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Nepenthesins are categorized under the subfamily of the nepenthesin-like plant aspartic proteases (PAPs) that form a distinct group of atypical PAPs. This study describes the effect of nepenthesin 1 ( HvNEP-1 ) protease from barley ( Hordeum vulgare  L.) on fungal histidine acid phosphatase (HAP) phytase activity. Signal peptide lacking HvNEP-1 was expressed in  Pichia pastoris  and biochemically characterized. Recombinant HvNEP-1 (rHvNEP-1) strongly inhibited the activity of  Aspergillus  and  Fusarium  phytases, which are enzymes that release inorganic phosphorous from phytic acid. Moreover, rHvNEP-1 suppressed  in vitro  fungal growth and strongly reduced the production of mycotoxin, 15-acetyldeoxynivalenol (15-ADON), from  Fusarium graminearum . The quantitative PCR analysis of trichothecene biosynthesis genes ( TRI ) confirmed that rHvNEP-1 strongly repressed the expression of  TRI4 ,  TRI5 ,  TRI6 , and  TRI12  in  F .  graminearum . The co-incubation of rHvNEP-1 with recombinant  F. graminearum  (rFgPHY1) and  Fusarium culmorum  (FcPHY1) phytases induced substantial degradation of both  Fusarium  phytases, indicating that HvNEP-1-mediated proteolysis of the fungal phytases contributes to the HvNEP-1-based suppression of  Fusarium .

Barley Nepenthesin-Like Aspartic Protease HvNEP-1 Degrades Fusarium Phytase, Impairs Toxin Production, and Suppresses the Fungal Growth