The Chlamydia trachomatis CT149 protein exhibits esterase activity in vitro and catalyzes cholesteryl ester hydrolysis when expressed in HeLa cells

Jan Peters, Vijaya Onguri, Satoru Nishimoto, Tony Marion, Gerald I. Byrne

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Chlamydia, like other intracellular bacteria, are auxotrophic for a variety of essential metabolites and obtain cholesterol and fatty acids from their eukaryotic host cell, however not many Chlamydia-specific enzymes have been identified that are involved in lipid metabolism. In silico analysis of one candidate Chlamydia trachomatis enzyme, annotated as a conserved putative hydrolase (CT149), identified two lipase/esterase GXSXG motifs, and a potential cholesterol recognition/interaction amino acid consensus (CRAC) sequence. His-tag purified recombinant CT149 exhibited ester hydrolysis activity in a nitrophenyl acetate-based cell-free assay system. When cholesteryl linoleate was used as substrate, ester hydrolysis occurred and production of cholesterol was detected by high performance liquid chromatography. Exogenous expression of transfected CT149 in HeLa cells resulted in a significant decrease of cytoplasmic cholesteryl esters within 48 h. These results demonstrate that CT149 has cholesterol esterase activity and is likely to contribute to the hydrolysis of eukaryotic cholesteryl esters during intracellular chlamydial growth.

Original languageEnglish (US)
Pages (from-to)1196-1204
Number of pages9
JournalMicrobes and Infection
Volume14
Issue number13
DOIs
StatePublished - Nov 1 2012

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Cholesterol Esters
Chlamydia trachomatis
Esterases
HeLa Cells
Hydrolysis
Chlamydia
Cholesterol
Esters
Sterol Esterase
Proteins
Cell-Free System
Consensus Sequence
Eukaryotic Cells
Hydrolases
Enzymes
Lipase
Lipid Metabolism
Computer Simulation
Amino Acid Sequence
Acetates

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Infectious Diseases

Cite this

The Chlamydia trachomatis CT149 protein exhibits esterase activity in vitro and catalyzes cholesteryl ester hydrolysis when expressed in HeLa cells. / Peters, Jan; Onguri, Vijaya; Nishimoto, Satoru; Marion, Tony; Byrne, Gerald I.

In: Microbes and Infection, Vol. 14, No. 13, 01.11.2012, p. 1196-1204.

Research output: Contribution to journalArticle

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