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The bacterial cell wall of oral bacteria is an essential, mesh-like structure primarily composed of peptidoglycan—a polymer of alternating N-acetylglucosamine and N-acetylmuramic acid sugars cross-linked by short peptides[1][4][7]. It provides mechanical strength, maintains cell shape, protects against osmotic lysis, and anchors surface-associated virulence factors. In Gram-positive oral bacteria (e.g., Streptococcus mutans), the cell wall is thick, includes teichoic acids, and is a key target for various antibiotics and antimicrobial peptides. In Gram-negative bacteria, the wall is thinner and supplemented by an outer membrane. Many traditional antibiotics (β-lactams, glycopeptides) and newer agents (specific peptides, bacteriocins, lysins) disrupt the cell wall in order to kill or inhibit bacteria. This strategy benefits from high selective toxicity since human cells lack equivalent structures, making the cell wall a classic and highly effective antimicrobial target[2][3][4][6][9].
Inhibition of peptidoglycan biosynthesis: block transpeptidation or transglycosylation enzymes (e.g., β-lactam antibiotics inhibit penicillin-binding proteins); Disruption of cell wall integrity: lytic enzymes (phage lysins), targeted peptides; Prevention of cell wall unit transport: bacitracin blocks lipid carrier recycling; Selective targeting/lysis: some STAMPs or engineered proteins
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