Mihailovic Jelena, Inic-Kanada Aleksandra, Smiljanic Katarina, Stein Elisabeth, Barisani-Asenbauer Talin, Cirkovic Velickovic Tanja
Center of Excellence for Molecular Food Sciences and Department of Biochemistry, University of Belgrade⿿Faculty of Chemistry, Belgrade, Serbia.
OCUVAC⿿Center of Ocular Inflammation and Infection, Laura Bassi Centers of Expertise, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Austria.
EuPA Open Proteom. 2016 Jan 28;10:63-69. doi: 10.1016/j.euprot.2016.01.007. eCollection 2016 Mar.
(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.
沙眼衣原体（Ct）是一种导致沙眼和不孕的人类病原体。我们研究了衣原体抗原蛋白赖氨酸残基的乙酰化情况：主要外膜蛋白（MOMP）、60 kDa伴侣蛋白（衣原体热休克蛋白60）、延伸因子G（EF-G）、烯醇化酶以及多态膜蛋白PmpB、PmpE和PmpF。60 kDa伴侣蛋白、EF-G和PmpB表现出最高程度的乙酰化。我们的数据表明，重要的Ct抗原可能在多个位点通过赖氨酸残基的乙酰化进行翻译后修饰。需要进一步研究来调查Ct的全乙酰化组以及翻译后修饰可能对Ct生物学和致病性产生的影响。
