Lysine acetylation of major Chlamydia trachom atis antigens

Jelena Mihailovic; Aleksandra Inic-Kanada; Katarina Smiljanic; Elisabeth Stein; Talin Barisani-Asenbauer; Tanja Cirkovic Velickovic

doi:10.1016/j.euprot.2016.01.007

Lysine acetylation of major Chlamydia trachom atis antigens

EuPA Open Proteom. 2016 Jan 28:10:63-69. doi: 10.1016/j.euprot.2016.01.007. eCollection 2016 Mar.

Authors

Jelena Mihailovic¹, Aleksandra Inic-Kanada², Katarina Smiljanic¹, Elisabeth Stein², Talin Barisani-Asenbauer², Tanja Cirkovic Velickovic¹

Affiliations

¹ Center of Excellence for Molecular Food Sciences and Department of Biochemistry, University of Belgrade⿿Faculty of Chemistry, Belgrade, Serbia.
² OCUVAC⿿Center of Ocular Inflammation and Infection, Laura Bassi Centers of Expertise, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Austria.

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), 60 kDa chaperonin (chlamydial Hsp60), elongation factor G (EF-G), enolase and the polymorphic membrane proteins PmpB, PmpE and PmpF. 60 kDa 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.

Keywords: Antigens; Chlamydia trachomatis; Lysine acetylation; Mass spectrometry.