Fig 3.

Role of OMPs in mediating the binding of H. pylori to mucins. (A) Detection of H. pylori surface adhesins involved in mucin binding. Outer membrane protein fractions of H. pylori were prepared and were probed with biotinylated porcine stomach mucin. A protein of ∼80 kDa, corresponding to the expected size of the surface adhesin BabA, was detected in strains J99 and G27 but was absent from 26695 and from a babA knockout mutant of G27. (B) Binding of H. pylori strains to Lewis blood group antigen structures. Microarrays containing neoglyconjugate Lewis blood group antigen structures were probed with fluorescently labeled H. pylori organisms. The structures probed were Lewis^x-BSA (LexBSA), di-Lewis^x-aminophenylethyl-human serum albumin (DiLexHSA), tri-Lewis^x-HSA (TriLexHSA), 3′-sialyl-Lewis^x-BSA (SLexBSA), 3-sulfo-Lewis^x-BSA (3SuLexBSA), 6-sulfo-Lewis^x-BSA (6SuLexBSA), and lacto-N-difucohexaose I-BSA, (LNDHIBSA), which consists of Lewis^b tetrasaccharide and lactose and is used as a Lewis^b active structure in immunochemical and functional inhibition studies. Shown are histograms representing the mean fluorescence intensities from three replicate microarray slides of H. pylori strains binding to printed neoglycoconjugates. The dashed line marks the level of marginal or background binding. Error bars represent the standard deviations of the means for three replicate microarray slides.