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Uropathogenic, Escherichia coli can express serologically identical pili of different receptor binding specificities
Author(s) -
Lund B.,
Marklund B.I.,
Strömberg N.,
Lindberg F.,
Karlsson K.A.,
Normark S.
Publication year - 1988
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.1365-2958.1988.tb00027.x
Subject(s) - pilus , bacterial adhesin , biology , escherichia coli , epitope , microbiology and biotechnology , gene cluster , complementation , agglutination (biology) , glycoconjugate , gene , fimbria , antigen , mutant , biochemistry , genetics
Summary Uropathogenic Escherichia coli frequently express P‐pilus adhesins that recognize Galα(1–4)Gal‐containing glycoconjugates. The P‐pilus adhesin of the, E. coli isolate J96 is encoded by the pap gene cluster and has been shown to agglutinate P 1 ‐erythrocytes. We now describe a novel gene cluster from J96, prs , which is responsible for the agglutination of sheep erythrocytes. The structurally related gene clusters both expressed pili exhibiting the F13 antigen. Analysis of mutants of cloned prs sequences, together with trans ‐complementation of pap and prs genes, identified the sheep‐specific adhesin as the 37‐kD PrsG protein. The prsG gene occupies the equivalent position in prs as occupied by papG , which specifies the Galeα(1–4)Gal‐specific adhesion of pap. PrsG was shown to be structurally distinct from PapG since PapG‐specific antiserum did not cross‐react with PrsG. Using a solid phase glycolipid receptor binding assay, PrsG was found to specify preferential binding to the Forssman antigen, a major constituent of sheep erythrocyte membranes. The binding epitope was identified as the GaINAcα(1–3)GaINAc moiety. This is the first direct evidence that serologically identical pili may present antigenically distinct adhesins, each capable of binding to a specific receptor.