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dc.creatorMihailović-Vesić, Jelena
dc.creatorInic-Kanada, A.
dc.creatorSmiljanić, Katarina
dc.creatorStein, E.
dc.creatorBarisani-Asenbauer, T.
dc.creatorĆirković-Veličković, Tanja
dc.date.accessioned2018-11-22T00:34:14Z
dc.date.available2018-11-22T00:34:14Z
dc.date.issued2016
dc.identifier.issn2212-9685
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/295
dc.description.abstractChlamydia 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.en
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.relationAustrian Research Promotion Agency (FFG Project Number: 822768).
dc.rightsopenAccess
dc.sourceEuPA Open Proteomics
dc.subjectAntigensen
dc.subjectChlamydia trachomatisen
dc.subjectLysine acetylationen
dc.subjectMass spectrometryen
dc.titleLysine acetylation of major Chlamydia trachomatis antigensen
dc.typearticle
dc.rights.licenseBY
dcterms.abstractСтеин, Е.; Барисани-Aсенбауер, Т.; Михаиловић Весић, Јелена; Ћирковић-Величковић, Тања; Смиљанић, Катарина; Иниц-Канада, A.;
dc.citation.volume10
dc.citation.spage63
dc.citation.epage69
dc.identifier.doi10.1016/j.euprot.2016.01.007
dc.citation.other10: 63-69
dc.type.versionpublishedVersion
dc.identifier.scopus2-s2.0-84956640653
dc.identifier.rcubKon_1248


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