Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001511 (Adhesion)
5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The aim of this study was to characterize the Escherichia coli K88-specific receptors in mucus from the small intestines of 35-day-old piglets with the isogenic strains E. coli K-12(pMK005) (K88+) and E. coli K-12(pMK002) (K88-). These strains differed only in that the latter one cannot produce intact K88 fimbriae because of a deletion in the gene coding for the major fimbrial subunit. Adhesion was studied by incubating 3H-labeled bacteria with crude mucus, pronase-treated whole mucus, mucus fractionated by gel filtration, delipidated mucus, or extracted lipids immobilized in microtiter wells. In addition, E. coli strains were tested for adhesion to glycolipids extracted from mucus by overlaying glycolipid chromatograms with 125I-labeled bacteria. The recently reported finding that K88 fimbriae bind to glycoproteins in mucus from the piglet small intestine was confirmed in two ways. Pronase treatment of immobilized mucus reduced adhesion by 82%, and adhesion to delipidated mucus was 14 times greater for the K88+ than for the K88- strain. E. coli K88+ adhered to several of the fractions collected after gel filtration of crude mucus, including the void volume (M(r), > 250,000). Receptor activity specific for the K88 fimbriae was demonstrated in the lipids extracted from mucus, as the neutral lipids contained six times as much receptor activity as the acidic lipid fraction. Specificity was confirmed by demonstrating that adhesion to the total lipids could be inhibited by pretreatment of the immobilized lipids with K88 fimbriae. Relative to K-12 (K88-), the K-12 (K88+) bacterial cells bound more avidly to galactosylceramide when the neutral lipids were separated on thin-layer chromatography plates. No adhesion to lipids in the acidic fraction separated on thin-layer plates was detected. Relative to adhesion of K-12 (K88-), adhesion of K-12 (K88+) to commercially available galactosylceramide immobilized in microtiter wells confirmed the results with the thin-layer plates. It can be concluded that 35-day-old piglet mucus contains both protein and glycolipid receptors specific for K88 fimbriae, the latter being galactosylceramide.
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PMID:Piglet ileal mucus contains protein and glycolipid (galactosylceramide) receptors specific for Escherichia coli K88 fimbriae. 809 67

Adhesion of conidia of the endoparasitic fungus Drechmeria coniospora to the cuticles of the wild type and four different head defective mutants of Caenorhabditis elegans, and subsequent infection, was studied. The conidia adhered around the sensory structures in the head region, vulva, and occasionally to other parts of the cuticle in both mutant and wild type hosts. Infection took place after adhesion to the head region by penetration through the cuticle, and, following adhesion around the vulva, through the natural orifice. Infection was not observed after adhesion to other parts of the cuticle. Adhesion was reduced after treatment of the nematodes with Pronase E. Adhesion returned towards normal again within 2 hours, indicating that the proteinaceous material emanating from the sensory structures was rapidly replaced.
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PMID:Adhesion of Conidia of Drechmeria coniospora to Caenorhabditis elegans Wild Type and Mutants. 1927 12