Lysine acetylation of major Chlamydia trachomatis antigens

Publication date: Available online 28 January 2016 Source:EuPA Open Proteomics Author(s): Jelena Mihailovic, Aleksandra Inic-Kanada, Katarina Smiljanic, Elisabeth Stein, Talin Barisani-Asenbauer, Tanja Cirkovic Velickovic 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 the total acetylome of Ct and the impact the PTMs might have on Ct biology and pathogenicity. Graphical abstract
Source: EuPA Open Proteomics - Category: Bioinformatics Source Type: research