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• W2971588807 abstract "Abstract O -linked protein glycosylation is a conserved feature of the Burkholderia genus. For Burkholderia cenocepacia , the addition of the trisaccharide β-Gal-(1,3)-α-GalNAc-(1,3)-β-GalNAc to membrane exported proteins is required for virulence and resistance to environmental stress. However, the underlying causes of the defects observed in the absence of glycosylation are unclear. This study demonstrates that the global B. cenocepacia proteome undergoes dramatic changes consistent with alterations in global transcriptional regulation in the absence of glycosylation. Using luciferase reporter assays and DNA cross-linking analysis, we confirm the repression of the master quorum sensing regulon CepR/I in response to the loss of glycosylation, which leads to the abolition of biofilm formation, defects in siderophore production, and reduced virulence. The abundance of most of the known glycosylated proteins did not significantly change in the glycosylation-defective mutants except for BCAL1086 and BCAL2974, which were found in reduced amount, suggesting they could be degraded. However, the loss of these two proteins was not responsible for driving the proteomic alterations, as well as for reduced virulence and siderophore production. Together, our results show that loss of glycosylation in B. cenocepacia results in a global cell reprogramming via alteration of the CepR/I regulon, which cannot be explained by the abundance changes in known B. cenocepacia glycoproteins. IMPORTANCE Protein glycosylation is increasingly recognised as a common protein modification in bacterial species. Despite this commonality our understanding of the role of most glycosylation systems in bacterial physiology and pathogenesis is incomplete. In this work, we investigated the effect of the disruption of O -linked glycosylation in the opportunistic pathogen Burkholderia cenocepacia using a combination of proteomic, molecular and phenotypic assays. We find that in contrast to recent findings on the N -linked glycosylation systems of Campylobacter jejuni, O -linked glycosylation does not appear to play a role in proteome stabilization of most glycoproteins. Our results reveal that virulence attenuation observed within glycosylation-null B. cenocepacia strains are consistent with alteration of the master virulence regulator CepR. The repression of CepR transcription and its associated phenotypes support a model in which the virulence defects observed in glycosylation-null strains are at least in part due to transcriptional alteration and not the direct result of the loss of glycosylation per-se . This research unravels the pleotropic effects of O -linked glycosylation in B. cenocepacia, demonstrating that its loss does not simply affect the stability of the glycoproteome, but also interferes with transcription and the broader proteome." @default.
• W2971588807 created "2019-09-12" @default.
• W2971588807 creator A5008818347 @default.
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• W2971588807 date "2019-09-04" @default.
• W2971588807 modified "2023-09-26" @default.
• W2971588807 title "Loss ofO-linked protein glycosylation inBurkholderia cenocepaciaimpairs biofilm formation and siderophore production via alteration of quorum sensing regulation" @default.
• W2971588807 cites W1515133252 @default.
• W2971588807 cites W1541706183 @default.
• W2971588807 cites W1542126860 @default.
• W2971588807 cites W1826402150 @default.
• W2971588807 cites W1849737063 @default.
• W2971588807 cites W1905597718 @default.
• W2971588807 cites W1938742570 @default.
• W2971588807 cites W1963056106 @default.
• W2971588807 cites W1969179300 @default.
• W2971588807 cites W1969483014 @default.
• W2971588807 cites W1971439989 @default.
• W2971588807 cites W1972435343 @default.
• W2971588807 cites W1981759007 @default.
• W2971588807 cites W1986656413 @default.
• W2971588807 cites W1987246303 @default.
• W2971588807 cites W1991690081 @default.
• W2971588807 cites W1996201718 @default.
• W2971588807 cites W2007918210 @default.
• W2971588807 cites W2010877382 @default.
• W2971588807 cites W2013740990 @default.
• W2971588807 cites W2016079458 @default.
• W2971588807 cites W2017007425 @default.
• W2971588807 cites W2023935690 @default.
• W2971588807 cites W2026318469 @default.
• W2971588807 cites W2034552316 @default.
• W2971588807 cites W2036699296 @default.
• W2971588807 cites W2043503013 @default.
• W2971588807 cites W2049562184 @default.
• W2971588807 cites W2052211754 @default.
• W2971588807 cites W2055613435 @default.
• W2971588807 cites W2064193137 @default.
• W2971588807 cites W2064977870 @default.
• W2971588807 cites W2068521408 @default.
• W2971588807 cites W2069692343 @default.
• W2971588807 cites W2072281124 @default.
• W2971588807 cites W2075797628 @default.
• W2971588807 cites W2079042331 @default.
• W2971588807 cites W2083216114 @default.
• W2971588807 cites W2087797688 @default.
• W2971588807 cites W2096911199 @default.
• W2971588807 cites W2097414503 @default.
• W2971588807 cites W2097905651 @default.
• W2971588807 cites W2098159838 @default.
• W2971588807 cites W2098332059 @default.
• W2971588807 cites W2098429327 @default.
• W2971588807 cites W2105167594 @default.
• W2971588807 cites W2106121058 @default.
• W2971588807 cites W2106801743 @default.
• W2971588807 cites W2106996236 @default.
• W2971588807 cites W2110219060 @default.
• W2971588807 cites W2115274774 @default.
• W2971588807 cites W2116386244 @default.
• W2971588807 cites W2117317865 @default.
• W2971588807 cites W2121103946 @default.
• W2971588807 cites W2121432800 @default.
• W2971588807 cites W2122262573 @default.
• W2971588807 cites W2125724353 @default.
• W2971588807 cites W2125863307 @default.
• W2971588807 cites W2128429807 @default.
• W2971588807 cites W2128671556 @default.
• W2971588807 cites W2131647525 @default.
• W2971588807 cites W2132666490 @default.
• W2971588807 cites W2134817486 @default.
• W2971588807 cites W2135581618 @default.
• W2971588807 cites W2143497668 @default.
• W2971588807 cites W2145253466 @default.
• W2971588807 cites W2145658355 @default.
• W2971588807 cites W2148306004 @default.
• W2971588807 cites W2148703390 @default.
• W2971588807 cites W2149341297 @default.
• W2971588807 cites W2149928655 @default.
• W2971588807 cites W2150232178 @default.
• W2971588807 cites W2150764734 @default.
• W2971588807 cites W2151906718 @default.
• W2971588807 cites W2154741848 @default.
• W2971588807 cites W2160197593 @default.
• W2971588807 cites W2160389489 @default.
• W2971588807 cites W2160959934 @default.
• W2971588807 cites W2161171034 @default.
• W2971588807 cites W2163626935 @default.
• W2971588807 cites W2164753077 @default.
• W2971588807 cites W2165401419 @default.
• W2971588807 cites W2165497874 @default.
• W2971588807 cites W2166421183 @default.
• W2971588807 cites W2167964916 @default.

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