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Subversion of integrins by enteropathogenic Yersinia
1Howard Hughes Medical Institute and Dept Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA. ralph.isberg@tufts.edu
Journal of Cell Science
|December 12, 2000
Summary
Enteropathogenic Yersinia bacteria invade host cells by binding to integrin receptors on M cells via the invasin protein. This interaction facilitates bacterial translocation into deeper tissues, initiating infection.
Area of Science:
- Microbiology
- Immunology
- Cell Biology
Background:
- Enteropathogenic Yersinia are gram-negative bacteria capable of translocating from the intestine to deep tissues.
- These bacteria initiate infection by binding to host cell receptors.
Purpose of the Study:
- To elucidate the mechanism by which enteropathogenic Yersinia bind to host cells for invasion.
- To identify the key bacterial and host factors involved in early-stage disease.
Main Methods:
- Investigated the interaction between bacterial outer-membrane protein invasin and host cell integrin receptors.
- Analyzed the role of integrin-substrate affinity, concentration, and aggregation in bacterial uptake.
Main Results:
- Enteropathogenic Yersinia bind to integrin receptors on intestinal M cells using the invasin protein.
- Invasin exhibits high-affinity binding to multiple (beta)1 integrins.
- Bacterial internalization is influenced by receptor-ligand interaction dynamics.
Conclusions:
- The invasin-integrin interaction is critical for the initial adherence and entry of enteropathogenic Yersinia into host tissues.
- Understanding these early events is key to developing strategies against Yersinia infections.