Abstract

Burkholderia pseudomallei (B. pseudomallei), the etiological agent of melioidosis, is present in the water and soil of equatorial and subtropical climates worldwide. Melioidosis occurs after environmental exposure to B. pseudomallei and is linked to comorbidities that impair the immune response, including diabetes, as well as socioeconomic hardship. This study aims to characterize and describe the functional annotation of the hypothetical protein of B. pseudomallei. The physicochemical properties determined the protein’s theoretical pI, estimated half-life in different media, and the negative hydropathicity of the selected protein. The subcellular identification determined that the protein was in the extracellular location with no transmembrane helices. The protein contained a functional domain associated with the aldose 1-epimerase superfamily that is related to carbohydrate metabolism. The protein-protein interaction network identified the protein’s correlation with 10 interacting proteins. The secondary structural documentation revealed that the protein contains mostly random coils, followed by extended strands and alpha helices. The tertiary structure modeling and assessment uncovered that the protein’s structural properties were a significant number of residues in the most favored regions compared to other regions. This functional protein can be targeted for further study on potential drug and vaccine candidates against the protein of B. pseudomallei.

Key words: Burkholderia pseudomallei; Hypothetical protein AAFM48_25015; Melioidosis; In silico characterization; 3D structure modeling; Structural and Functional analysis.