Bacterial surface receptors on Staphylococcus aureus, Klebsiella pneumoniae, and Pseudomonas aeruginosa

Bacterial surface receptors on Staphylococcus aureus, Klebsiella pneumoniae, and Pseudomonas aeruginosa encompass a diverse array of proteins, polysaccharides, and lipids that serve as the primary interface between these pathogens and their environment [1, 6]. These structures, including penicillin-binding proteins (PBPs), outer membrane porins (e.g., OmpK36), and siderophore receptors (e.g., FpvA), are essential for nutrient acquisition, cell wall integrity, and environmental sensing [5, 8]. In clinical settings, these receptors are critical virulence factors that facilitate host cell adhesion and biofilm formation, contributing to the high pathogenicity of these ESKAPE organisms [2, 3]. They also play a central role in antibiotic resistance, either by limiting drug entry through porin loss or by actively expelling drugs via efflux pump components like OprM [1, 8]. These surface receptors are the primary targets for bacteriophage therapy, where viral receptor-binding proteins (RBPs) recognize specific motifs such as Type IV pili or wall teichoic acids to initiate infection [4, 6]. Therapeutic strategies often exploit these receptors to create evolutionary trade-offs; for instance, phages targeting efflux pump receptors can select for bacterial mutants that are more sensitive to traditional antibiotics [1, 5]. Additionally, specialized antibiotics like cefiderocol utilize siderophore receptors for active transport into the bacterial cell, bypassing traditional resistance mechanisms [8]. Understanding the structural diversity and mutational landscape of these receptors is vital for developing next-generation antimicrobials and personalized phage cocktails to combat multidrug-resistant infections [4, 7].

Other names

ESKAPE pathogen surface receptorsPhage receptorsBacterial cell surface targets

Bacteriophages bind to these receptors to initiate viral entry and subsequent bacterial lysis; certain antibiotics utilize these receptors for active transport into the cell or as binding sites to inhibit cell wall synthesis.