Literature DB >> 126547

Chemical structure of the peptidoglycan, its modifiability and relation to the biological activity.

K H Schleifer.   

Abstract

The peptidoglycan is a heteropolymer composed of polysaccharide chains which are cross-linked through short peptides. The polysaccharide moiety (glycan) is made up of beta-1,4 glycosidically linked N-acetylglucosamine and N-acylmuramic acid residues. The carboxyl group of muramic acid is usually substituted by a peptide which consists of alternating L- and D-amino acids. These peptide subunits are cross-linked between the diamino acid in position 3 and the C-terminal D-alanine in position 4 of an adjacent peptide subunit either in a direct way or via an interpeptide bridge (Group A). In some coryneform bacteria the cross-linkage extends from the alpha-carboxyl group of D-glutamic acid in position 2 to D-alanine of a neighbouring peptide subunit (Group B). In the latter case a diamino acid is always found in the interpeptide bridge. A chemical modification of the peptidoglycan may occur in some bacteria due to growth in a quite unbalanced medium. The influence of glycine-rich and glycine-deficient growth medium on the chemical structure of the peptidoglycan of S. aureus will be discussed. Inhibiting concentrations of penicillin, glycine or D-amino acids can also modify the peptidoglycan. Further modification can occur through different extraction procedures which are used to obtain a clean peptidoglycan free of non-peptidoglycan cell wall material. Little is known about the molecular basis of the biological activity. The chemical composition is at least important for the antigenic determinants. The lysozyme susceptibility and the size of the preparation may be other crucial points for the biological activity of the peptidoglycan.

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Year:  1975        PMID: 126547

Source DB:  PubMed          Journal:  Z Immunitatsforsch Exp Klin Immunol        ISSN: 0300-872X


  9 in total

1.  Modulation of the immune response by a synthetic adjuvant and analogs.

Authors:  L Chedid; F Audibert; P Lefrancier; J Choay; E Lederer
Journal:  Proc Natl Acad Sci U S A       Date:  1976-07       Impact factor: 11.205

2.  Protective role of D-amino acid oxidase against Staphylococcus aureus infection.

Authors:  Hideaki Nakamura; Jun Fang; Hiroshi Maeda
Journal:  Infect Immun       Date:  2012-01-23       Impact factor: 3.441

Review 3.  Rheumatoid arthritis: review of searches for an infectious cause. Part II.

Authors:  E Wilkes; E S Meek
Journal:  Infection       Date:  1979       Impact factor: 3.553

Review 4.  Molecular mechanisms in endotoxin fever.

Authors:  C A Dinarello
Journal:  Agents Actions       Date:  1983-08

5.  Specific immunoglobulin A antibodies to a peptide subunit sequence of bacterial cell wall peptidoglycan.

Authors:  N Franken; P H Seidl; T Kuchenbauer; H J Kolb; K H Schleifer; L Weiss; K D Tympner
Journal:  Infect Immun       Date:  1984-04       Impact factor: 3.441

6.  Complement activation by cell wall fractions of Micropolyspora faeni.

Authors:  S M Smith; R Burrell; I S Snyder
Journal:  Infect Immun       Date:  1978-11       Impact factor: 3.441

7.  Specific antibodies to the N-termini of the interpeptide bridges of peptidoglycan.

Authors:  P H Seidl; K H Schleifer
Journal:  Arch Microbiol       Date:  1978-08-01       Impact factor: 2.552

8.  Composition of peptidoglycans in Bacteroidaceae: determination and distribution of lanthionine.

Authors:  E N Vasstrand; H B Jensen; T Miron; T Hofstad
Journal:  Infect Immun       Date:  1982-04       Impact factor: 3.441

9.  Crystal structures of lysine-preferred racemases, the non-antibiotic selectable markers for transgenic plants.

Authors:  Hsin-Mao Wu; Yi-Chia Kuan; Chia-Han Chu; Wen-Hwei Hsu; Wen-Ching Wang
Journal:  PLoS One       Date:  2012-10-31       Impact factor: 3.240

  9 in total

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