Lysine acetylation of major Chlamydia trachomatis antigens

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 membran...

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Main Authors:	Jelena Mihailovic, Aleksandra Inic-Kanada, Katarina Smiljanic, Elisabeth Stein, Talin Barisani-Asenbauer, Tanja Cirkovic Velickovic
Format:	Article
Language:	English
Published:	Elsevier 2016-03-01
Series:	EuPA Open Proteomics
Subjects:	Chlamydia trachomatis Lysine acetylation Antigens Mass spectrometry
Online Access:	http://www.sciencedirect.com/science/article/pii/S2212968516300101

id	doaj-d9434b59d2cc48809ac94e4b21ba80a9
record_format	Article
spelling	doaj-d9434b59d2cc48809ac94e4b21ba80a92020-11-24T21:31:53ZengElsevierEuPA Open Proteomics2212-96852016-03-0110C636910.1016/j.euprot.2016.01.007Lysine acetylation of major Chlamydia trachomatis antigensJelena Mihailovic0Aleksandra Inic-Kanada1Katarina Smiljanic2Elisabeth Stein3Talin Barisani-Asenbauer4Tanja Cirkovic Velickovic5Center of Excellence for Molecular Food Sciences and Department of Biochemistry, University of Belgrade—Faculty of Chemistry, Belgrade, SerbiaOCUVAC—Center of Ocular Inflammation and Infection, Laura Bassi Centers of Expertise, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, AustriaCenter of Excellence for Molecular Food Sciences and Department of Biochemistry, University of Belgrade—Faculty of Chemistry, Belgrade, SerbiaOCUVAC—Center of Ocular Inflammation and Infection, Laura Bassi Centers of Expertise, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, AustriaOCUVAC—Center of Ocular Inflammation and Infection, Laura Bassi Centers of Expertise, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, AustriaCenter of Excellence for Molecular Food Sciences and Department of Biochemistry, University of Belgrade—Faculty of Chemistry, Belgrade, SerbiaChlamydia 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.http://www.sciencedirect.com/science/article/pii/S2212968516300101Chlamydia trachomatisLysine acetylationAntigensMass spectrometry
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Jelena Mihailovic Aleksandra Inic-Kanada Katarina Smiljanic Elisabeth Stein Talin Barisani-Asenbauer Tanja Cirkovic Velickovic
spellingShingle	Jelena Mihailovic Aleksandra Inic-Kanada Katarina Smiljanic Elisabeth Stein Talin Barisani-Asenbauer Tanja Cirkovic Velickovic Lysine acetylation of major Chlamydia trachomatis antigens EuPA Open Proteomics Chlamydia trachomatis Lysine acetylation Antigens Mass spectrometry
author_facet	Jelena Mihailovic Aleksandra Inic-Kanada Katarina Smiljanic Elisabeth Stein Talin Barisani-Asenbauer Tanja Cirkovic Velickovic
author_sort	Jelena Mihailovic
title	Lysine acetylation of major Chlamydia trachomatis antigens
title_short	Lysine acetylation of major Chlamydia trachomatis antigens
title_full	Lysine acetylation of major Chlamydia trachomatis antigens
title_fullStr	Lysine acetylation of major Chlamydia trachomatis antigens
title_full_unstemmed	Lysine acetylation of major Chlamydia trachomatis antigens
title_sort	lysine acetylation of major chlamydia trachomatis antigens
publisher	Elsevier
series	EuPA Open Proteomics
issn	2212-9685
publishDate	2016-03-01
description	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.
topic	Chlamydia trachomatis Lysine acetylation Antigens Mass spectrometry
url	http://www.sciencedirect.com/science/article/pii/S2212968516300101
work_keys_str_mv	AT jelenamihailovic lysineacetylationofmajorchlamydiatrachomatisantigens AT aleksandrainickanada lysineacetylationofmajorchlamydiatrachomatisantigens AT katarinasmiljanic lysineacetylationofmajorchlamydiatrachomatisantigens AT elisabethstein lysineacetylationofmajorchlamydiatrachomatisantigens AT talinbarisaniasenbauer lysineacetylationofmajorchlamydiatrachomatisantigens AT tanjacirkovicvelickovic lysineacetylationofmajorchlamydiatrachomatisantigens
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Lysine acetylation of major Chlamydia trachomatis antigens

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