Abstract

Staphylococcus aureus secretes numerous virulence factors that are necessary for infection and colonization. Secretion of virulence factors is dependent on an array of proteins, including chaperones, which help traffic proteins to the secretion machinery and fold proteins into their active confirmation. Keogh et al. (e00681-20) show that the chaperone trigger factor (TF) contributes to biofilm formation and cooperates with the chaperone PpiB. They demonstrate that a ppiB tig double mutant is attenuated for virulence in a systemic model of infection. This work establishes a role for TF in S. aureus and suggests cooperation between chaperone proteins in this bacterium.

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