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The pathogenic fungus  Histoplasma capsulatum  secretes dipeptidyl peptidase (Dpp) IV enzyme activity and has two putative  DPPIV  homologs ( HcDPPIVA  and  HcDPPIVB ). We previously showed that  HcDPPIVB  is the gene responsible for the majority of secreted DppIV activity in  H. capsulatum  culture supernatant, while we could not detect any functional contribution from  HcDPPIVA . In order to determine whether  HcDPPIVA  encodes a functional DppIV enzyme, we expressed  HcDPPIVA  in  Pichia pastoris  and purified the recombinant protein. The recombinant enzyme cleaved synthetic DppIV substrates and had similar biochemical properties to other described DppIV enzymes, with temperature and pH optima of 42°C and 8, respectively. Recombinant HcDppIVA cleaved the host immunoregulatory peptide substance P, indicating the enzyme has the potential to affect the immune response during infection. Expression of  HcDPPIVA  under heterologous regulatory sequences in  H. capsulatum  resulted in increased secreted DppIV activity, indicating that the encoded protein can be expressed and secreted by its native organism. However,  HcDPPIVA  was not required for virulence in a murine model of histoplasmosis. This work reports a fungal enzyme that can function to cleave the immunomodulatory host peptide substance P.

Histoplasma capsulatum Encodes a Dipeptidyl Peptidase Active against the Mammalian Immunoregulatory Peptide, Substance P