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[The association of HLA-B27 binding peptide and spondylarthropathies]
Objective:
To explore the association of spondylarthropathies HAL-B27 binding peptide.
Methods:
B27 molecules expressed on the B27-T2 mutant cell line do not have peptides. Such empty B27 molecules were not recognized by peptide-dependent monoclonal antibody, B27.M2. Positive B27.M2 reactivity resulted when B27-T2 cells were incubated with peptide RRKAMFEDI derived from Chlamydia hsp60. THe importance of each residue in RRKAMFEDI was analysed by testing analogs in which each of the 9 residues in the peptide was consecutively substituted by 19 other amino acids.
Results:
B27.M2 reactivity was the highest with arginine in second residue. The reactivities of residues other than arginine were less than 30% of the value with the parent peptide.
Conclusion:
The stringency for other residues was relatively low, indicating that immune recognition of B27-peptide complexes might have rather low stringency for peptide sequences. These peptide residues probably influenced antibody reactivity by inducing conformational changes.