Bioinformatic analysis and prokaryotic expression of FtnB protein from Salmonella typhimurium
Wei Mingqing
Ding Ying
Liu Feifan
Wang Tianchen
Zhou Xia
Zhang Qian
Wang Zhen
Zhang Hui
Abstract：The experiment aims to deeply study the potential biological functions of the FtnB protein of Salmonella typhimurium and obtain high-purity protein samples.The study utilized bioinformatics technology to predict and analyze the structure of FtnB protein and post-translational modification sites.The Salmonella typhimurium FtnB gene obtained by PCR amplification was inserted into the pET-32a(+)vector and transformed into the Escherichia coli BL21(DE3)expression strain.The expression level of FtnB protein was detected by SDS-PAGE and Western blotting methods.The results show that the FtnB protein is a hydrophilic protein and does not contain transmembrane structures or signal peptides.The secondary structures mainly include α-helices,random curls,β-folds and extended chains.There are multiple T and B cell antigenic epitopes,and modification sites of phosphorylation,glycosylation and methylation.According to the predictive analysis results of protein interactions,there are interactions between the FtnB protein and the norV and aphF proteins.The research successfully amplified the FtnB gene with a size of 524 bp.The FtnB protein with a size of approximately 35.9 ku was identified by SDS-PAGE and Western blotting.Studies have shown that the FtnB gene was successfully cloned in the experiment,and the FtnB protein was prepared through prokaryotic expression,providing a reference for further exploration of the functional study of the FtnB protein in Salmonella typhimurium.
Keywords：Salmonella typhimuriumBioinformatics analysisProkaryotic expression
Publication Date：2025-08-15
Online Publishing Date：2025-09-22(First online date of this platform, not the publication date of the document)
Pages：7( 7-13 )