Jelena Mihailovic , Aleksandra Inic-Kanada , Katarina Smiljanic , Elisabeth Stein , Talin Barisani-Asenbauer , Tanja Cirkovic Velickovic
{"title":"Lysine acetylation of major Chlamydia trachomatis antigens","authors":"Jelena Mihailovic , Aleksandra Inic-Kanada , Katarina Smiljanic , Elisabeth Stein , Talin Barisani-Asenbauer , Tanja Cirkovic Velickovic","doi":"10.1016/j.euprot.2016.01.007","DOIUrl":null,"url":null,"abstract":"<div><p><em>Chlamydia trachomatis</em> (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.</p><p>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.</p></div>","PeriodicalId":38260,"journal":{"name":"EuPA Open Proteomics","volume":"10 ","pages":"Pages 63-69"},"PeriodicalIF":0.0000,"publicationDate":"2016-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.euprot.2016.01.007","citationCount":"3","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"EuPA Open Proteomics","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2212968516300101","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 3
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.
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