Bioinformatics Analysis of Mycobacterium Tuberculosis Phage Protein
Objective:Bioinformatics software was used to predict the structure and function of Phage protein encoded by Mycobacterium tuberculosis Rv1579c gene.Methods:The amino acid sequence encoded by Rv1579c was obtained from the NCBI Gene database.The physicochemical properties,hydrophilicity,phosphorylation sites,transmembrane helical structure,secondary structure and tertiary structure of Phage protein were predicted and analyzed by ProtParam,Protscale,NetPhos,TMHMM,SOPMA,and SWISS-MODEL.IEDB,ABCpred,SYFPEITHI and other software were used to predict the cellular epitopes of Phage protein.The BLAST database,UniProt database and MEGA-X software were used to analyze the homology of Phage protein and the construction of phylogenetic tree.The STING database predicts its interacting proteins.Results:Phage protein contains a total of 104 amino acids,the molecular formula is C480H750N140O164S4,the total number of atoms is 1 538,it is a hydrophilic protein,the highest hydrophobic score of amino acid in the 22nd,23rd position is-1.433,and the highest amino acid hydrophilic score is-2.511 in the 94th amino acid.The instability index of the protein is 42.81,which is an unstable protein,no glycosylation sites,contains 12 phosphorylation sites,and has no transmembrane helix structure.In addition,Phage proteins obtained a total of multiple dominant cellular epitopes.Conclusion:Bioinformatics analysis showed that Phage protein was a hydrophilic unstable protein in the cell membrane of Mycobacterium tuberculosis,which mediated the occurrence of pyroptosis and drug resistance in Mycobacterium tuberculosis.At the same time,multiple dominant cellular epitopes of this protein can become new targets for the diagnosis and treatment of tuberculosis in the future.
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