Some lectins like WGA, which detects chitin (and other carbohydrate polymers), are used as versatile probes for detecting glycoconjugates in histochemical and flow cytometric applications and for localizing glycoproteins in gels. So far, none of the lectins characterised bind specifically to β-1,6-glycosidic bounds. Therefore, FGB1 is a valuable tool to study fungal and oomycete cell wall development and composition.
As FGB1 represents a tool to detect the presence of microbes in complex mixtures, it could also function for the diagnosis of human infections caused by fungal and oomycete pathogens.
In addition, the biochemical properties of FGB1 suggest that it could be an ideal platform to engineer molecules with specific and novel carbohydrate binding properties.
It is imaginable that a fusion protein of FGB1 and a fungicide would significantly increase the effect of such fungicide as it would stick the effector to the microbe.
- β-1,6-glucan is an important fungal MAMP
- Easy detection of microbes and glucans containing β1,6 glycosidic linkages in complex mixtures
- Useful as a research tool for histochemical and flow cytometric applications and for localizing glycoproteins
- Useful for medical diagnostic purposes
- Fusion proteins might be useful in medical or agricultural applications
- Easy application
The detection of β-1,6-glycosidic bounds with a conjugate of FGB1 and a detectable label has successfully been tested on different types of fungi in a variety of complex samples.
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Fesel, P. and Zuccaro, A. (2016) β-glucan: Crucial component of the fungal cell wall and elusive MAMP in plants. Fungal Genetics and Biology. 90, 53-60
Wawra, S. et al (2016) The novel fungal specific β-glucan binding lectin FGB1 alters susceptibility to cell wall stress and prevents glucan-triggered immunity in plants. Nature Communications. 13188, DOI: 10.1038