A heat shock operon in Coxiella burnetti produces a major antigen homologous to a protein in both mycobacteria and Escherichia coli

Cloning and Sequence Analysis of the 10 kDa Antigen Gene of Mycobacterium tuberculosis

“…The sequence should encode 99 amino acids, starting with alanine, corresponding to a protein of 10673 Da; this is in good agreement with previous estimates of 10 kDa (Minden et al, 1984) and 12 kDa (Engers et al, 1986). Homology was found between this protein and two heat-shock proteins (Baird et al, 1988), the groES protein of E. coli (Hemmingsen et al, 1988) and the htpA gene product of Coxiella burnetii (Vodkin & Williams, 1988). This finding suggests that 10 kDa heat-shock proteins are widely conserved amongst bacteria.…”

“…This finding suggests that 10 kDa heat-shock proteins are widely conserved amongst bacteria. Whilst the biological significance of such proteins in M. tuberculosis is still unknown, it has been shown in other organisms, including C. burnetii, that stress or heat will induce their production (Vodkin & Williams, 1988). As a potential candidate for a vaccine, highly conserved proteins might protect against a range of bacterial infections.…”

Yersinia enterocolitica immunodominant 60 kDa antigen, common to a broad range of bacteria, is a heat-shock protein

“…In addition, it stimulates the proliferation of T cells in immune mice, suggesting that it is likely to be involved in the development of cellmediated immunity (Kaufmann et al, 1987). In contrast, Willem et al (1985) suggested that arthritis was induced by a T-cell clone which recognized an epitope on the mycobacterial 65 kDa antigen.…”

Molecular cloning of a Coxiella burnetii gene encoding a macrophage infectivity potentiator (Mip) analogue

“…In addition, at 7 bases upstream of the ATG codon was a putative ribosome-binding site (RBS), AGGAGA (Shine & Dalgarno, 1975). At the 3' end of this sequence was a potential termination signal similar to those in the C. burnetii hptAB operon, the transposase gene and citrate synthase gene (Heinzen & Mallavia, 1987;Hoover et al, 1992;Vodkin & Williams, 1988). Computer analysis indicated it could form a stem-loop structure with a free energy of -41.5.…”