Primary structure of the wall peptidoglycan of leprosy-derived corynebacteria
- 1 February 1981
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 145 (2) , 775-779
- https://doi.org/10.1128/jb.145.2.775-779.1981
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.This publication has 21 references indexed in Scilit:
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