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The amino‐terminal domain of the P‐pilus adhesin determines receptor specificity
Author(s) -
Haslam David B.,
Borén Thomas,
Falk Per,
Liver Dag,
Chou Amy,
Xu Zheng,
Normark Staffan
Publication year - 1994
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1994.tb02175.x
Subject(s) - pilus , bacterial adhesin , biology , escherichia coli , receptor , fusion protein , tropism , glycolipid , microbiology and biotechnology , biochemistry , recombinant dna , genetics , gene , virus
Summary 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.