| Title |
Ligand-Receptor Recognition for Activation of Quorum Sensing in Staphylococcus aureus |
| Author |
Li-Chun Chen, Li-Tse Tsou, and Feng-Jui Chen* |
| Address |
Division of Infectious Diseases, National Health Research Institutes, Zhunan Town, Miaoli County 350, Taiwan |
| Bibliography |
Journal of Microbiology, 47(5),572-581, 2009,
|
| DOI |
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| Key Words |
histidine protein kinases, ligands, protein structure, quorum sensing, transmembrane receptors, two-component system |
| Abstract |
The accessory gene regulator (agr) locus controls many of the virulence toxins involved in Staphylococcus aureus pathogenesis, and can be divided into four specificity groups. AgrC is the only group-specific receptor to mediate both intra-group activation and inter-group inhibition. We studied the ligand-receptor recognition of the agr system in depth by using a luciferase reporter system to identify the key residues responsible for AgrC activation in two closely related agr groups, AgrC-I, and AgrC-IV. Fusion PCR and site-directed mutagenesis were used to screen for functional residues of AgrC. Our data suggest that for AgrC-IV activation, residue 101 is critical for activating the receptor. In contrast, the key residues for the activation of AgrC-I are located at residues 49~59, 107, and 116. However, three residue changes, T101A, V107S, I116S, are sufficient to convert the AIP recognizing specificity from AgrC-IV to AgrC-I. |
