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
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.)
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  Data: Generation of Arabidopsis thaliana plants with complex N-glycans lacking β1,2-linked xylose and core α1,3-linked fucose
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  Data: <searchLink fieldCode="JN" term="%22FEBS+Letters%22">FEBS Letters</searchLink>. Mar2004, Vol. 561 Issue 1-3, p132. 5p.
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  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>
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  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]
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  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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      – Type: doi
        Value: 10.1016/S0014-5793(04)00150-4
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      – Code: eng
        Text: English
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        Type: general
      – SubjectFull: Glycosyltransferases
        Type: general
      – SubjectFull: Plant enzymes
        Type: general
      – SubjectFull: Arabidopsis thaliana
        Type: general
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      – TitleFull: Generation of Arabidopsis thaliana plants with complex N-glycans lacking β1,2-linked xylose and core α1,3-linked fucose
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              Text: Mar2004
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