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Fungi and Water
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
Recently, a novel antibiotic called plectasin has been isolated from a fungus, the saprophytic ascomycete Pseudoplectania nigrella, also called ebony cup, hairy black cup, or black false plectania. The fungus P. nigrella is an inedible small black saprophytic ascomycete (about two cm) found on the floor of pine forests in Europe, North America, and other temperate countries (13). Plectasin is a peptide composed of 40 amino acids that fold into an α-β-β structure stabilized by three disulfide bonds (93). In vitro, plectasin was especially active against Gram-positive bacteria such as Streptococcus pneumoniae, including strains resistant to conventional antibiotics (13, 93). In vivo, plectasin showed extremely low toxicity in mice, and cured them of experimental peritonitis and pneumonia caused by S. pneumoniae as efficaciously as vancomycin and penicillin (13). Importantly, it does not show any cytotoxicity to mammalian cells such as murine L929 fibroblasts, human erythrocytes, and THP-1 monocytes (93). These findings show the therapeutic potential of plectasin as a novel source of antimicrobial agents (13, 93). Thus, plectasin is a potential alternative for conventional antibiotics, and is now being commercialized as antimicrobial.
Programmed cell death in human pathogenic fungi – a possible therapeutic target
Published in Expert Opinion on Therapeutic Targets, 2018
Éva Leiter, László Csernoch, István Pócsi
The relative shortage of the recently effective antimycotics can be overcome by the small molecular mass antimicrobial proteins. These proteins are highly stable; any resistance against them develops only rarely. They are easy to manufacture on a large scale, therefore can be good candidates for the treatment and prevention of various microbial infections. Unfortunately, some antimicrobial peptides/proteins have failed in preclinical and clinical trials due to their cytotoxicity and/or their immunogenicity [64,65]. Antimicrobial proteins can induce immune response by producing antidrug antibodies or by developing allergic reactions, e.g. erythema, urticaria [65,66]. For example, larger peptides can trigger immune response, like NZ2114, which is a derivative of plectasin [65]. Nevertheless, there are also good examples of such peptide/protein-based antimicrobials, which lack any toxic effects on various mammalian cells and tissues including cellular components of the immune system, which highly support their future applications even in human antifungal therapies [67–70]. Some of these peptides/proteins exert their antimycotic action via the induction of apoptosis [2]. Table 1, Figures 1, and 2 summarizes today’s knowledge on the mechanisms of the apoptosis-inducing effects of some well-studied antimicrobial proteins.