Escherichia coli fimbriae recognizing sialyl galactosides.

Abstract:

:Fimbriae recognizing sialyl galactosides (S fimbriae) were purified from an Escherichia coli strain. The S fimbriae were morphologically identical to type 1 and P fimbriae of E. coli and showed a hemagglutination that was abolished when erythrocytes were treated with neuraminidase. Hemagglutination by the purified fimbriae was inhibited by orosomucoid but not by its desialylated derivative. Of the oligosaccharides tested, sialyl-(alpha 2-3)-lactose and sialyl-(alpha 2-3)-N-acetyllactosamine had the strongest inhibitory activities. It was concluded that S fimbriae have the strongest affinity for (alpha 2-3)-linked sialyl galactosides. In the enzyme-linked immunosorbent assay, the hyperimmune serum to the S fimbriae reacted strongly with the homologous antigen but not with type 1, P, or nonhemagglutinating KS71C fimbriae of E. coli. Analogously, the hyperimmune sera to the other E. coli fimbriae did not react with the purified S fimbriae. The immunoprecipitation assay showed that S fimbriae on different E. coli serotypes shared immunological cross-reactivity.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Korhonen TK,Väisänen-Rhen V,Rhen M,Pere A,Parkkinen J,Finne J

doi

10.1128/JB.159.2.762-766.1984

subject

Has Abstract

pub_date

1984-08-01 00:00:00

pages

762-6

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

159

pub_type

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