A general approach to explore prokaryotic protein glycosylation reveals the unique surface layer modulation of an anammox bacterium.
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| Title: | A general approach to explore prokaryotic protein glycosylation reveals the unique surface layer modulation of an anammox bacterium. |
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| Authors: | Pabst, Martin1 (AUTHOR) m.pabst@tudelft.nl, Grouzdev, Denis S.2 (AUTHOR), Lawson, Christopher E.3 (AUTHOR), Kleikamp, Hugo B. C.1 (AUTHOR), de Ram, Carol1 (AUTHOR), Louwen, Rogier4 (AUTHOR), Lin, Yue Mei1 (AUTHOR), Lücker, Sebastian5 (AUTHOR), van Loosdrecht, Mark C. M.1 (AUTHOR), Laureni, Michele1 (AUTHOR) |
| Source: | ISME Journal: Multidisciplinary Journal of Microbial Ecology. Feb2022, Vol. 16 Issue 2, p346-357. 12p. |
| Abstract: | The enormous chemical diversity and strain variability of prokaryotic protein glycosylation makes their large-scale exploration exceptionally challenging. Therefore, despite the universal relevance of protein glycosylation across all domains of life, the understanding of their biological significance and the evolutionary forces shaping oligosaccharide structures remains highly limited. Here, we report on a newly established mass binning glycoproteomics approach that establishes the chemical identity of the carbohydrate components and performs untargeted exploration of prokaryotic oligosaccharides from large-scale proteomics data directly. We demonstrate our approach by exploring an enrichment culture of the globally relevant anaerobic ammonium-oxidizing bacterium Ca. Kuenenia stuttgartiensis. By doing so we resolve a remarkable array of oligosaccharides, which are produced by two seemingly unrelated biosynthetic routes, and which modify the same surface-layer protein simultaneously. More intriguingly, the investigated strain also accomplished modulation of highly specialized sugars, supposedly in response to its energy metabolism—the anaerobic oxidation of ammonium—which depends on the acquisition of substrates of opposite charges. Ultimately, we provide a systematic approach for the compositional exploration of prokaryotic protein glycosylation, and reveal a remarkable example for the evolution of complex oligosaccharides in bacteria. [ABSTRACT FROM AUTHOR] |
| Copyright of ISME Journal: Multidisciplinary Journal of Microbial Ecology is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 154791875 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: A general approach to explore prokaryotic protein glycosylation reveals the unique surface layer modulation of an anammox bacterium. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Pabst%2C+Martin%22">Pabst, Martin</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> m.pabst@tudelft.nl</i><br /><searchLink fieldCode="AR" term="%22Grouzdev%2C+Denis+S%2E%22">Grouzdev, Denis S.</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lawson%2C+Christopher+E%2E%22">Lawson, Christopher E.</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Kleikamp%2C+Hugo+B%2E+C%2E%22">Kleikamp, Hugo B. C.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22de+Ram%2C+Carol%22">de Ram, Carol</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Louwen%2C+Rogier%22">Louwen, Rogier</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lin%2C+Yue+Mei%22">Lin, Yue Mei</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lücker%2C+Sebastian%22">Lücker, Sebastian</searchLink><relatesTo>5</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22van+Loosdrecht%2C+Mark+C%2E+M%2E%22">van Loosdrecht, Mark C. M.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Laureni%2C+Michele%22">Laureni, Michele</searchLink><relatesTo>1</relatesTo> (AUTHOR) – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22ISME+Journal%3A+Multidisciplinary+Journal+of+Microbial+Ecology%22">ISME Journal: Multidisciplinary Journal of Microbial Ecology</searchLink>. Feb2022, Vol. 16 Issue 2, p346-357. 12p. – Name: Abstract Label: Abstract Group: Ab Data: The enormous chemical diversity and strain variability of prokaryotic protein glycosylation makes their large-scale exploration exceptionally challenging. Therefore, despite the universal relevance of protein glycosylation across all domains of life, the understanding of their biological significance and the evolutionary forces shaping oligosaccharide structures remains highly limited. Here, we report on a newly established mass binning glycoproteomics approach that establishes the chemical identity of the carbohydrate components and performs untargeted exploration of prokaryotic oligosaccharides from large-scale proteomics data directly. We demonstrate our approach by exploring an enrichment culture of the globally relevant anaerobic ammonium-oxidizing bacterium Ca. Kuenenia stuttgartiensis. By doing so we resolve a remarkable array of oligosaccharides, which are produced by two seemingly unrelated biosynthetic routes, and which modify the same surface-layer protein simultaneously. More intriguingly, the investigated strain also accomplished modulation of highly specialized sugars, supposedly in response to its energy metabolism—the anaerobic oxidation of ammonium—which depends on the acquisition of substrates of opposite charges. Ultimately, we provide a systematic approach for the compositional exploration of prokaryotic protein glycosylation, and reveal a remarkable example for the evolution of complex oligosaccharides in bacteria. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of ISME Journal: Multidisciplinary Journal of Microbial Ecology is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1038/s41396-021-01073-y Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 12 StartPage: 346 Titles: – TitleFull: A general approach to explore prokaryotic protein glycosylation reveals the unique surface layer modulation of an anammox bacterium. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Pabst, Martin – PersonEntity: Name: NameFull: Grouzdev, Denis S. – PersonEntity: Name: NameFull: Lawson, Christopher E. – PersonEntity: Name: NameFull: Kleikamp, Hugo B. C. – PersonEntity: Name: NameFull: de Ram, Carol – PersonEntity: Name: NameFull: Louwen, Rogier – PersonEntity: Name: NameFull: Lin, Yue Mei – PersonEntity: Name: NameFull: Lücker, Sebastian – PersonEntity: Name: NameFull: van Loosdrecht, Mark C. M. – PersonEntity: Name: NameFull: Laureni, Michele IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 02 Text: Feb2022 Type: published Y: 2022 Identifiers: – Type: issn-print Value: 17517362 Numbering: – Type: volume Value: 16 – Type: issue Value: 2 Titles: – TitleFull: ISME Journal: Multidisciplinary Journal of Microbial Ecology Type: main |
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