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Binding of outer surface protein A and human lymphocyte function-associated antigen 1 peptides to HLA-DR molecules

Allen C Steere1, Ben Falk, Elise E Drouin

  • 1Tufts University School of Medicine, New England Medical Center, Boston, Massachusetts, USA. asteere@partners.org

Arthritis and Rheumatism
|February 7, 2003
PubMed
Abstract

Insights

Outer surface protein A (OspA) peptide binding to HLA-DRB1 alleles correlates with treatment-resistant Lyme arthritis. Human lymphocyte function-associated antigen 1 (hLFA-1) peptide binding shows a weaker association, suggesting OspA is a key trigger.

Area of Science:

  • Immunology
  • Molecular Biology
  • Genetics

Background:

  • Lyme arthritis is an inflammatory condition with a subset of patients developing treatment-resistant disease.
  • Major histocompatibility complex (MHC) molecules play a crucial role in antigen presentation and immune responses.
  • Outer surface protein A (OspA) from Borrelia burgdorferi and human lymphocyte function-associated antigen 1 (hLFA-1) are implicated in autoimmune responses.

Purpose of the Study:

  • To investigate the binding affinity of OspA and hLFA-1 peptides to specific human MHC class II molecules.
  • To correlate peptide-MHC binding with the prevalence of MHC alleles in patients with treatment-resistant Lyme arthritis.

Main Methods:

  • In vitro peptide binding assays were performed to quantify the interaction between OspA(163-175) and hLFA-1alpha(L330-342) peptides with five different MHC class II molecules (HLA-DRB1*0101, *0401, *0404, *0801, *1101).
  • Frequencies of these MHC alleles were analyzed in a cohort of patients diagnosed with treatment-resistant Lyme arthritis.

Main Results:

  • HLA-DRB1*0401 demonstrated strong binding to both OspA(163-175) and hLFA-1alpha(L330-342) peptides.
  • HLA-DRB1*0404 showed moderate binding to both peptides, while DRB1*0101 preferentially bound OspA(163-175).
  • Binding of OspA(163-175) strongly correlated with DRB1 allele frequencies in treatment-resistant Lyme arthritis patients, whereas hLFA-1alpha(L330-342) binding was associated only with DRB1*04 alleles.

Conclusions:

  • The strong correlation between OspA(163-175) binding and MHC allele frequencies supports its role as a critical epitope in triggering antibiotic-resistant Lyme arthritis.
  • The differential binding of hLFA-1alpha(L330-342) suggests it may not be a significant autoantigen, particularly in individuals positive for the DRB1*0101 allele.

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