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Effects of interferon gamma on Chlamydia trachomatis serovar A and L2 protein expression investigated by two‐dimensional gel electrophoresis
Author(s) -
Shaw Allan Christian,
Christiansen Gunna,
Birkelund Svend
Publication year - 1999
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/(sici)1522-2683(19990101)20:4/5<775::aid-elps775>3.0.co;2-z
Subject(s) - chlamydia trachomatis , intracellular , biology , intracellular parasite , microbiology and biotechnology , gel electrophoresis , interferon gamma , interferon , chlamydiaceae , chlamydia , virology , immune system , immunology , biochemistry
Chlamydia trachomatis is an obligate intracellular bacterium causing human ocular and genital disease. The lymphokine interferon gamma (IFN‐γ) is an important immune effector exerting antimicrobial effects towards several intracellular parasites, the chlamydia included. IFN‐γ has been reported to inhibit the chlamydial replication in vitro in part by depleting intracellular levels of tryptophan in a dose‐dependent manner. In addition, down‐regulation of important immunogens has been described. These findings are extended in this paper, in which we are combining pulse labeling with [ 35 S]methionine and two‐dimensional gel electrophoresis with immobilized pH gradients in order to investigate changes in the protein expression of C. trachomatis serovar A and L2 caused by treatment with IFN‐γ. In contrast to what was observed in C. trachomatis L2, our results showed that, in C. trachomatis A, down‐regulations of the chlamydia major outer membrane protein and of several other proteins were detectable upon IFN‐γ treatment. In addition, we report the up‐regulations of C. trachomatis A and L2 proteins with molecular masses of approximately 30 kDa and 40 kDa which may be part of an, as yet, uncharacterized chlamydial response to IFN‐γ treatment.