ANTIBODIES TO ESCHERICHIA-COLI-06 PORINS CROSS-REACT WITH URINARY PATHOGENS

Antibodies to partially purified E. coli 06 35-40 KDa porin trimers re cognized the reactive epitopes in the intact porin surface molecule pr esent in various wild-type, heterologous, urinary pathogens. The prese nce of lipopolysaccharide in the membrane did not shield the antibody binding sites. The reactivity was shown to be specific for porins sinc e LPS-absorbed porin antisera reacted with porins on immunoblots and s howed no reactivity with LPS. Additionally, the cross-reactions were a bolished by absorption of the porin antisera with E. coil 06 containin g porin trimers. These data strengthen the rationale for exploring the enhancement of immunoprotection by monoclonal antibodies to specific immunoreactive antigens in the porin molecule.