This MedLibrary.org supplementary page on Peptidoglycan is provided directly from the open source Wikipedia as a service to our readers. Please see the note below on authorship of this content, as well as the Wikipedia usage guidelines. To search for other content from our encyclopedia supplement, please use the form below:
Related Sponsors
- Not to be confused with glycoprotein.
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 (cell-wall). The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid residues. 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. 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.[1]
The peptidoglycan layer is substantially thicker in Gram-positive bacteria (20 to 80 nm) than in Gram-negative bacteria (7 to 8 nm), 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]
Contents |
Antibiotic inhibition
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.[4] Mutations in transpeptidases that lead to reduced interactions with an antibiotic are a significant source of emerging antibiotic resistance.[5]
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.
Structure
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 mesodiaminopimelic acid in the case of E. coli (Gram negative) or L-alanine, D-glutamine, L-lysine, and D-alanine in the case of S. aureus (Gram positive). These amino acids do not occur in proteins and are thought to help protect against attacks by most peptidases (reference needed). Cross-linking between amino acids in different linear amino sugar chains by an enzyme known as transpeptidase result in a 3-dimensional structure that is strong and rigid. The specific amino acid sequence and molecular structure vary with the bacterial species.[6]
See also
References
- ^ Madigan M; Martinko J (editors). (2005). Brock Biology of Microorganisms, 11th ed., Prentice Hall. ISBN 0-13-144329-1.
- ^ a b Salton MRJ, Kim KS (1996). Structure. In: Baron's Medical Microbiology (Barron S et al, eds.), 4th ed., Univ of Texas Medical Branch. (via NCBI Bookshelf) ISBN 0-9631172-1-1.
- ^ Demchick PH and Koch AL (1996). "The permeability of the wall fabric of Escherichia coli and Bacillus subtilis". Journal of Bacteriology 178 (3): 768–73.[1]
- ^ Bauman, R. (2007). Microbiology with Diseases by Taxonomy. Benjamin Cummings. ISBN 0-8053-7679-8.
- ^ Spratt BG (1994). "Resistance to antibiotics mediated by target alterations". Science 264 (5157): 388–93. doi:. PMID 8153626.
- ^ Ryan KJ; Ray CG (editors) (2004). Sherris Medical Microbiology, 4th ed., McGraw Hill. ISBN 0-8385-8529-9.
External links
 |
This bacteria-related article is a stub. You can help Wikipedia by expanding it. |
 |
This cell biology article is a stub. You can help Wikipedia by expanding it. |
|
||||||||
Wikipedia content modification information:
- This page was last modified on 3 October 2008, at 03:16.
Wikipedia Authorship and Review
Wikipedia content provided here is not reviewed directly by MedLibrary.org. Wikipedia content is authored by an open community of volunteers and is not produced by or in any way affiliated with MedLibrary.org.
Wikipedia Usage Guidelines
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article on "Peptidoglycan".
The URL for this specific entry is:
All Wikipedia text is available under the terms of the GNU Free Documentation License. (See Copyrights for details). Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc.