Mycobacterium tuberculosis (Mtb) is known to be responsible for tuberculosis (TB), but the pathogenesis of this disease and the host defense mechanisms involved are, for the most part, poorly understood. In this study, we divided 30 male C57BL/6 mice into control and infection groups, and following injection with physiological saline or Mtb, respectively, euthanized five mice from each group on days 1, 3, and 7.
We constructed a Mycobacterium tuberculosis vector expressing CFP-10 and Rv2626c to examine the expression of these proteins in Escherichia coli as well as their immunoreactivity. The CFP-10 and Rv2626c genes were amplified from tuberculosis H37Rv genomic DNA using polymerase chain reaction. They were ligated into the expression vector PET30a and expressed in E. coli. Histidine tag nickel column chromatography was used to purify the recombinant protein. An enzyme-linked immunosorbent assay (ELISA) was used for detection. In our E.
We constructed a prokaryotic expression vector expressing the Mycobacterium tuberculosis protein TB16.3, as well as 3 other proteins, including TB15.3, CFP-10, and Rv2626C, which were purified and analyzed for their effectiveness as detection antibodies. The TB16.3 genes of M. tuberculosis H37Rv genomic DNA were amplified by polymerase chain reaction, inserted into the expression vector pET-30a, and expressed in Escherichia coli. An enzyme-linked immunosorbent assay was used to detect the 4 M. tuberculosis antibodies. Engineered E.