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Escherichia coli O25b lipopolysaccharide (LPS) is a major surface glycolipid and primary virulence factor of the ST131-O25b:H4 lineage, a globally dominant multidrug-resistant clone responsible for severe extraintestinal infections (Nicolas-Chanoine et al., 2014, Clinical Microbiology Reviews). The LPS molecule is composed of a conserved lipid A moiety, a core oligosaccharide, and a variable O-antigen polysaccharide, which in this case is the O25b serotype (Poolman & Wacker, 2015, Journal of Infectious Diseases). This O-antigen serves as a protective shield against the host's innate immune system, specifically preventing complement-mediated lysis and phagocytosis. Because of its surface exposure and high prevalence in antibiotic-resistant uropathogenic E. coli (UPEC), the O25b LPS is a high-priority target for the development of glycoconjugate vaccines like ExPEC9V and monoclonal antibodies such as JNJ-63871860 (Frenck et al., 2019, The Lancet Infectious Diseases). These therapeutic interventions aim to facilitate opsonophagocytic killing of the bacteria, providing a narrow-spectrum, resistance-proof approach to treating and preventing urosepsis and other invasive ExPEC diseases (Guachalla et al., 2017, Antimicrobial Agents and Chemotherapy).
Induction of opsonophagocytic killing (OPK) and neutralization of bacterial virulence by targeting the O-specific polysaccharide chain of the lipopolysaccharide.
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