AustralieFrV1, Main, Exploration, bibRecord, 008C16

Listeria monocytogenes internalins bind to the human intestinal mucin MUC2

Identifieur interne : 008C16 ( Main/Exploration ); précédent : 008C15; suivant : 008C17

Listeria monocytogenes internalins bind to the human intestinal mucin MUC2

Auteurs : Sara K. Linden [Australie] ; Hélène Bierne [France] ; Christophe Sabet [France] ; Chin Wen Png [Australie] ; Timothy H. Florin [Australie] ; Michael A. Mcguckin [Australie] ; Pascale Cossart [France]

Source :

Archives of microbiology [ 0302-8933 ] ; 2008.

RBID : Pascal:08-0348894

Descripteurs français

Pascal (Inist)
- Listeria monocytogenes, Homme, Intestin, Mucine.
Wicri :
- topic : Homme.

English descriptors

KwdEn :
- Gut, Human, Listeria monocytogenes, Mucin.

Abstract

Listeria monocytogenes cross the intestinal barrier causing systemic infections with high mortality rates. Intestinal infection triggers release of intestinal mucus. We show that three L. monocytogenes internalins, InlB, InlC and InlJ all bound to MUC2 (the major component of intestinal mucus), but not to the cell surface mucin MUC1. Binding was strongest to InlB>InlC>InlJ (P < 0.001). Listerial internalins are characterized by their internalin domain, composed by leucine rich repeats (LRR) followed by an immunogloblin-like region. We report here that the internalin domain of the InlJ protein also bound MUC2, suggesting that an internalin domain is sufficient to bind to MUC2.

Affiliations:

Links toward previous steps (curation, corpus...)

to stream PascalFrancis, to step Corpus: 003422
to stream PascalFrancis, to step Curation: 002C27
to stream PascalFrancis, to step Checkpoint: 003101
to stream Main, to step Merge: 009515
to stream Main, to step Curation: 008C16

Le document en format XML

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<keywords scheme="Pascal" xml:lang="fr"><term>Listeria monocytogenes</term>
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<front><div type="abstract" xml:lang="en">Listeria monocytogenes cross the intestinal barrier causing systemic infections with high mortality rates. Intestinal infection triggers release of intestinal mucus. We show that three L. monocytogenes internalins, InlB, InlC and InlJ all bound to MUC2 (the major component of intestinal mucus), but not to the cell surface mucin MUC1. Binding was strongest to InlB>InlC>InlJ (P < 0.001). Listerial internalins are characterized by their internalin domain, composed by leucine rich repeats (LRR) followed by an immunogloblin-like region. We report here that the internalin domain of the InlJ protein also bound MUC2, suggesting that an internalin domain is sufficient to bind to MUC2.</div>
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   |wiki=    Wicri/Asie
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   |clé=     Pascal:08-0348894
   |texte=   Listeria monocytogenes internalins bind to the human intestinal mucin MUC2
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	Serveur d'exploration sur les relations entre la France et l'Australie
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Serveur d'exploration sur les relations entre la France et l'Australie

Listeria monocytogenes internalins bind to the human intestinal mucin MUC2

Listeria monocytogenes internalins bind to the human intestinal mucin MUC2

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