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d glucosamine/gin diare

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Bovine septicemic Escherichia coli 31A agglutinates bovine, rabbit, and human erythrocytes and adheres in vitro to the brush border of bovine or ovine intestinal epithelial cells and to the human colon carcinoma Caco-2 cell line. The adhesion and hemagglutination of E. coli 31A are mediated by a
The binding of ShigeUa dysenteriae 1 cytotoxin to HeLa cells in culture and to isolated rat liver cell membranes was studied by means of an indirect consumption assay of toxicity from the medium, or by determination of cytotoxicity to the HeLa cell monolayer. Both liver cell membranes and HeLa cells

The structural basis of receptor-binding by Escherichia coli associated with diarrhea and septicemia.

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GafD in Escherichia coli G (F17) fimbriae is associated with diarrheal disease, and the structure of the ligand-binding domain, GafD1-178, has been determined at 1.7A resolution in the presence of the receptor sugar N-acetyl-D-glucosamine. The overall fold is a beta-barrel jelly-roll fold. The
Pathogenic mechanisms in infectious diseases often involve specific receptor-ligand interactions of cells and soluble molecules. To further elucidate structure-function relations for shigella toxin receptors, we studied binding of purified 125I-labeled toxin and biologic response under various

Aspartylglucosaminuria in a Canadian family.

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Aspartylglucosaminuria (McKusick 208400) is a lysosomopathy associated with aspartylglucosaminidase (L-aspartamido-beta-N-acetylglucosamine amidohydrolase, EC 3.5.1.26) deficiency. It has been most frequently encountered in Finland, where the regional incidence may be as high as 1 in 3600 births. In
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