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Arch Microbiol. 2008 Jul;190(1):101-4. doi: 10.1007/s00203-008-0358-6. Epub 2008 Mar 8.

Listeria monocytogenes internalins bind to the human intestinal mucin MUC2.

Author information

1
Mucosal Diseases Program, Mater Medical Research Institute, Level 3 Aubigny Place, Raymond Terrace, South Brisbane, QLD, 4101, Australia. slinden@mmri.mater.org.au

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.

PMID:
18327567
DOI:
10.1007/s00203-008-0358-6
[Indexed for MEDLINE]

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