@article{17264,
  keywords = {Corynebacterium, Glycopeptides, leprosy, Peptidoglycan},
  author = {Janczura E and Leyh-Bouille M and Cocito C and Ghuysen J M},
  title = {Primary structure of the wall peptidoglycan of leprosy-derived corynebacteria.},
  abstract = {<p>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.</p>},
  year = {1981},
  journal = {Journal of bacteriology},
  volume = {145},
  pages = {775-9},
  month = {1981 Feb},
  issn = {0021-9193},
  language = {eng},
}