Lysine acetylation of major Chlamydia trachomatis antigens
2016
Authors
Mihailović-Vesić, JelenaInić-Kanada, Aleksandra
Smiljanić, Katarina
Stein, Elisabeth
Barisani-Asenbauer, T.
Ćirković-Veličković, Tanja
Article (Published version)
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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 spectrometrySource:
EuPA Open Proteomics, 2016, 10, 63-69Funding / projects:
- Molecular properties and modifications of some respiratory and nutritional allergens (RS-MESTD-Basic Research (BR or ON)-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-FP7-256716)
- Austrian Research Promotion Agency (FFG Project Number: 822768).
Note:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3563
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Hemijski fakultet / Faculty of ChemistryTY - 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 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" }
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
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 .
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 . .