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Escherichia coli surface receptors are a heterogeneous group of molecules, including adhesins (e.g., FimH), porins (e.g., OmpC, OmpF), and lipopolysaccharides (LPS), that reside on the bacterial outer membrane (Klemm et al., 2000). These receptors are essential for the bacteria's survival, facilitating nutrient uptake, environmental sensing, and adherence to host tissues, which is the critical first step in the pathogenesis of urinary tract infections and enteric diseases (Sokurenko et al., 1998). In pathogenic strains, specific receptors like FimH facilitate binding to the bladder epithelium, leading to colonization and subsequent infection. In the context of susceptibility, these surface structures serve as the primary docking sites for bacteriophages; for instance, the T4 phage utilizes LPS and OmpC for attachment (Bertozzi Silva et al., 2016). Therapeutic strategies targeting these receptors include anti-adhesion molecules like D-mannose or specific FimH inhibitors, which prevent colonization, and phage therapy, which exploits these receptors for viral entry and subsequent bacterial lysis. While promising, targeting these receptors faces challenges such as the rapid evolution of receptor-negative mutants and the high degree of structural variation across different E. coli strains (Labrie et al., 2010). Targeting these receptors offers a strategy to combat antibiotic-resistant strains by either preventing the initial stages of infection or providing a narrow-spectrum alternative to traditional antibiotics.
Therapeutic agents targeting these receptors function by competitively inhibiting bacterial attachment to host cells or by utilizing the receptors as entry points for bactericidal viral agents (phages) (Sokurenko et al., 1998; Bertozzi Silva et al., 2016).
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