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Proteus mirabilis  is an important uropathogen, featured with urinary stone formation.  F ormate  h ydrogen l yase (FHL), consisting of formate dehydrogenase H and hydrogenase for converting proton to hydrogen, has been implicated in virulence. In this study, we investigated the role of  P. mirabilis  FHL hydrogenase and the FHL activator, FhlA . fhlA  and  hyfG  (encoding hydrogenase large subunit) displayed a defect in acid resistance.  fhlA  and  hyfG  mutants displayed a delay in medium deacidification compared to wild-type and  ureC  mutant failed to deacidify the medium. In addition, loss of  fhlA  or  hyfG  decreased urease activity in the pH range of 5–8. The reduction of urease activities in  fhlA  and  hyfG  mutants subsided gradually over the pH range and disappeared at pH 9. Furthermore, mutation of  fhlA  or  hyfG  resulted in a decrease in urinary stone formation in synthetic urine. These indicate  fhlA - and  hyf -mediated deacidification affected urease activity and stone formation .  Finally,  fhlA  and  hyfG  mutants exhibited attenuated colonization in mice .  Altogether, we found expression of  fhlA  and  hyf  confers medium deacidification via facilitating urease activity, thereby urinary stone formation and mouse colonization. The link of acid resistance to urease activity provides a potential strategy for counteracting urinary tract infections by  P. mirabilis .

Deacidification by FhlA-dependent hydrogenase is involved in urease activity and urinary stone formation in uropathogenic Proteus mirabilis