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The lipoprotein encoded by the  Francisella tularensis subsp. tularensis  locus FTT1103 is essential for virulence; an FTT1103 deletion mutant is defective in uptake and intracellular survival, and mice survive high dose challenges of greater than 10 8  bacteria. This protein has two conserved domains; one is found in a class of virulence proteins called macrophage infectivity potentiator (Mip) proteins, and the other in oxidoreductase Disulfide Bond formation protein A (DsbA)-related proteins. We have designated the protein encoded by FTT1103 as FipB for   F rancisella   i nfectivity  p otentiator protein B. The locus FTT1102 ( fipA ), which is upstream of  fipB , also has similarity to same conserved Mip domain. Deletion and site-specific mutants of  fipA  and  fipB  were constructed in the Schu S4 strain, and characterized with respect to intracellular replication and  in vivo  virulence. A nonpolar  fipA  mutant demonstrated reduced survival in host cells, but was only slightly attenuated  in vivo . Although FipB protein was present in a  fipA  mutant, the abundance of the three isoforms of FipB was altered, suggesting that FipA has a role in post-translational modification of FipB. Similar to many DsbA homologues, FipB contains a cysteine-any amino acid-any amino acid-cysteine (CXXC) motif. This motif was found to be important for FipB's role in virulence; a deletion mutant complemented with a gene encoding a FipB protein in which the first cysteine was changed to an alanine residue (AXXC) failed to restore intracellular survival or  in vivo  virulence. Complementation with a gene that encoded a CXXA containing FipB protein was significantly defective in intracellular growth; however, only slightly attenuated  in vivo .

Requirement of the CXXC Motif of Novel Francisella Infectivity Potentiator Protein B FipB, and FipA in Virulence of F. tularensis subsp. tularensis