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Updated: Oct 1, 2026

Invasion of Human Cells by a Bacterial Pathogen
Published on: March 21, 2011
Fibronectin attachment protein is necessary for efficient attachment and invasion of epithelial cells by
1Department of Veterinary Pathobiology, Purdue University, West Lafayette, Indiana 47907, USA.
Abstract:
Attachment and ingestion of Mycobacterium avium subsp. paratuberculosis by two epithelial cell lines were enhanced by soluble fibronectin (FN). Peptide blocking of the FN attachment protein (FAP-P) inhibited the internalization of M. avium subsp. paratuberculosis. Disruption of FAP-P expression significantly reduced attachment and ingestion of M. avium subsp. paratuberculosis by T-24 and Caco-2 cells. The results indicate that the interaction between FN and FAP-P facilitates attachment and internalization of M. avium subsp. paratuberculosis by epithelial cells.
Insights
Mycobacterium avium subsp. paratuberculosis attachment and ingestion by epithelial cells are enhanced by fibronectin (FN). Blocking the fibronectin attachment protein (FAP-P) significantly reduced bacterial entry, indicating FAP-P
Area of Science:
- Microbiology
- Cell Biology
- Immunology
Background:
- Mycobacterium avium subsp. paratuberculosis (MAP) is an important pathogen.
- Epithelial cells form a barrier against pathogens but can be entry points.
- Fibronectin (FN) is an extracellular matrix protein involved in cell adhesion and pathogen interactions.
Purpose of the Study:
- To investigate the role of fibronectin (FN) in the attachment and ingestion of Mycobacterium avium subsp. paratuberculosis (MAP) by epithelial cells.
- To determine the specific contribution of the FN attachment protein (FAP-P) in this interaction.
Main Methods:
- Utilized two epithelial cell lines (T-24 and Caco-2).
- Assessed the effect of soluble fibronectin (FN) on MAP attachment and ingestion.
- Employed peptide blocking of the FN attachment protein (FAP-P) and disruption of FAP-P expression to evaluate its role.
Main Results:
- Soluble fibronectin (FN) significantly enhanced the attachment and ingestion of MAP by epithelial cells.
- Peptide blocking of the FN attachment protein (FAP-P) effectively inhibited MAP internalization.
- Disruption of FAP-P expression markedly reduced both MAP attachment and ingestion by T-24 and Caco-2 cells.
Conclusions:
- The interaction between fibronectin (FN) and the FN attachment protein (FAP-P) is crucial for MAP attachment and entry into epithelial cells.
- FAP-P acts as a key mediator facilitating MAP's interaction with and invasion of host epithelial cells.
- Targeting the FN-FAP-P pathway could offer novel strategies for controlling MAP infections.
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