| Literature DB >> 6150011 |
H Smit, W Gaastra, J P Kamerling, J F Vliegenthart, F K de Graaf.
Abstract
The erythrocyte receptor for Escherichia coli K99 fimbrial adhesin was isolated from equine erythrocytes and characterized as Neu5Gc-alpha(2----3)-Galp-beta(1----4)-GLcp-beta(1----1)-Ceramide. This glycolipid acted as the receptor for K99 by four different experimental approaches: inhibition of equine erythrocyte hemagglutination by preincubation of K99-positive bacteria or purified K99 fimbriae with the isolated glycolipid; inhibition of attachment of K99-positive bacteria to porcine intestinal epithelial cells in the presence of the isolated glycolipid; induction of binding of K99-positive bacteria or purified K99 fimbriae to normally unreactive guinea pig erythrocytes by coating these cells with the isolated glycolipid; and isolation of the receptor by affinity chromatography with K99 coupled to CNBr-activated Sepharose 4B, indicating a strong interaction between K99 and the isolated glycolipid.Entities:
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Year: 1984 PMID: 6150011 PMCID: PMC261574 DOI: 10.1128/iai.46.2.578-584.1984
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441