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Campylobacter protein glycosylation affects host cell interactions
Christine M Szymanski1, Donald H Burr, Patricia Guerry
1Enteric Diseases Program, Naval Medical Research Center, Silver Spring, Marland 20910-7500, USA.
Infection and Immunity
|March 16, 2002
Summary
Campylobacter jejuni mutants lacking general protein glycosylation (pgl) had reduced adhesion and invasion of human intestinal cells. These pgl mutants also showed decreased colonization in a mouse intestinal model.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Molecular Biology
Background:
- Campylobacter jejuni is a leading cause of bacterial gastroenteritis worldwide.
- Protein glycosylation is a crucial post-translational modification in bacteria, affecting various cellular functions.
- The role of general protein glycosylation in C. jejuni virulence remains incompletely understood.
Purpose of the Study:
- To investigate the role of general protein glycosylation in Campylobacter jejuni virulence.
- To determine the impact of pgl mutations on bacterial adhesion, invasion, and intestinal colonization.
Main Methods:
- Construction and characterization of Campylobacter jejuni 81-176 pgl mutants.
- In vitro assays to assess bacterial adhesion to and invasion of INT407 human intestinal cells.
- In vivo colonization studies in a murine model of intestinal infection.
Main Results:
- Campylobacter jejuni pgl mutants exhibited significantly reduced adherence to INT407 cells compared to wild-type strains.
- Invasion of INT407 cells by pgl mutants was also markedly decreased.
- Colonization of the murine intestinal tract by pgl mutants was significantly impaired.
Conclusions:
- General protein glycosylation is essential for optimal Campylobacter jejuni virulence.
- Disruption of pgl genes attenuates C. jejuni's ability to interact with host cells and establish intestinal colonization.
- Targeting protein glycosylation pathways may represent a novel strategy for controlling C. jejuni infections.