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Gram-negative bacterial surface glycans are complex carbohydrate structures, including lipopolysaccharides (LPS), capsular polysaccharides (CPS), and O-antigens, that constitute the outermost layer of the bacterial cell envelope. These molecules are essential for maintaining the structural integrity of the outer membrane and serve as a critical barrier against detergents, host complement systems, and various antibiotics. LPS, in particular, is a potent pyrogen and the primary driver of the inflammatory cascade that leads to sepsis and septic shock when released into the bloodstream. Because these glycans often exhibit high species or strain specificity, they are primary targets for the development of conjugate vaccines and monoclonal antibodies aimed at narrow-spectrum antimicrobial therapy. Drugs targeting these epitopes typically work by neutralizing the toxic Lipid A component of LPS, disrupting membrane stability, or marking the bacteria for destruction by the host immune system.
Binding and neutralization of endotoxin, disruption of the bacterial outer membrane, opsonization for phagocytosis, and inhibition of bacterial adhesion to host cells.
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