Abstract
Two novel antifungal proteins were purified and characterized from cheeseweed (Malva parviflora). Both proteins, designated CW-1 and CW-2, are composed of two different subunits of 5000 and 3000 Da, respectively. These proteins possess very potent antifungal activities, and more interestingly the inhibition is fungicidal instead of fungistatic. At low salt condition, the IC50 of CW-1 and CW-2 against Fusarium graminearum (Fg) is 2.5 ppm. At high salt condition which diminishes the antifungal activity of many antifungal proteins, both CW-1 and CW-2 still maintain potent activity against Fg with IC50 of 10 ppm.. The two subunits could be separated by gel filtration in the presence of 6 M urea, but their antifungal activity cannot be recovered after the removal of urea. Amino acid sequence analysis indicates that both subunits of CW-1 show homology to 2S albumin, whereas the two subunits of CW-2 have homology to vicilin protein from cotton. To our knowledge, this is the first report of isolation and characterization of heterologous antifungal proteins from any source.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
