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Article

Antifungal Activity and Molecular Mechanisms of Partial Purified Antifungal Proteins from Rhinacanthus nasutus against Talaromyces marneffei

1
Department of Microbiology, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand
2
Department of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand
3
Molecular, Cellular and Developmental Biology, School of Biosciences, University of Melbourne, 3010 Victoria, Australia
4
Functional Ingredients and Food Innovation Research Group, National Center for Genetic Engineering and Biotechnology, Pathum Thani 12120, Thailand
*
Author to whom correspondence should be addressed.
J. Fungi 2020, 6(4), 333; https://doi.org/10.3390/jof6040333
Received: 23 November 2020 / Accepted: 1 December 2020 / Published: 3 December 2020
Antifungal proteins (AFPs) are able to inhibit a wide spectrum of fungi without significant toxicity to the hosts. This study examined the antifungal activity of AFPs isolated from a Thai medicinal plant, Rhinacanthus nasutus, against the human pathogenic fungus Talaromycesmarneffei. This dimorphic fungus causes systemic infections in immunocompromised individuals and is endemic in Southeast Asian countries. The R. nasutus crude protein extract inhibited the growth of T. marneffei. The anti-T. marneffei activity was completely lost when treated with proteinase K and pepsin, indicating that the antifungal activity was dependent on a protein component. The total protein extract from R. nasutus was partially purified by size fractionation to ≤10, 10–30, and ≥30 kDa fractions and tested for the minimal inhibitory concentration (MIC) and minimal fungicidal concentration (MFC). All fractions showed anti-T. marneffei activity with the MIC and MFC values of 32 to 128 μg/mL and >128 μg/mL, respectively. In order to determine the mechanism of inhibition, all fractions were tested with T. marneffei mutant strains affected in G-protein signaling and cell wall integrity pathways. The anti-T. marneffei activity of the 10–30 kDa fraction was abrogated by deletion of gasA and gasC, the genes encoding alpha subunits of heterotrimeric G-proteins, indicating that the inhibitory effect is related to intracellular signaling through G-proteins. The work demonstrates that antifungal proteins isolated from R. nasutus represent sources for novel drug development. View Full-Text
Keywords: antifungal protein; AFP; Talaromyces marneffei; Rhinacanthus nasutus; G-protein antifungal protein; AFP; Talaromyces marneffei; Rhinacanthus nasutus; G-protein
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MDPI and ACS Style

Jeenkeawpieam, J.; Yodkeeree, S.; Andrianopoulos, A.; Roytrakul, S.; Pongpom, M. Antifungal Activity and Molecular Mechanisms of Partial Purified Antifungal Proteins from Rhinacanthus nasutus against Talaromyces marneffei. J. Fungi 2020, 6, 333. https://doi.org/10.3390/jof6040333

AMA Style

Jeenkeawpieam J, Yodkeeree S, Andrianopoulos A, Roytrakul S, Pongpom M. Antifungal Activity and Molecular Mechanisms of Partial Purified Antifungal Proteins from Rhinacanthus nasutus against Talaromyces marneffei. Journal of Fungi. 2020; 6(4):333. https://doi.org/10.3390/jof6040333

Chicago/Turabian Style

Jeenkeawpieam, Juthatip, Supachai Yodkeeree, Alex Andrianopoulos, Sittiruk Roytrakul, and Monsicha Pongpom. 2020. "Antifungal Activity and Molecular Mechanisms of Partial Purified Antifungal Proteins from Rhinacanthus nasutus against Talaromyces marneffei" Journal of Fungi 6, no. 4: 333. https://doi.org/10.3390/jof6040333

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