Analysis of the peptidoglycan of Rickettsia prowazekii

H. Pang, H. H. Winkler

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Abstract

In the present study, peptidoglycan from Rickettsia prowazekii, an obligate intracellular bacterium, was purified. The rickettsial peptidoglycan is like that of gram-negative bacteria; that is, it is sodium dodecyl sulfate insoluble, lysozyme sensitive, and composed of glutamic acid, alanine, and diaminopimelic acid in a molar ratio of 1.0:2.3:1.0. The small amount of lysine found in the peptidoglycan preparation suggests that a peptidoglycan- linked lipoprotein(s) may be present in the rickettsiae. D-Cycloserine, a D- alanine analog which inhibits the biosynthesis of bacterial cell walls, prevented rickettsial growth in mouse L929 cells at a high concentration and altered the morphology of the rickettsiae at a low concentration. These effects were prevented by the addition of D-alanine. This suggests that R. prowazekii contains D-alanine in the peptidoglycan and has D-Ala-D-Ala ligase and alanine racemase activities.

Original languageEnglish (US)
Pages (from-to)923-926
Number of pages4
JournalJournal of bacteriology
Volume176
Issue number3
DOIs
Publication statusPublished - Jan 1 1994

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ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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