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Evidence for a beta 1 integrin fibronectin receptor in Candida tropicalis
1Department of Pediatrics, University of Minnesota, Minneapolis, USA.
The Journal of Infectious Diseases
|July 1, 1996
Summary
Candida tropicalis binds to fibronectin via a receptor similar to the human integrin alpha 5 beta 1. This study identifies and characterizes this fungal fibronectin receptor.
Area of Science:
- Mycology
- Cell Biology
- Biochemistry
Background:
- Fungal adherence to host tissues is crucial for infection.
- Fibronectin (FN) is a key extracellular matrix protein involved in cell adhesion.
- Understanding fungal receptors for host proteins like FN is vital for developing anti-adhesion strategies.
Purpose of the Study:
- To characterize the fibronectin (FN) receptor on the surface of Candida tropicalis.
- To investigate the molecular nature and similarities of the C. tropicalis FN receptor to known vertebrate receptors.
Main Methods:
- Saturation analysis of FN binding to C. tropicalis cells.
- Inhibition assays using C. tropicalis cell membrane extracts.
- Immunoblotting and immunoprecipitation using purified FN and specific antibodies.
Main Results:
- FN binding to C. tropicalis was saturable, with a dissociation constant (Kd) of 2.3 x 10(-9) M and a receptor density of 854 receptors/cell.
- C. tropicalis cell membrane extracts significantly inhibited FN binding.
- A C. tropicalis membrane protein of approximately 125 kDa was recognized by antibodies against the human integrin alpha 5 beta 1 and the beta 1 integrin subunit.
Conclusions:
- Candida tropicalis possesses a fibronectin receptor with functional and antigenic similarities to the vertebrate beta 1 integrin family.
- The identified receptor is a potential target for therapeutic interventions aimed at preventing C. tropicalis adhesion.