Identification of Chlamydia trachomatis outer membrane complex proteins by differential proteomics

Xiaoyun Liu, Mary Afrane, David E. Clemmer, Guangming Zhong, David E. Nelson

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

Abstract

The extracellular chlamydial infectious particle, or elementary body (EB), is enveloped by an intra- and intermolecular cysteine cross-linked protein shell called the chlamydial outer membrane complex (COMC). A few abundant proteins, including the major outer membrane protein and cysteine-rich proteins (OmcA and OmcB), constitute the overwhelming majority of COMC proteins. The identification of less-abundant COMC proteins has been complicated by limitations of proteomic methodologies and the contamination of COMC fractions with abundant EB proteins. Here, we used parallel liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) analyses of Chlamydia trachomatis serovar L2 434/Bu EB, COMC, and Sarkosyl-soluble EB fractions to identify proteins enriched or depleted from COMC. All well-described COMC proteins were specifically enriched in the COMC fraction. In contrast, multiple COMC-associated proteins found in previous studies were strongly enriched in the Sarkosyl-soluble fraction, suggesting that these proteins are not COMC components or are not stably associated with COMC. Importantly, we also identified novel proteins enriched in COMC. The list of COMC proteins identified in this study has provided reliable information for further understanding chlamydial protein secretion systems and modeling COMC and EB structures.

Original languageEnglish (US)
Pages (from-to)2852-2860
Number of pages9
JournalJournal of bacteriology
Volume192
Issue number11
DOIs
StatePublished - Jun 2010

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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