PubMed · 2862034
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M J Harber. 1985. Bacterial adherence.. https://doi.org/10.1007/bf02013648
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Human urinary tract infection is an infectious disease that depends on a series of host-microbial interactions. The bacteria first colonize the colon and then the periurethral/vaginal areas; they ascend to and infect first the bladder and then the kidneys. Expression of Escherichia coli P-fimbriae constitutes the strongest correlation to renal pathogenicity, but is also related to first-time cystitis in children. The role of P-fimbriae in the preceding steps in the infectious process is unknown. To examine this, we constructed, from a P-fimbriated E. coli strain with a class II G-adhesin preferentially binding to globoside, one isogenic mutant lacking the G-adhesin and another isogenic mutant in which we replaced the papG class II allele with a class III adhesin preferentially binding to the Forssman antigen. We report here the comparison of the adhesin knockout mutant (DS17-8) and the class-switch mutant (DS17-1) with the wild-type (DS17) for in vivo colonization of the gut, vagina, and bladder of cynomolgus monkeys. It was recently shown that the class II tip G-adhesin is a prerequisite for acute pyelonephritis to occur in the monkey model in the absence of other kidney-specific adhesins or obstruction of the urinary flow. Here we show that it is not required for bladder infection but gives a competitive advantage in mixed infections. In the vagina and colon, the G-adhesin gives no competitive advantage.
The conformation and thermodynamic stability of the four polymeric carbohydrate-specific bacterial recognition proteins K88ab, AFA-1, NFA-1, and CFA-1 and their monomeric subunits that can be obtained by variation of pH were studied by infrared spectroscopy and differential scanning microcalorimetry. For NFA-1, a pH-dependent dissociation of the polymeric form cannot be achieved due to the stronger interactions of the neighboring subunits. Generally, no alterations in secondary structure are observed between the monomeric and the polymeric proteins. All adhesins reveal a high degree of beta-sheet structure (40-55%), while the alpha-helix component is of minor importance (10-20%). The adhesins investigated in this study revealed unusually high denaturation temperatures (69-104 degrees C) and stabilizing Gibbs energies, delta G (40-125 kJ/mol), compared to common globular proteins. Statistical deconvolution of the DSC curves yields a two-state transition of K88ab, NFA-1, and the monomeric CFA-1 and the existence of intermediate states for AFA-1 and polymeric CFA-1 during the denaturation process. The irreversible denaturation of K88ab, AFA-1, and CFA-1 is explained by aggregation of the polypeptide chains forming a three-dimensional network of intermolecular beta-sheet-type structures. In contrast, denaturation of NFA-1 is completely reversible. At a physiologically relevant temperature of approximately 40 degrees C, we observe predenaturational events in the DSC curves of polymeric K88ab and NFA-1 with no concomittant changes in the secondary structure of these proteins.
We investigated the hemolytic activity of Escherichia coli strain EC901 carrying plasmid pBJN406 containing genes draA-E involved in expression of the mannose-resistant Dr hemagglutinin, and in its isogenic insertion mutants devised with Tn5, Tn3, and TnphoA. While E. coli BN406 displayed rapid hemolytic activity against equine erythrocytes, insertion mutations in draD and draE, but not in draA, draB, and draC, abolished all hemolytic activity. These data suggest a role for draD and draE in the expression of hemolysis.