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The Staphylococcus aureus KdpDE two-component system couples extracellular K+ sensing and Agr signaling to infection programming.


ABSTRACT: The Kdp system is widely distributed among bacteria. In Escherichia coli, the Kdp-ATPase is a high-affinity K+ uptake system and its expression is activated by the KdpDE two-component system in response to K+ limitation or salt stress. However, information about the role of this system in many bacteria still remains obscure. Here we demonstrate that KdpFABC in Staphylococcus aureus is not a major K+ transporter and that the main function of KdpDE is not associated with K+ transport but that instead it regulates transcription for a series of virulence factors through sensing external K+ concentrations, indicating that this bacterium might modulate its infectious status through sensing specific external K+ stimuli in different environments. Our results further reveal that S. aureus KdpDE is upregulated by the Agr/RNAIII system, which suggests that KdpDE may be an important virulence regulator coordinating the external K+ sensing and Agr signaling during pathogenesis in this bacterium.

SUBMITTER: Xue T 

PROVIDER: S-EPMC3125826 | biostudies-other | 2011 Jun

REPOSITORIES: biostudies-other

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The Staphylococcus aureus KdpDE two-component system couples extracellular K+ sensing and Agr signaling to infection programming.

Xue Ting T   You Yibo Y   Hong De D   Sun Haipeng H   Sun Baolin B  

Infection and immunity 20110321 6


The Kdp system is widely distributed among bacteria. In Escherichia coli, the Kdp-ATPase is a high-affinity K+ uptake system and its expression is activated by the KdpDE two-component system in response to K+ limitation or salt stress. However, information about the role of this system in many bacteria still remains obscure. Here we demonstrate that KdpFABC in Staphylococcus aureus is not a major K+ transporter and that the main function of KdpDE is not associated with K+ transport but that inst  ...[more]

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