Abstract
The type-1 pilus of Escherichia coli is the prototype of this class of hair-like, multimeric adhesive organelles1,2. This pilus mediates adherence to mannose-containing receptors3 on mucosal epithelia and other cells4. The type-1 pilus, in one of several serological variants, is expressed by nearly all E. coli strains5,6, and its promotion of colonization by pathogenic bacteria and the protective effects of purified pilus vaccines suggest that it is important as a bacterial virulence factor5,7,8. Both the adhesive function and the serological variation of the type-1 pilus have been attributed to the thousand or so pilin protein monomers making up the pilus rods. This idea has been contradicted by our earlier observations on an E. coli strain expressing adhesion-defective pili9. More recent genetic evidence also indicates that auxiliary pilus proteins are required for adhesive function10,11. We report here the identification of three previously undetected integral minor proteins on the type-1 pilus, and show that one of them is the receptor-binding adhesin. This protein is antigenically conserved among strains with different pilin serotypes and is located at the pilus tip.
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Hanson, M., Brinton, C. Identification and characterization of E. coli type-1 pilus tip adhesion protein. Nature 332, 265–268 (1988). https://doi.org/10.1038/332265a0
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DOI: https://doi.org/10.1038/332265a0
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