Abstract
The emergence and spread of pathogenic fungi resistant to currently used antifungal drugs represents a serious challenge for medicine and agriculture. The use of smart antimicrobials, so-called “dirty drugs” which affect multiple cellular targets, is one strategy to prevent resistance. Of special interest is the exploitation of the AFP family of antimicrobial peptides, which include its founding member AFP from Aspergillus giganteus. This latter is a highly potent inhibitor of chitin synthesis and affects plasma membrane integrity in many human and plant pathogenic fungi. A transcriptomic meta-analysis of the afp-encoding genes in A. giganteus and A. niger predicts a role for these proteins during asexual sporulation, autophagy, and nutrient recycling, suggesting that AFPs are molecules important for the survival of A. niger and A. giganteus under nutrient limitation. In this review, we discuss parallels which exist between AFPs and bacterial cannibal toxins and provide arguments that the primary function of AFPs could be to kill genetically identical siblings. We hope that this review inspires computational and experimental biologists studying alternative explanations for the nature and function of antimicrobial peptides beyond the general assumption that they are mere defense molecules to fight competitors.
Highlights
The antimicrobial peptide field is rapidly moving forward
We show that parallels exist to cannibal toxins in bacteria, and we will provide plausible plausible arguments that AFPs are important molecules for their hosts to ensure the survival of a subpopulation of its producing organism and, by this, survival of the whole species
Data on transcriptional regulation of antifungal peptides is available for only a few members of the AFP family: AFP (A. giganteus), PAF (P. chrysogenum), AnAFP (A. niger), and AFPB (P. digitatum)
Summary
The antimicrobial peptide field is rapidly moving forward. PubMed lists about 9000 publications for the year 2017 alone, and the Antimicrobial Peptide Database (APD, [1]) currently contains data on 2950 antimicrobial peptides (AMPs). The focus has been on two peptides—AFP from Aspergillus giganteus and PAF from Penicillium chrysogenum—as these peptides were the first studied and considered as interesting lead compounds for the development of novel antifungal drugs to combat against devastating fungal pathogens threatening human welfare and food security [5,8]. The last 10 years have witnessed an increasing interest in antifungal peptides of fungal origin Their mode of action on fungal strains including model strains and human and plant pathogens was. Microorganisms 2018, 6, 50 arguments that AFPs are important molecules for their hosts to ensure the survival of a subpopulation of its producing organism and, by this, survival of the whole species
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