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          Institute: MPI für Biochemie     Collection: Independent Research Groups     Display Documents



ID: 35293.0, MPI für Biochemie / Independent Research Groups
Analysis of the quorum-sensing regulon of the opportunistic pathogen Burkholderia cepacia H111 by proteomics
Authors:Riedel, K.; Arevalo-Ferro, C.; Reil, G.; Gorg, A.; Lottspeich, F.; Eberl, L.
Language:English
Date of Publication (YYYY-MM-DD):2003-02
Title of Journal:Electrophoresis
Journal Abbrev.:Electrophoresis
Volume:24
Issue / Number:4
Start Page:740
End Page:750
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Burkholderia cepacia H111, an important pathogen for persons suffering from cystic fibrosis, employs a quorum-sensing (QS) system, cep, to control expression of virulence factors as well as the formation of biofilms. The QS system is thought to ensure that pathogenic traits are only expressed when the bacterial population density is high enough to overwhelm the host before it is able to mount an efficient response. In this study, we compared the protein pattern of the intracellular, extracellular, and surface protein fractions of an AHL- deficient cep/mutant with the one of the parent strain H111 by means of two-dimensional gel electrophoresis (2-DE). Our analysis showed that 55 proteins out of 985 detected spots were differentially expressed; these are expected to represent QS- controlled gene products. Addition of the respective signal molecules to the growth medium of the cep mutant fully restored the wild-type protein expression profile. In total about 5% of the B. cepacia proteome was downregulated and 1% upregulated in the cep/mutant, indicating that quorum sensing represents a global regulatory system. Nineteen proteins were identified with high confidence by N-terminal sequence analysis.
Free Keywords:Burkholderia cepacia; microbial proteomics; quorum sensing
Comment of the Author/Creator:Date: 2003, FEB
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Independent Research Groups/Protein Analytics (F. Lottspeich)
External Affiliations:Tech Univ Munich, Dept Microbiol, Hochanger 4, D-85350 Freising; Weihenstephan, Germany; Tech Univ Munich, Dept Microbiol, D-85350 Freising Weihenstephan, Germany; Tech Univ Munich, Dept Chem Tech Anal & Chem Food Technol, D-85350 Freising Weihenstephan, Germany; Tech Univ Munich, Proteom Dept, D-85350 Freising Weihenstephan, Germany
Identifiers:ISI:000181507200023 [ID No:1]
ISSN:0173-0835 [ID No:2]
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