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Updated: Apr 3, 2026

Biomimetic Materials to Characterize Bacteria-host Interactions
Published on: November 16, 2015
A novel adhesive factor contributing to the virulence of Vibrio parahaemolyticus
Ming Liu1,2, Sheng Chen1,2
1Shenzhen Key Lab for Food Biological Safety Control, Food Safety and Technology Research Center, Hong Kong PolyU Shenzhen Research Institute, Shenzhen, China.
Abstract:
Bacterial adhesins play a pivotal role in the tight bacteria-host cells attachment to initiate the downstream processes and bacterial infection of hosts. In this study, we identified a novel adhesin, VpadF in V. parahaemolyticus. Deletion of VpadF in V. parahaemolyticus markedly impaired its attachment and cytotoxicity to epithelial cells, as well as attenuated the virulence in murine model. Biochemical studies revealed that VpadF recognized both fibronectin and fibrinogen. The binding of VpadF to these two host receptors was mainly dependent on the its fifth bacterial immunoglobulin-like group domain and its C-terminal tail. Our finding suggested that VpadF is a major virulence factor of V. parahaemolyticus and a potential good candidate for V. parahaemolyticus infection control for both vaccine development and drug target.
Insights
Researchers discovered VpadF, a novel bacterial adhesin in Vibrio parahaemolyticus. This adhesin is crucial for bacterial attachment, host cell damage, and overall virulence, offering potential targets for infection control.
Area of Science:
- Microbiology
- Molecular Biology
- Infectious Diseases
Background:
- Bacterial adhesins are key to host cell attachment and infection.
- Vibrio parahaemolyticus is a significant human pathogen.
Purpose of the Study:
- To identify and characterize novel adhesins in Vibrio parahaemolyticus.
- To investigate the role of VpadF in bacterial virulence and host interaction.
Main Methods:
- Genetic deletion of the VpadF gene in V. parahaemolyticus.
- Assays for bacterial attachment and cytotoxicity to epithelial cells.
- Murine model of infection to assess virulence.
- Biochemical analysis of VpadF-host receptor interactions.
Main Results:
- Deletion of VpadF significantly reduced bacterial attachment and cytotoxicity.
- VpadF deficiency attenuated V. parahaemolyticus virulence in a murine model.
- VpadF was found to bind fibronectin and fibrinogen, mediated by its fifth immunoglobulin-like domain and C-terminal tail.
Conclusions:
- VpadF is a major virulence factor for V. parahaemolyticus.
- VpadF represents a promising target for developing V. parahaemolyticus vaccines and therapeutics.
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