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. 1981 Feb;145(2):775–779. doi: 10.1128/jb.145.2.775-779.1981

Primary structure of the wall peptidoglycan of leprosy-derived corynebacteria.

E Janczura, M Leyh-Bouille, C Cocito, J M Ghuysen
PMCID: PMC217178  PMID: 7462160

Abstract

The cell walls isolated from axenically grown leprosy-derived corynebacteria were submitted to various chemical and enzymatic degradations. The glycan strands of the wall peptidoglycan are essentially composed of N-acetylglycosaminyl-N-acetylmuramic acid disaccharide units. Small amounts of N-acetylglycosaminyl-N-glycolylmuramic acid (less than 10%) were also detected. The muramic acid residues of adjacent glycan strands are substituted by amidated tetrapeptide units which, in turn, are cross-linked through direct linkages extending between the C-terminal D-alanine residue of one tetrapeptide and the mesodiaminopimelic acid residue of another tetrapeptide. Such a structure is very similar to that of the wall peptidoglycan found in the taxonomically related microorganisms of the Corynebacterium, Mycobacterium, and Nocardia groups.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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