Peptidoglycan of Gram-positive bacterial cell wall (null)

Peptidoglycan is a major, essential structural polymer forming the thick cell wall layer characteristic of Gram-positive bacteria, sometimes comprising up to 40 layers and up to 20% of the cell wall dry weight[1][6]. It is composed of alternating glycan chains of N-acetylglucosamine and N-acetylmuramic acid, cross-linked by peptide chains, forming a rigid lattice[1][2]. This structure provides mechanical strength, protects against osmotic lysis, helps maintain cell morphology, and serves as a scaffold for cell envelope components[1][6]. Peptidoglycan synthesis and cross-linking are the targets of widely used antibacterial drugs, including β-lactams and glycopeptides, making it one of the most important and validated antibacterial targets in infectious disease pharmacology[5][7]. Modifications to peptidoglycan structure contribute to antibiotic resistance mechanisms in clinically important pathogens. The peptidoglycan of Gram-positive bacteria is notably thicker than that in Gram-negative bacteria, lacking an outer membrane[1][2].

Other names

Gram-positive cell wall peptidoglycanBacterial mureinGram-positive peptidoglycanCell wall peptidoglycan

Inhibition of transpeptidation/cross-linking of peptidoglycan strands (β-lactams like penicillins, cephalosporins, carbapenems, monobactams); Inhibition of peptidoglycan polymerization (glycopeptides like vancomycin bind D-Ala-D-Ala, blocking cross-linking); Inhibition of cell wall precursor synthesis/transport (bacitracin, fosfomycin)