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Ample glycosylation in membrane and cell envelope proteins may explain the phenotypic diversity and virulence in the Mycobacterium tuberculosis complex

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dc.contributor.author Alemayehu, Godana Birhanu
dc.contributor.author Solomon, AbebeYimer
dc.contributor.author Shewit, Kalayou
dc.contributor.author Tahira, Riaz
dc.contributor.author Ephrem, Debebe Zegeye
dc.contributor.author Gunnstein, Norheim
dc.contributor.author Carol, Holm-Hansen
dc.contributor.author Abraham, Asefa
dc.contributor.author Markos, Abebe
dc.contributor.author Tone, Tønjum
dc.date.accessioned 2020-05-15T08:10:25Z
dc.date.available 2020-05-15T08:10:25Z
dc.date.issued 2019
dc.identifier.uri http://hdl.handle.net/123456789/1279
dc.description.abstract Multiple regulatory mechanisms including post-translational modifcations (PTMs) confer complexity to the simpler genomes and proteomes of Mycobacterium tuberculosis (Mtb). PTMs such as glycosylation play a signifcant role in Mtb adaptive processes. The glycoproteomic patterns of clinical isolates of the Mycobacterium tuberculosis complex (MTBC) representing the lineages 3, 4, 5 and 7 were characterized by mass spectrometry. A total of 2944 glycosylation events were discovered in 1325 proteins. This data set represents the highest number of glycosylated proteins identifed in Mtb to date. O-glycosylation constituted 83% of the events identifed, while 17% of the sites were N-glycosylated. This is the frst report on N-linked protein glycosylation in Mtb and in Gram-positive bacteria. Collectively, the bulk of Mtb glycoproteins are involved in cell envelope biosynthesis, fatty acid and lipid metabolism, twocomponent systems, and pathogen-host interaction that are either surface exposed or located in the cell wall. Quantitative glycoproteomic analysis revealed that 101 sites on 67 proteins involved in Mtb ftness and survival were diferentially glycosylated between the four lineages, among which 64% were cell envelope and membrane proteins. The diferential glycosylation pattern may contribute to phenotypic variabilities across Mtb lineages. The study identifed several clinically important membrane-associated glycolipoproteins that are relevant for diagnostics as well as for drug and vaccine discovery en_US
dc.description.sponsorship Armauer Hansen Research Institute (AHRI) Research Council of Norway (RCN) FRIMEDBIO en_US
dc.publisher nature.com en_US
dc.rights Attribution-NonCommercial-ShareAlike 3.0 United States *
dc.rights.uri http://creativecommons.org/licenses/by-nc-sa/3.0/us/ *
dc.subject Ample glycosylation en_US
dc.subject Membrane en_US
dc.subject Phenotypic en_US
dc.subject Mycobacterium en_US
dc.title Ample glycosylation in membrane and cell envelope proteins may explain the phenotypic diversity and virulence in the Mycobacterium tuberculosis complex en_US
dc.type Article en_US


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