scholarly journals Characterization of the transcriptional response of Candida parapsilosis to the antifungal peptide MAF-1A

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e9767
Author(s):  
Rong Cheng ◽  
Wei Li ◽  
Klarke M. Sample ◽  
Qiang Xu ◽  
Lin Liu ◽  
...  

Candida parapsilosis is a major fungal pathogen that leads to sepsis. New and more effective antifungal agents are required due to the emergence of resistant fungal strains. MAF-1A is a cationic antifungal peptide isolated from Musca domestica that is effective against a variety of Candida species. However, the mechanism(s) of its antifungal activity remains undefined. Here, we used RNA-seq to identify differentially expressed genes (DEGs) in Candida parapsilosis following MAF-1A exposure. The early (6 h) response included 1,122 upregulated and 1,065 downregulated genes. Late (18 h) responses were associated with the increased expression of 101 genes and the decreased expression of 151 genes. Upon MAF-1A treatment for 18 h, 42 genes were upregulated and 25 genes were downregulated. KEGG enrichment showed that the DEGs in response to MAF-1A were mainly involved in amino acid synthesis and metabolism, oxidative phosphorylation, sterol synthesis, and apoptosis. These results indicate that MAF-1A exerts antifungal activity through interference with Candida parapsilosis cell membrane integrity and organelle function. This provides new insight into the interaction between Candida parapsilosis and this antimicrobial peptide and serves as a reference for future Candida parapsilosis therapies.

2019 ◽  
Author(s):  
Rong Cheng ◽  
Wei Li ◽  
Klarke M. Sample ◽  
Qiang Xu ◽  
Lin Liu ◽  
...  

Abstract Background Candida parapsilosis is a major fungal pathogen that can cause sepsis in man. Novel antifungal agents are urgently required due to the threat of resistance to current therapeutic strategies. MAF-1A is a novel cationic antimicrobial peptide isolated from Musca domestica and is effective against a variety of Candida species. However, its antifungal mechanism is still unclear. Here, RNA-seq was used to identify differentially expressed genes (DEGs) in Candida parapsilosis after MAF-1A exposure. And then, we want to understand how the antimicrobial peptide MAF-1A work as an antifungal agent. Results The early (6 hour) response included 1122 genes with increased expression and 1065 genes with decreased expression. The late (18 hour) response was associated with the increased expression of 101 genes and decreased expression of 151 genes. When treated with MAF-1A from six to 18 hours, 42 genes were no longer expressed at elevated levels, and 25 genes that had a decreased expression pattern were reversed and demonstrated an increased expression pattern. KEGG enrichment showed that the DEGs caused by MAF-1A mainly involved amino acid synthesis and metabolism, oxidative phosphorylation, sterol synthesis and apoptosis. Conclusion These results indicate that MAF-1A may have multiple downstream effects in Candida parapsilosis. MAF-1A may exert antifungal activity by interfering with Candida parapsilosis cell membrane integrity and the function of certain organelles.


2020 ◽  
Vol 61 (35) ◽  
pp. 152240
Author(s):  
Zilun Hu ◽  
Guoliang Lin ◽  
Matthew Sender ◽  
Kevin C. Cannon ◽  
Franklin A. Davis ◽  
...  

2019 ◽  
Vol 64 (1) ◽  
Author(s):  
Jiao Gong ◽  
Jun Wu ◽  
Melanie Ikeh ◽  
Li Tao ◽  
Yulong Zhang ◽  
...  

ABSTRACT Mammalian serum amyloid A (SAA) is a major acute phase protein that shows a massive increase in plasma concentration during inflammation. In the present study, we demonstrate that the expression of mouse SAA1 in serum was increased when infected with Candida albicans, a major human fungal pathogen, in a systemic infection model. We then set out to investigate the antifungal activity of SAA proteins against C. albicans. Recombinant human and mouse SAA1 (rhSAA1 and rmSAA1) were expressed and purified in Escherichia coli. Both rhSAA1 and rmSAA1 exhibited a potent antifungal activity against C. albicans. We further demonstrate that rhSAA1 binds to the cell surface of C. albicans, disrupts cell membrane integrity, and induces rapid fungal cell death in C. albicans. Our finding expands the known functions of SAA1 and provides new insight into host-Candida interactions during fungal infection.


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