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Shotgun proteomic analysis of Chlamydia trachomatis

Shotgun proteomic analysis of Chlamydia trachomatis
Shotgun proteomic analysis of Chlamydia trachomatis
Chlamydiae are widespread bacterial pathogens responsible for a broad range of diseases, including sexually transmitted infections, pneumonia and trachoma. To validate the existence of hitherto hypothetical proteins predicted from recent chlamydial genome sequencing projects and to examine the patterns of expression of key components at the protein level, we have surveyed the expressed proteome of Chlamydia trachomatis strain L2. A combination of two-dimensional gel analysis, multi-dimensional protein identification (MudPIT) and nanocapillary liquid chromatography-tandem mass spectrometry allowed a total of 328 chlamydial proteins to be unambiguously assigned. Proteins identified as being expressed in the metabolically inert form, elementary body, of Chlamydia include the entire set of predicted glycolytic enzymes, indicating that metabolite flux rather than de novo synthesis of this pathway is triggered upon infection of host cells. An enzyme central to cell wall biosynthesis was also detected in the intracellular form, reticulate body, of Chlamydia, suggesting that the peptidoglycan is produced during growth within host cells. Other sets of proteins identified include 17 outer membrane-associated proteins of potential significance in vaccine studies and 67 proteins previously annotated as hypothetical or conserved hypothetical. Taken together, ?35% of the predicted proteome for C. trachomatis has been experimentally verified, representing the most extensive survey of any chlamydial proteome to date.
chlamydia, multidimensional protein identification technology, shotgun, trachoma
1615-9853
1558-1573
Skipp, Paul
1ba7dcf6-9fe7-4b5c-a9d0-e32ed7f42aa5
Robinson, Jo
0a015569-3527-40db-b0b1-5f942c451472
O'Connor, C. David
17ff63ee-30d8-44c5-84b5-775d51e45d46
Clarke, Ian N.
ff6c9324-3547-4039-bb2c-10c0b3327a8b
Skipp, Paul
1ba7dcf6-9fe7-4b5c-a9d0-e32ed7f42aa5
Robinson, Jo
0a015569-3527-40db-b0b1-5f942c451472
O'Connor, C. David
17ff63ee-30d8-44c5-84b5-775d51e45d46
Clarke, Ian N.
ff6c9324-3547-4039-bb2c-10c0b3327a8b

Skipp, Paul, Robinson, Jo, O'Connor, C. David and Clarke, Ian N. (2005) Shotgun proteomic analysis of Chlamydia trachomatis. Proteomics, 5 (6), 1558-1573. (doi:10.1002/pmic.200401044).

Record type: Article

Abstract

Chlamydiae are widespread bacterial pathogens responsible for a broad range of diseases, including sexually transmitted infections, pneumonia and trachoma. To validate the existence of hitherto hypothetical proteins predicted from recent chlamydial genome sequencing projects and to examine the patterns of expression of key components at the protein level, we have surveyed the expressed proteome of Chlamydia trachomatis strain L2. A combination of two-dimensional gel analysis, multi-dimensional protein identification (MudPIT) and nanocapillary liquid chromatography-tandem mass spectrometry allowed a total of 328 chlamydial proteins to be unambiguously assigned. Proteins identified as being expressed in the metabolically inert form, elementary body, of Chlamydia include the entire set of predicted glycolytic enzymes, indicating that metabolite flux rather than de novo synthesis of this pathway is triggered upon infection of host cells. An enzyme central to cell wall biosynthesis was also detected in the intracellular form, reticulate body, of Chlamydia, suggesting that the peptidoglycan is produced during growth within host cells. Other sets of proteins identified include 17 outer membrane-associated proteins of potential significance in vaccine studies and 67 proteins previously annotated as hypothetical or conserved hypothetical. Taken together, ?35% of the predicted proteome for C. trachomatis has been experimentally verified, representing the most extensive survey of any chlamydial proteome to date.

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Published date: April 2005
Keywords: chlamydia, multidimensional protein identification technology, shotgun, trachoma

Identifiers

Local EPrints ID: 37518
URI: https://eprints.soton.ac.uk/id/eprint/37518
ISSN: 1615-9853
PURE UUID: 6ab1042f-dae1-443d-a544-b0766ce9eae8
ORCID for Paul Skipp: ORCID iD orcid.org/0000-0002-2995-2959
ORCID for Ian N. Clarke: ORCID iD orcid.org/0000-0002-4938-1620

Catalogue record

Date deposited: 22 May 2006
Last modified: 07 Aug 2019 00:55

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