Rabbit sucrase-isomaltase contains a functional intestinal receptor for Clostridium difficile toxin A.
Identifieur interne : 000740 ( Pmc/Checkpoint ); précédent : 000739; suivant : 000741Rabbit sucrase-isomaltase contains a functional intestinal receptor for Clostridium difficile toxin A.
Auteurs : C. Pothoulakis ; R J Gilbert ; C. Cladaras ; I. Castagliuolo ; G. Semenza ; Y. Hitti ; J S Montcrief ; J. Linevsky ; C P Kelly ; S. Nikulasson ; H P Desai ; T D Wilkins ; J T LamontSource :
- Journal of Clinical Investigation [ 0021-9738 ] ; 1996.
Abstract
The intestinal effects of Clostridium difficile toxin A are inidated by toxin binding to luminal enterocyte receptors. We reported previously that the rabbit ileal brush border (BB) 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 BB 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 BB. 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 ileal loops in vivo. Chinese hamster 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 binding domain of toxin A. These data suggest that toxin A binds specifically to carbohydrate domains on rabbit ileal SI, and that such binding is relevant to signal transduction mechanisms that mediate in vitro and in vivo toxicity.
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PubMed: 8698855
PubMed Central: 507473
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<author><name sortKey="Gilbert, R J" sort="Gilbert, R J" uniqKey="Gilbert R" first="R J" last="Gilbert">R J Gilbert</name>
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<front><div type="abstract" xml:lang="en"><p>The intestinal effects of Clostridium difficile toxin A are inidated by toxin binding to luminal enterocyte receptors. We reported previously that the rabbit ileal brush border (BB) 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 BB 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 BB. 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 ileal loops in vivo. Chinese hamster 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 binding domain of toxin A. These data suggest that toxin A binds specifically to carbohydrate domains on rabbit ileal SI, and that such binding is relevant to signal transduction mechanisms that mediate in vitro and in vivo toxicity.</p>
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<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Clin Invest</journal-id>
<journal-title>Journal of Clinical Investigation</journal-title>
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<article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject>
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<title-group><article-title>Rabbit sucrase-isomaltase contains a functional intestinal receptor for Clostridium difficile toxin A.</article-title>
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<contrib-group><contrib contrib-type="author"><name><surname>Pothoulakis</surname>
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<contrib contrib-type="author"><name><surname>Castagliuolo</surname>
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<contrib contrib-type="author"><name><surname>Semenza</surname>
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<contrib contrib-type="author"><name><surname>Nikulasson</surname>
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<aff>Section of Gastroenterology, Boston University School of Medicine, Massachusetts, USA.</aff>
<pub-date pub-type="ppub"><day>1</day>
<month>8</month>
<year>1996</year>
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<volume>98</volume>
<issue>3</issue>
<fpage>641</fpage>
<lpage>649</lpage>
<abstract><p>The intestinal effects of Clostridium difficile toxin A are inidated by toxin binding to luminal enterocyte receptors. We reported previously that the rabbit ileal brush border (BB) 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 BB 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 BB. 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 ileal loops in vivo. Chinese hamster 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 binding domain of toxin A. These data suggest that toxin A binds specifically to carbohydrate domains on rabbit ileal SI, and that such binding is relevant to signal transduction mechanisms that mediate in vitro and in vivo toxicity.</p>
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<tree><noCountry><name sortKey="Castagliuolo, I" sort="Castagliuolo, I" uniqKey="Castagliuolo I" first="I" last="Castagliuolo">I. Castagliuolo</name>
<name sortKey="Cladaras, C" sort="Cladaras, C" uniqKey="Cladaras C" first="C" last="Cladaras">C. Cladaras</name>
<name sortKey="Desai, H P" sort="Desai, H P" uniqKey="Desai H" first="H P" last="Desai">H P Desai</name>
<name sortKey="Gilbert, R J" sort="Gilbert, R J" uniqKey="Gilbert R" first="R J" last="Gilbert">R J Gilbert</name>
<name sortKey="Hitti, Y" sort="Hitti, Y" uniqKey="Hitti Y" first="Y" last="Hitti">Y. Hitti</name>
<name sortKey="Kelly, C P" sort="Kelly, C P" uniqKey="Kelly C" first="C P" last="Kelly">C P Kelly</name>
<name sortKey="Lamont, J T" sort="Lamont, J T" uniqKey="Lamont J" first="J T" last="Lamont">J T Lamont</name>
<name sortKey="Linevsky, J" sort="Linevsky, J" uniqKey="Linevsky J" first="J" last="Linevsky">J. Linevsky</name>
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<name sortKey="Pothoulakis, C" sort="Pothoulakis, C" uniqKey="Pothoulakis C" first="C" last="Pothoulakis">C. Pothoulakis</name>
<name sortKey="Semenza, G" sort="Semenza, G" uniqKey="Semenza G" first="G" last="Semenza">G. Semenza</name>
<name sortKey="Wilkins, T D" sort="Wilkins, T D" uniqKey="Wilkins T" first="T D" last="Wilkins">T D Wilkins</name>
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