[Bioinformatics analysis of pathogenesis-associated protein Rv2387 in Mycobacterium tuberculosis]

Objective To predict and analyze the structure and function of the protein encoding the Mycobacterium tuberculosis (Mtb) Rv2387 gene by bioinformatics methods. Methods Basic information about the Rv2387 gene and the protein it encodes was obtained from the National Center for Biological Information (NCBI) database. Physicochemical properties and the hydrophilicity/hydrophobicity of proteins were predicted using ProtParam and ProtScale tools; TMHMM-2.0, SignalP-6.0, and ProtCompB were used to analyze the transmembrane regions, signal peptides, and subcellular localization of proteins; NetPhos-3.1, NetNGlyc-1.0, and YinOYang-1.2 were applied to predict the phosphorylation, N-glycosylation, and O-glycosylation sites of the protein; SOPMA and SWISS-MODEL were used to predict the protein's secondary and tertiary structures; IEDB Database and SYFPEITHI were applied to predict the protein's B-cell and T-cell dominant epitopes. The amino acid sequence of Rv2387 was compared by the Blast tool in NCBI, and the evolutionary tree was constructed by MEGA 11 software; protein interactions were predicted and analyzed by the STRING database. Results The Rv2387 gene is 1254 bp long and encodes 417 amino acids. Predictions show that the protein has eight open reading frames. The Rv2387 protein is a stable hydrophilic transmembrane protein with an isoelectric point of 5.39, no signal peptide, and subcellular localization at the cell membrane. The protein was predicted to have 27 amino acid phosphorylation sites, 3 N-glycosylation sites, and 41 O-glycosylation sites. The secondary structure consists of 47.96% α-helices, 4.80% β-turns, 35.25% irregular coils, and 11.99% extended strands. It contains several antigenic epitopes and interacts with proteins such as Rv2423, Rv2067c, eccD2, Rv3899c, and glnB. Conclusion Bioinformatics predicted that Rv2387 is a hydrophilic protein with multiple phosphorylation sites and the ability to interact with a variety of proteins. The presence of multiple T and B cell antigenic epitopes of this protein suggests that it could be a candidate antigen for Mtb vaccine, providing a new idea for Mtb therapy.