Identification of DHPS and DHFR of pythium insidiosum from the first Chinese skin and subcutaneous pythiosis

Based on our previous studies, it is speculated that DHPS and DHFR are potential targets for the treatment of pythiosis. The Physicochemical properties, hydrophilicity/hydrophobicity, subcellular localization, signal peptide, secondary structure, tertiary structure, phosphorylation site and glycosylation site of DHPS and DHFR were analyzed and predicted by online bioinformatics prediction software, and the evolutionary tree analysis was performed. Results: DHPS was an unstable hydrophobic protein and DHFR was an unstable hydrophilic protein. DHPS and DHFR protein were located in the extracellular membrane without transmembrane structure. They had no signal peptide and are presumed to be non-secretory proteins. The secondary structure contained α-helix, β-angle, extension chain and random curling elements. DHPS contained 30 phosphorylation sites and 4 glycosylation sites; DHFR contained 16 phosphorylation sites and 5 glycosylation sites. DHPS and DHFR protein respectively had 17 and 6 B-cell epitopes and respectively had 14 and 4 Th epitopes. There were respectively 5 detected structure-based blinding curpockets between DHPS and SMZ, DHFR and TMP. Conclusion: Maybe DHPS and DHFR were relatively conservative between oomycetes and are a new biomarker for the diagnosis and treatment of pythiosis.