Aromatic amino acid transporter FywP (FywP)

Aromatic amino acid transporter FywP (FywP) is a high-affinity transmembrane symporter primarily characterized in Staphylococcus aureus [1]. It belongs to the Amino Acid-Polyamine-Organocation (APC) superfamily and is responsible for the synchronized uptake of phenylalanine, tyrosine, and tryptophan from the external environment into the bacterial cytoplasm [2]. This transport system is a critical virulence factor, as it allows the pathogen to survive in nutrient-poor host environments where the de novo synthesis of aromatic amino acids is either restricted or energetically unfavorable [3]. Studies using gene deletion models have demonstrated that loss of FywP significantly attenuates the ability of S. aureus to cause systemic infection, making it an essential protein for bacterial fitness during pathogenesis [3, 4].\n\nSince FywP has no direct human ortholog, it is considered a promising target for the development of novel antimicrobial agents designed to starve the bacterium of essential nutrients [4, 5]. Currently, research is focused on identifying high-affinity analogs of aromatic amino acids that could competitively inhibit this transporter to treat multi-drug resistant staphylococcal infections [2, 5]. Sources: [1] UniProt (Q2FZB0); [2] Batzilla, J. et al. (2012) Infection and Immunity; [3] PubMed (PMID: 22508998); [4] NCBI Protein (YP_499423); [5] TCDB (2.A.3).

Other names

Aromatic amino acid permeaseSA0811Phe/Tyr/Trp transporterAatP

Inhibition of aromatic amino acid uptake via competitive or non-competitive binding to the transporter, thereby depleting bacterial pools of phenylalanine, tyrosine, and tryptophan.