Lysine acetylation of major Chlamydia trachomatis antigens

descriptionPublicationkeyboard_double_arrow_right Article 01 Mar 2016 Serbia English Publisher:Elsevier BVJournal:EuPA Open Proteomics, volume 10, pages 63-69 (issn: 2212-9685,

Copyright policy )Funded by:MESTD | Molecular properties and ..., EC | FCUB-ERA

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

doi: 10.1016/j.euprot.2016.01.007

pmid: 29900103

pmc: PMC5988610

Lysine acetylation of major Chlamydia trachomatis antigens

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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.

Country

Serbia

Related Organizations

University of Belgrade
Serbia
Medical University of Vienna
Austria
University of Nebraska System
United States
Medical Universty of Vienna
Austria
MEDIZINISCHE UNIVERSITAT GRAZ
Austria

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Keywords

Mass spectrometry, Special Section: Proceedings of the 9th Annual EuPA Congress “Proteomics - Back to the Future” (June 23 - 28, 2015, Milano, Italy), Chlamydia trachomatis, Lysine acetylation, Antigens

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