Specific regions of adherence binding sites and epitopes of the P1 adhesin of were synthesised as octapeptides and used as targets in a modified enzyme-linked immunosorbent assay. Acute phase and convalescent sera from 10 patients with infection were tested for antibody reactivity to these octapeptides. In convalescent sera, antibody activities were directed against octapeptides of the epitope regions, whereas no antibody activity was found in acute or convalescent sera to octapeptides of adherence-mediating binding sites. The non-responsiveness to adherence-mediating binding sites could be explained partially from the results of cross-reactivity experiments with adherence-inhibiting anti-Pi adhesin monoclonal antibodies (MAbs). Two of these MAbs showed cross-reactions with intracellular antigens of eukaryotic cell lines in immunofluorescence microscopy experiments. The cross-reacting antigens were isolated and characterised as glyceraldehyde-3-phosphate dehydrogenase and 2-phospho-D-glycerate hydrolase. Antigenic mimicry of eukaryotic structures by functional sites of the P1 adhesin of may influence the pathogenesis of infection.


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