Peptidoglycan, also known as murein, is a polymer consisting of sugars and amino acids that forms a mesh-like layer outside the plasma membrane of bacteria (but not Archaea), forming the cell wall. The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid. Attached to the N-acetylmuramic acid is a peptide chain of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. Some Archaea have a similar layer of pseudopeptidoglycan or pseudomurein, where the sugar residues are β-(1,3) linked N-acetylglycosamine and N-acetyltalosaminuronic acid. That is why the cell wall of Archaea is insensitive to lysozyme.[1] Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. A common misconception is that peptidoglycan gives the cell its shape; however, whereas peptidoglycan helps maintain the structure of the cell, it is actually the MreB protein that facilitates cell shape. Peptidoglycan is also involved in binary fission during bacterial cell reproduction
The peptidoglycan layer is substantially thicker in Gram-positive bacteria (20 to 80 nanometers) than in Gram-negative bacteria (7 to 8 nanometers), with the attachment of the S-layer. Peptidoglycan forms around 90% of the dry weight of Gram-positive bacteria but only 10% of Gram-negative strains. In Gram-positive strains, it is important in attachment roles and stereotyping purposes.[2] For both Gram-positive and Gram-negative bacteria, particles of approximately 2 nm can pass through the peptidoglycan.[3]
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The peptidoglycan layer in the bacterial cell wall is a crystal lattice structure formed from linear chains of two alternating amino sugars, namely N-acetylglucosamine (GlcNAc or NAG) and N-acetylmuramic acid (MurNAc or NAM). The alternating sugars are connected by a β-(1,4)-glycosidic bond. Each MurNAc is attached to a short (4- to 5-residue) amino acid chain, containing D-alanine, D-glutamic acid, and meso-diaminopimelic acid in the case of Escherichia coli (a Gram negative bacteria) or L-alanine, D-glutamine, L-lysine, and D-alanine in the case of Staphylococcus aureus (a Gram positive bacteria). These amino acids, except the L-amino acids, do not occur in proteins and are thought to help protect against attacks by most peptidases.
Cross-linking between amino acids in different linear amino sugar chains occurs with the help of the enzyme transpeptidase and results in a 3-dimensional structure that is strong and rigid. The specific amino acid sequence and molecular structure vary with the bacterial species.[4]
Some antibacterial drugs such as penicillin interfere with the production of peptidoglycan by binding to bacterial enzymes known as penicillin-binding proteins or transpeptidases[2]. Penicillin-binding proteins form the bonds between oligopeptide crosslinks in peptidoglycan. For a bacterial cell to reproduce through binary fission, more than a million peptidoglycan subunits (NAM-NAG+oligopeptide) must be attached to existing subunits.[5] Mutations in transpeptidases that lead to reduced interactions with an antibiotic are a significant source of emerging antibiotic resistance.[6]
Considered the human body's own antibiotic, lysozymes found in tears work by breaking the β-(1,4)-glycosidic bonds in peptidoglycan (see below) and thereby destroying many bacterial cells. Antibiotics such as penicillin commonly target bacterial cell wall formation (of which peptidoglycan is an important component) because animal cells do not have cell walls.
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