Originally published In Press as doi:10.1074/mcp.M600214-MCP200 on August 18, 2006.
Molecular & Cellular Proteomics 5:2311-2318, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.
Research
Identification of Chlamydia pneumoniae Proteins in the Transition from Reticulate to Elementary Body Formation*
Sanghamitra Mukhopadhyay , ,
David Good¶,
Richard D. Miller||,
James E. Graham||,
Sarah A. Mathews¶,
Peter Timms¶ and
James T. Summersgill ,||
From the Division of Infectious Diseases, Department of Medicine and || Department of Microbiology and Immunology, University of Louisville, Louisville, Kentucky 40292 and ¶ Infectious Diseases Program, School of Life Sciences, Queensland University of Technology, Brisbane Qld 4059, Australia
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.
To whom correspondence should be addressed: Biological Defense Research Directorate, Naval Medical Research Center, 12300 Washington Ave., Rockville, MD 20852. Tel.: 301-231-6798; Fax: 301-231-6799; E-mail: mukhopadhyays.ctr.in{at}nmrc.navy.mil

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Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
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