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Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii.

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  • Additional Information
    • Publisher Information:
      Springer 2004
    • Abstract:
      Microorganisms used in food technology and probiotics are exposed to technological and digestive stresses, respectively. Traditionally used as Swiss-type cheese starters, propionibacteria also constitute promising human probiotics. Stress tolerance and cross-protection in Propionibacterium freudenreichii were thus examined after exposure to heat, acid, or bile salts stresses. Adapted cells demonstrated acquired homologous tolerance. Cross-protection between bile salts and heat adaptation was demonstrated. By contrast, bile salts pretreatment sensitized cells to acid challenge and vice versa. Surprisingly, heat and acid responses did not present significant cross-protection in P. freudenreichii. During adaptations, important changes in cellular protein synthesis were observed using two-dimensional electrophoresis. While global protein synthesis decreased, several proteins were overexpressed during stress adaptations. Thirty-four proteins were induced by acid pretreatment, 34 by bile salts pretreatment, and 26 by heat pretreatment. Six proteins are common to all stresses and represent general stress-response components. Among these polypeptides, general stress chaperones, and proteins involved in energetic metabolism, oxidative stress response, or SOS response were identified. These results bring new insight into the tolerance of P. freudenreichii to heat, acid, and bile salts, and should be taken into consideration in the development of probiotic preparations.
    • Subject Terms:
      Acids; Mass Spectrometry; Molecular Chaperones; Molecular Sequence Data; Oxidative Stress; Probiotics; Propionibacterium; Proteome; SOS Response (Genetics); Temperature; Adaptation, Physiological; Amino Acid Sequence; Bacterial Proteins; Bile Acids and Salts; Electrophoresis, Gel, Two-Dimensional; Energy Metabolism; Food Microbiology; Heat-Shock Proteins; info:eu-repo/semantics/article
    • Availability:
      Open access content. Open access content
      info:eu-repo/semantics/restrictedAccess
    • Note:
      Ndonga
    • Other Numbers:
      UCDLC oai:dial.uclouvain.be:boreal:157229
      boreal:157229
      info:doi/10.1007/s00203-003-0646-0
      info:pmid/14730419
      urn:ISSN:0302-8933
      urn:EISSN:1432-072X
      1130482303
    • Contributing Source:
      UNIVERSITE CATHOLIQUE DE LOUVAIN
      From OAIster®, provided by the OCLC Cooperative.
    • Accession Number:
      edsoai.on1130482303
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