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

Abstract

Objective: To predict and analyze the structure and function of heat shock protein 33 by bioinformatics analysis. Methods: The 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. Results: Hsp33 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. Conclusion: This 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.