Lysine acetylation of major Chlamydia trachomatis antigens

Mihailović-Vesić, Jelena; Inić-Kanada, Aleksandra; Smiljanić, Katarina; Stein, Elisabeth; Barisani-Asenbauer, T.; Ćirković-Veličković, Tanja

doi:10.1016/j.euprot.2016.01.007

2016

293.pdf (718.0Kb)

Authors

Mihailović-Vesić, Jelena

Inić-Kanada, Aleksandra

Smiljanić, Katarina

Stein, Elisabeth
Barisani-Asenbauer, T.
Ćirković-Veličković, Tanja

Article (Published version)

Metadata

Show full item record

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. © 2016.

Keywords:

Antigens / Chlamydia trachomatis / Lysine acetylation / Mass spectrometry

Source:
EuPA Open Proteomics, 2016, 10, 63-69

Funding / projects:

Molecular properties and modifications of some respiratory and nutritional allergens (RS-172024)
Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)
Austrian Research Promotion Agency (FFG Project Number: 822768).

Note:

Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3563

DOI: 10.1016/j.euprot.2016.01.007

ISSN: 2212-9685

Scopus: 2-s2.0-84956640653

[ Google Scholar ]


	1

TY  - JOUR
AU  - Mihailović-Vesić, Jelena
AU  - Inić-Kanada, Aleksandra
AU  - Smiljanić, Katarina
AU  - Stein, Elisabeth
AU  - Barisani-Asenbauer, T.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/295
AB  - 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. © 2016.
T2  - EuPA Open Proteomics
T1  - Lysine acetylation of major Chlamydia trachomatis antigens
VL  - 10
SP  - 63
EP  - 69
DO  - 10.1016/j.euprot.2016.01.007
UR  - Kon_1248
ER  -

@article{
author = "Mihailović-Vesić, Jelena and Inić-Kanada, Aleksandra and Smiljanić, Katarina and Stein, Elisabeth and Barisani-Asenbauer, T. and Ćirković-Veličković, Tanja",
year = "2016",
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. © 2016.",
journal = "EuPA Open Proteomics",
title = "Lysine acetylation of major Chlamydia trachomatis antigens",
volume = "10",
pages = "63-69",
doi = "10.1016/j.euprot.2016.01.007",
url = "Kon_1248"
}

Mihailović-Vesić, J., Inić-Kanada, A., Smiljanić, K., Stein, E., Barisani-Asenbauer, T.,& Ćirković-Veličković, T.. (2016). Lysine acetylation of major Chlamydia trachomatis antigens. in EuPA Open Proteomics, 10, 63-69.
https://doi.org/10.1016/j.euprot.2016.01.007
Kon_1248

Mihailović-Vesić J, Inić-Kanada A, Smiljanić K, Stein E, Barisani-Asenbauer T, Ćirković-Veličković T. Lysine acetylation of major Chlamydia trachomatis antigens. in EuPA Open Proteomics. 2016;10:63-69.
doi:10.1016/j.euprot.2016.01.007
Kon_1248 .

Mihailović-Vesić, Jelena, Inić-Kanada, Aleksandra, Smiljanić, Katarina, Stein, Elisabeth, Barisani-Asenbauer, T., Ćirković-Veličković, Tanja, "Lysine acetylation of major Chlamydia trachomatis antigens" in EuPA Open Proteomics, 10 (2016):63-69,
https://doi.org/10.1016/j.euprot.2016.01.007 .,
Kon_1248 .