Generation of Arabidopsis thaliana plants with complex N-glycans lacking β1,2-linked xylose and core α1,3-linked fucose
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| Title: | Generation of Arabidopsis thaliana plants with complex N-glycans lacking β1,2-linked xylose and core α1,3-linked fucose |
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| Authors: | Strasser, R.1 richard.strasser@boku.ac.at, Altmann, F.2, Mach, L.1, Glössl, J.1, Steinkellner, H.1 |
| Source: | FEBS Letters. Mar2004, Vol. 561 Issue 1-3, p132. 5p. |
| Subjects: | Fucosyltransferases, Glycosyltransferases, Plant enzymes, Arabidopsis thaliana |
| Abstract: | The plant glycosyltransferases, β1,2-xylosyltransferase (XylT) and core α1,3-fucosyltransferase (FucT), are responsible for the transfer of β1,2-linked xylose and core α1,3-linked fucose residues to glycoprotein N-glycans. These glycan epitopes are not present in humans and thus may cause immunological responses, which represent a limitation for the therapeutic use of recombinant mammalian glycoproteins produced in transgenic plants. Here we report the genetic modification of the N-glycosylation pathway in Arabidopsis thaliana plants. Knockout plants were generated with complete deficiency of XylT and FucT. These plants lack antigenic protein-bound N-glycans and instead synthesise predominantly structures with two terminal βN-acetylglucosamine residues (GlcNAc2Man3GlcNAc2). [Copyright &y& Elsevier] |
| Copyright of FEBS Letters is the property of Wiley-Blackwell 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: 12435479 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Generation of Arabidopsis thaliana plants with complex N-glycans lacking β1,2-linked xylose and core α1,3-linked fucose – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Strasser%2C+R%2E%22">Strasser, R.</searchLink><relatesTo>1</relatesTo><i> richard.strasser@boku.ac.at</i><br /><searchLink fieldCode="AR" term="%22Altmann%2C+F%2E%22">Altmann, F.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Mach%2C+L%2E%22">Mach, L.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Glössl%2C+J%2E%22">Glössl, J.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Steinkellner%2C+H%2E%22">Steinkellner, H.</searchLink><relatesTo>1</relatesTo> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22FEBS+Letters%22">FEBS Letters</searchLink>. Mar2004, Vol. 561 Issue 1-3, p132. 5p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Fucosyltransferases%22">Fucosyltransferases</searchLink><br /><searchLink fieldCode="DE" term="%22Glycosyltransferases%22">Glycosyltransferases</searchLink><br /><searchLink fieldCode="DE" term="%22Plant+enzymes%22">Plant enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Arabidopsis+thaliana%22">Arabidopsis thaliana</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: The plant glycosyltransferases, β1,2-xylosyltransferase (XylT) and core α1,3-fucosyltransferase (FucT), are responsible for the transfer of β1,2-linked xylose and core α1,3-linked fucose residues to glycoprotein N-glycans. These glycan epitopes are not present in humans and thus may cause immunological responses, which represent a limitation for the therapeutic use of recombinant mammalian glycoproteins produced in transgenic plants. Here we report the genetic modification of the N-glycosylation pathway in Arabidopsis thaliana plants. Knockout plants were generated with complete deficiency of XylT and FucT. These plants lack antigenic protein-bound N-glycans and instead synthesise predominantly structures with two terminal βN-acetylglucosamine residues (GlcNAc2Man3GlcNAc2). [Copyright &y& Elsevier] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of FEBS Letters is the property of Wiley-Blackwell 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: 10.1016/S0014-5793(04)00150-4 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 5 StartPage: 132 Subjects: – SubjectFull: Fucosyltransferases Type: general – SubjectFull: Glycosyltransferases Type: general – SubjectFull: Plant enzymes Type: general – SubjectFull: Arabidopsis thaliana Type: general Titles: – TitleFull: Generation of Arabidopsis thaliana plants with complex N-glycans lacking β1,2-linked xylose and core α1,3-linked fucose Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Strasser, R. – PersonEntity: Name: NameFull: Altmann, F. – PersonEntity: Name: NameFull: Mach, L. – PersonEntity: Name: NameFull: Glössl, J. – PersonEntity: Name: NameFull: Steinkellner, H. IsPartOfRelationships: – BibEntity: Dates: – D: 12 M: 03 Text: Mar2004 Type: published Y: 2004 Identifiers: – Type: issn-print Value: 00145793 Numbering: – Type: volume Value: 561 – Type: issue Value: 1-3 Titles: – TitleFull: FEBS Letters Type: main |
| ResultId | 1 |