Analysis of the molecular mimicry between HLA-B27 and a bacterial OmpA protein using synthetic peptides.
In spite of a lack of sequence 'homology' between HLA-B27 and the bacterial OmpA outer membrane proteins, they both react with the Ye-2 monoclonal anti-HLA-B27 antibody. The Ye-2 antibody also reacted positively in ELISA with a synthetic peptide derived from the segment spanning residues 63-84 of B*2705. The critical peptide residues were determined by testing first with overlapping peptides, followed by a replacement set made according to the determined epitope. The results were compared with those with overlapping eight mers made to span a carboxyl fragment of the Escherichia coli OmpA protein. They indicate the reason why Ye-2 reacts with both sets of peptides is because it has a preference for polymers of arginine.
Yu
D T
DT
Department of Medicine, University of California, Los Angeles 90024-167022.
Hamachi
T
T
Hamachi
M
M
Tribbick
G
G
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000276:immunology; D004926:Escherichia coli; D015796:HLA-B27 Antigen / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis
D000911:Antibodies, Monoclonal; D001425:Bacterial Outer Membrane Proteins; D015796:HLA-B27 Antigen; D010455:Peptides