Accessory gene regulator protein A (AgrA)

Accessory gene regulator protein A (AgrA) is a DNA-binding response regulator that functions in the two-component Agr quorum-sensing system in Staphylococcus aureus and some other staphylococci[1][2][3][6][8][9]. It has an N-terminal CheY-like receiver domain and a C-terminal LytTR DNA-binding domain[1][3][5]. Upon receiving a phosphate from the sensor kinase AgrC in response to autoinducing peptide (AIP) signaling, phosphorylated AgrA dimerizes and binds to specific promoter regions (notably P2 and P3), activating transcription of genes, including those for toxins and other virulence factors[1][2][5]. AgrA is a key regulator of virulence, exoprotein synthesis, and stress responses in S. aureus, making it a validated but challenging target for antimicrobial drug development[3][4]. Small molecule inhibitors that target AgrA's DNA-binding activity have been reported in early-stage research[3]. AgrA's critical role in regulating pathogenicity links it to infection and virulence as disease roles, particularly in staphylococcal infections.

Other names

Accessory gene regulator ADNA-binding response regulator AgrA

Inhibition of DNA binding to prevent activation of quorum-sensing-regulated virulence genes [3]