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Titolo:
RABBIT SUCRASE-ISOMALTASE CONTAINS A FUNCTIONAL INTESTINAL RECEPTOR FOR CLOSTRIDIUM-DIFFICILE TOXIN-A
Autore:
POTHOULAKIS C; GILBERT RJ; CLADARAS C; CASTAGLIUOLO I; SEMENZA G; HITTI Y; MONTCRIEF JS; LINEVSKY J; KELLY CP; NIKULASSON S; DESAI HP; WILKINS TD; LAMONT JT;
Indirizzi:
BETH ISRAEL HOSP,DIV GASTROENTEROL,DANA 501,330 BROOKLINE AVE BOSTON MA 02215 BOSTON UNIV,SCH MED,GASTROENTEROL SECT,EVANS MEM DEPT CLIN RES BOSTONMA 02118 BOSTON UNIV,SCH MED,MOL GENET SECT,EVANS MEM DEPT CLIN RES BOSTON MA 02118 BOSTON UNIV,SCH MED,DEPT PATHOL,EVANS MEM DEPT CLIN RES BOSTON MA 02118 ST ELIZABETHS HOSP BOSTON,GASTROENTEROL SECT BOSTON MA 00000 VIRGINIA POLYTECH INST & STATE UNIV,DEPT ANAEROB MICROBIOL BLACKSBURGVA 24061 WINTHROP UNIV HOSP,DIV GASTROENTEROL & NUTR MINEOLA NY 11501 ETH ZURICH,DEPT BIOCHEM CH-8092 ZURICH SWITZERLAND SUNY STONY BROOK STONY BROOK NY 11794
Titolo Testata:
The Journal of clinical investigation
fascicolo: 3, volume: 98, anno: 1996,
pagine: 641 - 649
SICI:
0021-9738(1996)98:3<641:RSCAFI>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYPT-VILLUS AXIS; HYGROMYCIN-B; G-PROTEIN; GENE-EXPRESSION; PERTUSSIS TOXIN; CHOLERA-TOXIN; RHO-PROTEINS; RAT ILEUM; CELLS; COMPLEX;
Keywords:
CLOSTRIDIUM DIFFICILE; ENTEROTOXIN; TOXIN RECEPTOR; SUCRASE-ISOMALTASE; LECTIN BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
C. Pothoulakis et al., "RABBIT SUCRASE-ISOMALTASE CONTAINS A FUNCTIONAL INTESTINAL RECEPTOR FOR CLOSTRIDIUM-DIFFICILE TOXIN-A", The Journal of clinical investigation, 98(3), 1996, pp. 641-649

Abstract

The intestinal effects of Clostridium difficile toxin A are initiatedby toxin binding to luminal enterocyte receptors. We reported previously that the rabbit heal brush border (BE) receptor is a glycoprotein with an alpha-d-galactose containing trisaccharide in the toxin-binding domain (1991. J. Clin. Invest. 88:119-125). In this study we characterized the rabbit ileal BE receptor for this toxin. Purified toxin receptor peptides of 19 and 24 amino acids showed 100% homology with rabbit sucrase-isomaltase (SI). Guinea pig receptor antiserum reacted in Western blots with rabbit SI and with the purified toxin receptor. Antireceptor IgG blocked in vitro binding of toxin A to rabbit ileal villus cell BE. Furthermore, anti-SI IgG inhibited toxin A-induced secretion (by 78.1%, P < 0.01), intestinal permeability (by 80.8%, P < 0.01), and histologic injury (P < 0.01) in rabbit deal loops in vivo. Chinesehamster ovary cells transfected with SI cDNA showed increased intracellular calcium increase in response to native toxin (holotoxin) or to a recombinant 873-amino acid peptide representing the receptor bindingdomain of toxin A. These data suggest that toxin A binds specificallyto carbohydrate domains on rabbit ileal SI, and that such binding is relevant to signal transduction mechanisms that mediate in vitro and in vivo toxicity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/06/20 alle ore 02:28:39