Metalloprotease genes ofTrichophyton mentagrophytesare important for pathogenicity

Metalloproteases (Mep) of the M36 family are important virulence factors for the host invasion by the dermatophyte Trichophyton mentagrophytes. Dermatophytes secrete keratinase to degrade human and animal keratin and invade the skin. In previous studies, primers designed from the MEP gene sequences of Aspergillus fumigatus and A. oryzae were used to amplify the MEP genes from T. mentagrophytes, and the five MEP genes (MEP1-MEP5) were expressed. Differences in the expression of these five MEP genes in different dermatophytes were observed in an in vitro protein induction study, indicating their different functions and proteolytic abilities. However, specific pathogenic functions and mechanisms of each of the metalloproteases, as well as differences in their proteolytic activities, remain uncertain. In the current study, Agrobacterium tumefaciens-mediated transformation (ATMT) was used to successfully transform five MEP genes, resulting in five MEP mutant strains. MEP3 showed strongest proteolytic activity, hair biodegradation ability, and animal pathogenicity among the mutant strains. The MEP4 and MEP5 mutants were the least pathogenic through the above tests. Therefore, we hypothesize that the MEP4 and MEP5 genes are most likely to significantly affect the pathogenicity of T. mentagrophytes.