• LOGIN
    Login with username and password
Repository logo

BORIS Portal

Bern Open Repository and Information System

  • Publications
  • Theses
  • Research Data
  • Projects
  • Organizations
  • Researchers
  • More
  • Collections
  • Statistics
  • LOGIN
    Login with username and password
Repository logo
Unibern.ch
  1. Home
  2. Publications
  3. Glycerol metabolism is important for cytotoxicity of Mycoplasma pneumoniae

Glycerol metabolism is important for cytotoxicity of Mycoplasma pneumoniae

Details
Publisher DOI
10.1128/JB.01103-08
Abstract
Glycerol is one of the few carbon sources that can be utilized by Mycoplasma pneumoniae. Glycerol metabolism involves uptake by facilitated diffusion, phosphorylation, and the oxidation of glycerol 3-phosphate to dihydroxyacetone phosphate, a glycolytic intermediate. We have analyzed the expression of the genes involved in glycerol metabolism and observed constitutive expression irrespective of the presence of glycerol or preferred carbon sources. Similarly, the enzymatic activity of glycerol kinase is not modulated by HPr-dependent phosphorylation. This lack of regulation is unique among the bacteria for which glycerol metabolism has been studied so far. Two types of enzymes catalyze the oxidation of glycerol 3-phosphate: oxidases and dehydrogenases. Here, we demonstrate that the enzyme encoded by the M. pneumoniae glpD gene is a glycerol 3-phosphate oxidase that forms hydrogen peroxide rather than NADH(2). The formation of hydrogen peroxide by GlpD is crucial for cytotoxic effects of M. pneumoniae. A glpD mutant exhibited a significantly reduced formation of hydrogen peroxide and a severely reduced cytotoxicity. Attempts to isolate mutants affected in the genes of glycerol metabolism revealed that only the glpD gene, encoding the glycerol 3-phosphate oxidase, is dispensable. In contrast, the glpF and glpK genes, encoding the glycerol facilitator and the glycerol kinase, respectively, are essential in M. pneumoniae. Thus, the enzymes of glycerol metabolism are crucial for the pathogenicity of M. pneumoniae but also for other essential, yet-to-be-identified functions in the M. pneumoniae cell.
Date Issued
2009
Publication Type
Article
Language(s)
en
Author(s)
Hames, C.
Halbedel, S.
Hoppert, M.
Frey, Joachim  
Institut für Veterinär-Bakteriologie der Universität Bern  
Stulke, J.
Additional Credits
Institut für Veterinär-Bakteriologie der Universität Bern  
Journal
Journal of bacteriology
Publisher
American Society for Microbiology
ISSN
0021-9193
Access(Rights)
metadata.only
Show full item
BORIS Portal
Bern Open Repository and Information System
Build: 0eaa7c [ 7.08. 11:06]
Explore
  • Projects
  • Funding
  • Publications
  • Research Data
  • Organizations
  • Researchers
  • Audiovisual Material
  • Software & other digital items
  • Events
More
  • About BORIS Portal
  • BORIS Portal & Open Science
  • Send Feedback
  • Cookie settings
  • Service Policy
Follow us on
  • Mastodon
  • YouTube
  • LinkedIn
UniBe logo
Repository logo COAR Notify