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Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes
14:05

Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes

Published on: September 19, 2013

Listeria monocytogenes internalins bind to the human intestinal mucin MUC2

Sara K Lindén1, Hélène Bierne, Christophe Sabet

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

Archives of Microbiology
|March 11, 2008
PubMed

Insights

Listeria monocytogenes internalins InlB, InlC, and InlJ bind to MUC2, the main mucus component. This binding interaction is crucial for understanding how Listeria monocytogenes crosses the intestinal barrier.

Area of Science:

  • Microbiology
  • Immunology
  • Gastroenterology

Background:

  • Listeria monocytogenes is a pathogen that causes systemic infections by crossing the intestinal barrier.
  • Intestinal infection with L. monocytogenes leads to the release of intestinal mucus.
  • Mucus plays a critical role in host defense and pathogen interaction within the gut.

Purpose of the Study:

  • To investigate the interaction between L. monocytogenes internalins and intestinal mucus components.
  • To determine which L. monocytogenes internalins bind to MUC2, the major mucus protein.
  • To identify the specific domains of internalins responsible for MUC2 binding.

Main Methods:

  • In vitro binding assays were performed to assess the interaction between L. monocytogenes internalins (InlB, InlC, InlJ) and MUC2.
  • Binding affinities were quantified and compared between different internalins.
  • The internalin domain of InlJ was analyzed for its MUC2 binding capability.

Main Results:

  • Three L. monocytogenes internalins, InlB, InlC, and InlJ, demonstrated binding to MUC2.
  • No binding was observed between these internalins and the cell surface mucin MUC1.
  • The binding affinity followed the order InlB > InlC > InlJ.
  • The internalin domain of InlJ was sufficient for MUC2 binding.

Conclusions:

  • L. monocytogenes internalins exhibit specific binding to MUC2, a key component of the intestinal mucus layer.
  • This interaction suggests a mechanism by which L. monocytogenes may adhere to or traverse the intestinal mucus barrier.
  • The internalin domain is a critical functional unit for MUC2 interaction, potentially facilitating pathogen invasion.

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