Chlamydia trachomatis GlgA is secreted into host cell cytoplasm

Glycogen has been localized both inside and outside Chlamydia trachomatis organisms. We now report that C. trachomatis glycogen synthase (GlgA) was detected in both chlamydial organism-associated and -free forms. The organism-free GlgA molecules were localized both in the lumen of chlamydial inclusi...

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Bibliographic Details
Published in:PloS one 2013-07, Vol.8 (7), p.e68764-e68764
Main Authors: Lu, Chunxue, Lei, Lei, Peng, Bo, Tang, Lingli, Ding, Honglei, Gong, Siqi, Li, Zhongyu, Wu, Yimou, Zhong, Guangming
Format: Article
Language:English
Subjects:
Analysis
Antigens
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biology
Biosynthesis
Blotting, Western
Chlamydia
Chlamydia infections
Chlamydia trachomatis
Chlamydia trachomatis - enzymology
Chlamydia trachomatis - metabolism
Condoms
Cytoplasm
Cytosol
Enzyme-Linked Immunosorbent Assay
Enzymes
Fluorescent Antibody Technique
Genomes
Glycogen
Glycogen synthase
Glycogen Synthase - genetics
Glycogen Synthase - metabolism
Health aspects
HeLa Cells
Humans
Immunogenicity
Immunology
Infections
Infertility
Localization
Metabolism
Pathogenesis
Pathogens
Proteins
Risk factors
Science
Sexually transmitted diseases
STD
Womens health
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Summary:Glycogen has been localized both inside and outside Chlamydia trachomatis organisms. We now report that C. trachomatis glycogen synthase (GlgA) was detected in both chlamydial organism-associated and -free forms. The organism-free GlgA molecules were localized both in the lumen of chlamydial inclusions and in the cytosol of host cells. The cytosolic GlgA displayed a distribution pattern similar to that of a known C. trachomatis-secreted protease, CPAF. The detection of GlgA was specific since the anti-GlgA antibody labeling was only removed by preabsorption with GlgA but not CPAF fusion proteins. GlgA was detectable at 12h and its localization into host cell cytosol only became apparent at 24h after infection. The cytosolic localization of GlgA was conserved among all C. trachomatis serovars. However, the significance of the GlgA secretion into host cell cytoplasm remains unclear since, while expression of chlamydial GlgA in HeLa cells increased glycogen stores, it did not affect a subsequent infection with C. trachomatis. Similar to several other C. trachomatis-secreted proteins, GlgA is immunogenic in women urogenitally infected with C. trachomatis, suggesting that GlgA is expressed and may be secreted into host cell cytosol during C. trachomatis infection in humans. These findings have provided important information for further understanding C. trachomatis pathogenic mechanisms.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0068764