Polyphenol–protein interactions (Short Communication)

The association of some natural and synthetic polyphenols with beta-glucosidase was examined and some observations on the chemical nature of the complex were made.     

Enhancing river vegetation: conservation, development and restoration

The welcome increase in projects increasing river vegetation prompts theoretical consideration. To restore is to bring back what was there before — but at what period? 1860 to 1940 is suggested, as ‘traditional’. Traditional rivers differ greatly between river types and between rivers: in water, structural and biotic characters, and Sense of Place. Aiming at these, holistically, is aiming at restoration. Aiming at part, or trying to convert rivers to a Standard Recommended river is, at best, enhancement. The latter development lessens the unique variety and special features of rivers that are the heritage of each country.     

The amino-terminal domain of the P-pilus adhesin determines receptor specificity

Pyelonephritic isolates of Escherichia coli commonly express P-pili, which mediate bacterial attachment to glycolipids on epithelial cell surfaces. Three classes of P-pili have been defined, based on varying specificity for galabiose-containing glycolipids. Variation in adhesive capacity is correlated with a shift in preferred host, suggesting that host tropism depends largely on detailed specificity for the globoseries glycolipids. In this study we examined the importance of the PapG adhesin in determining receptor specificity. Translational fusions were constructed between the ammo-terminus of the PapG adhesin from each of the three pilus classes and a reporter protein. The binding specificity of the purified fusion proteins in vitro was identical to that seen with whole bacteria. Adherence of intact bacteria to cultured kidney cells was markedly reduced by a monoclonal antibody specific for the Class III adhesin (previously denoted PrsG), confirming the importance of the ammo-terminus of PapG in mediating attachment to a receptor when presented on the eukaryotic cell surface. These results suggest that the detailed receptor specificity resides solely within the amino-terminus of the PapG adhesin and is independent of the complex pilus architecture.