Identification of a novel heat shock protein 33 of Pythium insidiosum from the first Chinese skin and subcutaneous Pythiosis

Abstract

ObjectiveTo predict and analyze the structure and function of heat shock protein 33 by bioinformatics analysis. MethodsThe physical and chemical properties, hydrophilicity (hydrophobicity), transmembrane structure, secondary and tertiary structure, subcellular localization, signal peptide and glycosylation, phosphorylation sites, B cell, helper T (Th) cell epitopes of Hsp protein isolated from Pythium insidiosum were analyzed by corresponding bioinformatics software. ResultsHsp33 was composed of 608 amino acids, and the molecular formula was C2182H3538N624O654S16. Hsp33 was a hydrophilic unstable protein. The protein had no transmembrane domain and signal peptide sequence. Subcellular localization analysis shows that the amino acid was a nuclear protein;α-helix, β-sheet, β-turn and random coil accounted for 43.59%, 14.47%, 5.26% and 36.68%, respectively. There were 14 glycosylation sites and 48 phosphorylation sites. It has T cell and B cell dominant epitopes. TLR9 had the best affinity to HSP33 based on its binding affinity. ConclusionThis study lays the foundation for future research on vaccine construct and also provides clues to explore the pathogenic mechanism of HSP33-TLR9 signal pathway for Pythium insidiosum.