Intrabacterial stability of IglA and IglB in strains of F. tularensis. The intrabacterial stability of IglB produced by LVS, the ΔiglA mutant, and the ΔiglA mutant complemented in trans (pJEB415) (upper panel) and the intrabacterial stability of IglA produced by LVS, the ΔiglB mutant, and the ΔiglB mutant complemented in trans (pJEB416) grown in Chamberlain's medium (lower panel) were examined. At time zero, chloramphenicol was added to stop protein synthesis. Samples of pelleted bacteria were taken at different times, and the amount of proteins was detected by Western blotting. The experiment was repeated at least two times, and the results of a representative experiment are shown. α-IglA, anti-IglA; α-IglB, anti-IglB.