Structural and functional analysis of Rv1772 protein in Mycobacterium tuberculosis
Objective To analyze the structure and function of Rv1772 protein in Mycobacterium tuber-culosis(MTB).Methods Gene information for Rv1772 was obtained from the National Center for Biotechnol-ogy Information(NCBI).Bioinformatics tools were utilized to analyze the structure and function of Rv1772 protein.Results The Rv1772 protein had a relative molecular mass of 10 896.28 Da and consists of 103 amino acids.It exhibited a gravy index of 77.96 and an instability coefficient of 43.98(＞40).indicating it was an un-stable protein.The average hydrophilicity of Rv1772 was-0.105,with a solubility index of 0.49.The protein comprised only intracellular and extracellular domains,lacked transmembrane regions,suggesting it was a non-transmembrane protein.Rv1772 lacked a signal peptide[D value=0.112(＜0.45)],confirming its solu-bility and cytoplasmic localization.Rv1772 contained six serine phosphorylation sites and five threonine phos-phorylation sites,potentially involved in regulating signal transduction during MTB infection.The secondary structure of Rv1772 consisted of α-helix(52.43％),β-sheet(9.71％),β-turn(4.85％),and random coil(33.01％).It predominantly featured a-helical structures,suggesting multiple B-cell antigenic epitopes.Rv1772 harbored three IFN-γ-induced HTL antigenic epitopes,two dominant CTL antigenic epitopes,and one prominent linear B-cell antigenic epitope.It exhibited high homology with MTB proteins containing the AN-TAR domain.Rv1772 interacted with Rv1592c,Rv0340,efpA,kasA,fbpC,oxyR,Rv2242,iniB,ndh,and fadE24 proteins.Conclusion Rv1772 protein contains multiple potential dominant T-cell and B-cell antigenic epitopes,interacts with other proteins,and thus may serve as a promising antigen for tuberculosis vaccine de-velopment.
万方数据
维普
