Identification of Chlamydia pneumoniae proteins in the transition from reticulate to elementary body formation

Good, David A., Mukhopadhyay, Sanghamitra, Miller, Richard D., Mathews, Sarah A., Graham, James E., Timms, Peter, & Summersgill, James T. (2006) Identification of Chlamydia pneumoniae proteins in the transition from reticulate to elementary body formation. Molecular and Cellular Proteomics, 5(12), pp. 2311-2318.

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Chlamydia pneumoniae is an important human respiratory pathogen that is responsible for an estimated 10% of community-acquired pneumonia and 5% of bronchitis and sinusitis cases. We examined changes in global protein expression profiles associated with the redifferentiation of reticulate body (RB) to elementary body (EB) as C. pneumoniae cells progressed from 24 to 48 h postinfection in HEp2 cells. Proteins corresponding to those showing the greatest changes in abundance in the beginning of the RB to EB transition were then identified from purified EBs. Among the 300 spots recognized, 35 proteins that were expressed at sufficiently high levels were identified by mass spectrometry. We identified C. pneumoniae proteins that showed more than 2-fold increases in abundance in the early stages of RB to EB transition, including several associated with amino acid and cofactor biosynthesis (Ndk, TrxA, Adk, PyrH, and BirA), maintenance of cytoplasmic protein function (GroEL/ES, DnaK, DksA, GrpE, HtrA, ClpP, ClpB, and Map), modification of the bacterial cell surface (CrpA, OmpA, and OmcB), energy metabolism (Tal and Pyk), and the putative transcriptional regulator TctD. This study identified C. pneumoniae proteins involved in the process of redifferentiation into mature, infective EBs and indicates bacterial metabolic pathways that may be involved in this transition. The proteins involved in RB to EB transition are key to C. pneumoniae infection and are perhaps suitable targets for therapeutic intervention.

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14 citations in Scopus
9 citations in Web of Science®
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ID Code: 7176
Item Type: Journal Article
Refereed: Yes
Additional Information: This research was originally published in Molecular and Cellular Proteomics. Sanghamitra Mukhopadhyay, David Good, Richard D. Miller, James E. Graham, Sarah A. Mathews, Peter Timms and James T. Summersgill. Identification of Chlamydia pneumoniae Proteins in the Transition from Reticulate to Elementary Body Formation. Molecular & Cellular Proteomics. 2006; 5:2311-2318. © the American Society for Biochemistry and Molecular Biology.
Keywords: chlamydia pneumoniae, 2D gel electrophoresis, proteomics, RT, PCR, development
DOI: 10.1074/mcp.M600214-MCP200
ISSN: 1535-9476
Divisions: Past > QUT Faculties & Divisions > Faculty of Science and Technology
Current > Institutes > Institute of Health and Biomedical Innovation
Current > QUT Faculties and Divisions > Science & Engineering Faculty
Current > Research Centres > Science Research Centre
Copyright Owner: Copyright 2007 The American Society for Biochemistry and Molecular Biology, Inc.
Deposited On: 24 Apr 2007 00:00
Last Modified: 19 May 2017 02:21

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