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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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Autores principales: Mihailovic, Jelena, Inic-Kanada, Aleksandra, Smiljanic, Katarina, Stein, Elisabeth, Barisani-Asenbauer, Talin, Cirkovic Velickovic, Tanja
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5988610/
https://www.ncbi.nlm.nih.gov/pubmed/29900103
http://dx.doi.org/10.1016/j.euprot.2016.01.007
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author Mihailovic, Jelena
Inic-Kanada, Aleksandra
Smiljanic, Katarina
Stein, Elisabeth
Barisani-Asenbauer, Talin
Cirkovic Velickovic, Tanja
author_facet Mihailovic, Jelena
Inic-Kanada, Aleksandra
Smiljanic, Katarina
Stein, Elisabeth
Barisani-Asenbauer, Talin
Cirkovic Velickovic, Tanja
author_sort Mihailovic, Jelena
collection PubMed
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.
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spelling pubmed-59886102018-06-13 Lysine acetylation of major Chlamydia trachomatis antigens Mihailovic, Jelena Inic-Kanada, Aleksandra Smiljanic, Katarina Stein, Elisabeth Barisani-Asenbauer, Talin Cirkovic Velickovic, Tanja EuPA Open Proteom Special Section: Proceedings of the 9th Annual EuPA Congress “Proteomics - Back to the Future” (June 23 - 28, 2015, Milano, Italy) 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. Elsevier 2016-01-28 /pmc/articles/PMC5988610/ /pubmed/29900103 http://dx.doi.org/10.1016/j.euprot.2016.01.007 Text en © 2016 The Authors. Published by Elsevier B.V. on behalf of European Proteomics Association (EuPA). http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Special Section: Proceedings of the 9th Annual EuPA Congress “Proteomics - Back to the Future” (June 23 - 28, 2015, Milano, Italy)
Mihailovic, Jelena
Inic-Kanada, Aleksandra
Smiljanic, Katarina
Stein, Elisabeth
Barisani-Asenbauer, Talin
Cirkovic Velickovic, Tanja
Lysine acetylation of major Chlamydia trachomatis antigens
title 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_short Lysine acetylation of major Chlamydia trachomatis antigens
title_sort lysine acetylation of major chlamydia trachomatis antigens
topic Special Section: Proceedings of the 9th Annual EuPA Congress “Proteomics - Back to the Future” (June 23 - 28, 2015, Milano, Italy)
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5988610/
https://www.ncbi.nlm.nih.gov/pubmed/29900103
http://dx.doi.org/10.1016/j.euprot.2016.01.007
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