Davis JW, Alozie S, Harris C, Kabir M, Mercedes A, Sapp S, Williams K; American Society for Microbiology. General Meeting.
Abstr Gen Meet Am Soc Microbiol. 1996 May 19-23; 285 (abstract no. G-18).
Bronx Community College-CUNY, Bronx, NY.
Antigen (molecular) mimicry has been hypothesized as a potential mechanism of pathogenesis in HLA-B27 associated diseases. Cross reactivity of anti-B27 monoclonal antibody (MAb H2B6) in Western blots of purified urease from Ureaplasma urealyticum implicates urease as an antigen mimic. However, synthetic peptides corresponding to putative epitopes on urease do not inhibit MAb H2B6 binding to transfected L-cells (B27+) as would be expected with an antigen mimic. Furthermore, no anti-urease antibodies have been detected in sera from patients with B27-associated disease. These data suggest that microbial urease is not an antigen mimic of HLA-B27. Other recent data indicate that urease-derived peptides enhance antibody binding to HLA-B27, suggesting that these peptides may influence binding/receptor sites. The observation of peptide-modulated enhancement of antibody binding may be significant to the hypothesis of an arthritogenic peptide functioning in the pathogenesis of B27-associated disease. The arthritogenicity of Ureaplasma urease and urease-derived peptides is presently under investigation.
Publication Types:
Keywords:
- Antibodies, Monoclonal
- Blotting, Western
- Epitopes
- HLA-B27 Antigen
- Humans
- Peptides
- Urease
- immunology
Other ID:
UI: 102222983
From Meeting Abstracts