Literature DB >> 3938476

The peptidoglycan of Neisseria gonorrhoeae, with or without O-acetyl groups, contains anhydro-muramyl residues.

J K Blundell, H R Perkins.   

Abstract

Muramidase digests of alkali-treated SDS-insoluble peptidoglycan from two strains of Neisseria gonorrhoeae were examined. Both strains contained disaccharide peptide monomers that had intramolecular 1,6-anhydro-muramyl ends. In contrast to strain 1L260, in which 50% of the monomer fraction is O-acetylated, the monomer fraction from strain RD5 was completely devoid of O-acetyl groups, as shown by HPLC. Penicillin decreased the O-acetylation of peptidoglycan but did not affect the proportion of anhydro-muramyl residues.

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Year:  1985        PMID: 3938476     DOI: 10.1099/00221287-131-12-3397

Source DB:  PubMed          Journal:  J Gen Microbiol        ISSN: 0022-1287


  2 in total

1.  Mutations affecting peptidoglycan acetylation in Neisseria gonorrhoeae and Neisseria meningitidis.

Authors:  Joseph P Dillard; Kathleen T Hackett
Journal:  Infect Immun       Date:  2005-09       Impact factor: 3.441

2.  Alterations in peptidoglycan of Neisseria gonorrhoeae induced by sub-MICs of beta-lactam antibiotics.

Authors:  J F Garcia-Bustos; T J Dougherty
Journal:  Antimicrob Agents Chemother       Date:  1987-02       Impact factor: 5.191

  2 in total

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