autoimmune response. There are nine HLA‐B27 alleles differing from each other at one or more amino acid positions. It is important, for the identification of the arthritogenic peptide, to define which alleles, and therefore which polymorphic positions, predispose to the disease. Here, we report that HLA‐B★2709 is not associated with AS, as it was not found in patients. HLA‐B★2709 differs from the most frequent and disease‐associated HLA‐B★2705 allele for a single substitution (His vs. Asp) at position 116. Amino acid 116 is located at the bottom of the groove where the antigenic peptide sits, and it has been proven to influence the peptide‐binding specificity of HLA class I molecules. The most likely interpretation of these data is that the differences in charge and size that accompany the His‐to‐Asp substitution exclude the acceptance of the arthritogenic peptide.

AB - Ankylosing spondylitis (AS) is an autoimmune disorder strongly associated with HLA‐B27. A direct role of B27 molecules in the disease pathogenesis has been postulated, possibly by presenting to T cells an as‐yet unidentified arthritogenic peptide that triggers the autoimmune response. There are nine HLA‐B27 alleles differing from each other at one or more amino acid positions. It is important, for the identification of the arthritogenic peptide, to define which alleles, and therefore which polymorphic positions, predispose to the disease. Here, we report that HLA‐B★2709 is not associated with AS, as it was not found in patients. HLA‐B★2709 differs from the most frequent and disease‐associated HLA‐B★2705 allele for a single substitution (His vs. Asp) at position 116. Amino acid 116 is located at the bottom of the groove where the antigenic peptide sits, and it has been proven to influence the peptide‐binding specificity of HLA class I molecules. The most likely interpretation of these data is that the differences in charge and size that accompany the His‐to‐Asp substitution exclude the acceptance of the arthritogenic peptide.

KW - Ankylosing spondylitis

KW - Arthritogenic peptide

KW - HLA‐B27

UR - http://www.scopus.com/inward/record.url?scp=0028839838&partnerID=8YFLogxK

U2 - 10.1002/eji.1830251133

DO - 10.1002/eji.1830251133

M3 - Article

C2 - 7489765

AN - SCOPUS:0028839838

VL - 25

SP - 3199

EP - 3201

JO - European Journal of Immunology

JF - European Journal of Immunology

SN - 0014-2980

IS - 11

ER -