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.
Abbreviations
- LRR:
-
Leucine-rich repeats
- Inl:
-
Internalin
- MucBP:
-
MUCin-binding protein
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Acknowledgments
We thank Edith Gouin for the gift of the purified InlC protein. The work was supported by a post doctoral Fellowship from the Swedish Society for Medical Research (S. Linden), a Queensland Cancer Fund Senior Research Fellowship (M. McGuckin) and the Australian NHMRC Project Grant No. 382309. C. Sabet received financial support from the FRM. P. Cossart is an international research scholar of the Howard Hughes Medical Institute.
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Communicated by Erko Stackebrandt.
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Lindén, S.K., Bierne, H., Sabet, C. et al. Listeria monocytogenes internalins bind to the human intestinal mucin MUC2. Arch Microbiol 190, 101–104 (2008). https://doi.org/10.1007/s00203-008-0358-6
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DOI: https://doi.org/10.1007/s00203-008-0358-6