Abstract
Chlamydia trachomatis (Ct) is a human pathogen causing trachoma and infertility. We investigated acetylation at lysine residues of chlamydial antigenic proteins: major outer membrane protein (MOMP), 60kDa chaperonin (chlamydial Hsp60), elongation factor G (EF-G), enolase and the polymorphic membrane proteins PmpB, PmpE and PmpF. 60kDa chaperonin, EF-G and PmpB showed the highest degree of acetylation.Our data show that important Ct antigens could be post-translationally modified by acetylation of lysine residues at multiple sites. Further studies are needed to investigate total acetylome of Ct and the impact PTMs might have on Ct biology and pathogenicity.
Highlights
Chlamydia trachomatis (Ct) is an obligate intracellular pathogen causing socioeconomically significant morbidities as blindness and female infertility [1]
Ct serovar B (CtB) grown in McCoy cells were harvested between 3rd and 26th passage, EBs were purified and lysates were prepared for protein analysis
Lysates of CtB EB analysed by SDS PAGE showed different protein patterns especially lane C, compared to lanes A and B that share a high degree of similarity (Fig. 1)
Summary
Chlamydia trachomatis (Ct) is an obligate intracellular pathogen causing socioeconomically significant morbidities as blindness (trachoma) and female infertility [1]. Serovars A, B, Ba and C are considered ocular strains, serovars D–K cause sexually transmitted diseases worldwide, and serovars L1– L3 inflict severe systematic infection lymphogranuloma venereum [2]. Proteomic approaches could help elucidate involved mechanisms, since posttranslational modifications (PTMs) and level of protein expression are taken into account – categories otherwise frequently underestimated or overlooked in transcriptomics and genomics studies. In order for an organism to survive and thrive in ever changing and hostile environments it needs flexible survival mechanisms. PTM of proteins is a strategy that organisms employ to control their biological processes and to adapt to rapid environmental changes. Some of the most studied PTMs include phosphorylation (Ser, Thr, Tyr), ubiquitination and sumoylation (Lys), methylation (Arg, Lys) and acetylation (Lys) [3]
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