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Francisella tularensis , a highly infectious, intracellular bacterium possesses an atypical type VI secretion system (T6SS), which is essential for the virulence of the bacterium. Recent data suggest that the HSP100 family member, ClpB, is involved in T6SS disassembly in the subspecies  Francisella novicida . Here, we investigated the role of ClpB for the function of the T6SS and for phenotypic characteristics of the human pathogenic subspecies  holarctica  and  tularensis . The  ∆clpB  mutants of the human live vaccine strain, LVS, belonging to subspecies  holarctica , and the highly virulent SCHU S4 strain, belonging to subspecies  tularensis , both showed extreme susceptibility to heat shock and low pH, severely impaired type VI secretion (T6S), and significant, but impaired intracellular replication compared to the wild-type strains. Moreover, they showed essentially intact phagosomal escape. Infection of mice demonstrated that both Δ clpB  mutants were highly attenuated, but the SCHU S4 mutant showed more effective replication than the LVS strain. Collectively, our data demonstrate that ClpB performs multiple functions in the  F .  tularensis  subspecies  holarctica  and  tularensis  and its function is important for T6S, intracellular replication, and virulence.

ClpB mutants of Francisella tularensis subspecies holarctica and tularensis are defective for type VI secretion and intracellular replication