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Plant glyco-biotechnology on the way to synthetic biology

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Frontiers in Plant Science

Frontiers Media S.A.

glycoengineering, plant, glycosyltransferase, CTS, sub-Golgi targeting

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      Abstract

      Plants are increasingly being used for the production of recombinant proteins. One reason is that plants are highly amenable to glycan engineering processes and allow the production of therapeutic proteins with increased efficacies due to optimized glycosylation profiles. Removal and insertion of glycosylation reactions by knock-out/knock-down approaches and introduction of glycosylation enzymes have paved the way for the humanization of the plant glycosylation pathway. The insertion of heterologous enzymes at exactly the right stage of the existing glycosylation pathway has turned out to be of utmost importance. To enable such precise targeting chimeric enzymes have been constructed. In this short review we will exemplify the importance of correct targeting of glycosyltransferases, we will give an overview of the targeting mechanism of glycosyltransferases, describe chimeric enzymes used in plant N-glycosylation engineering and illustrate how plant glycoengineering builds on the tools offered by synthetic biology to construct such chimeric enzymes.

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      Most cited references 96

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      Biological roles of oligosaccharides: all of the theories are correct.

       A Varki (1993)
      Many different theories have been advanced concerning the biological roles of the oligosaccharide units of individual classes of glycoconjugates. Analysis of the evidence indicates that while all of these theories are correct, exceptions to each can also be found. The biological roles of oligosaccharides appear to span the spectrum from those that are trivial, to those that are crucial for the development, growth, function or survival of an organism. Some general principles emerge. First, it is difficult to predict a priori the functions a given oligosaccharide on a given glycoconjugate might be mediating, or their relative importance to the organism. Second, the same oligosaccharide sequence may mediate different functions at different locations within the same organism, or at different times in its ontogeny or life cycle. Third, the more specific and crucial biological roles of oligosaccharides are often mediated by unusual oligosaccharide sequences, unusual presentations of common terminal sequences, or by further modifications of the sugars themselves. However, such oligosaccharide sequences are also more likely to be targets for recognition by pathogenic toxins and microorganisms. As such, they are subject to more intra- and inter-species variation because of ongoing host-pathogen interactions during evolution. In the final analysis, the only common features of the varied functions of oligosaccharides are that they either mediate 'specific recognition' events or that they provide 'modulation' of biological processes. In so doing, they generate much of the functional diversity required for the development and differentiation of complex organisms, and for their interactions with other organisms in the environment.
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        Glycosylation in cellular mechanisms of health and disease.

        Glycosylation produces an abundant, diverse, and highly regulated repertoire of cellular glycans that are frequently attached to proteins and lipids. The past decade of research on glycan function has revealed that the enzymes responsible for glycosylation-the glycosyltransferases and glycosidases-are essential in the development and physiology of living organisms. Glycans participate in many key biological processes including cell adhesion, molecular trafficking and clearance, receptor activation, signal transduction, and endocytosis. This review discusses the increasingly sophisticated molecular mechanisms being discovered by which mammalian glycosylation governs physiology and contributes to disease.
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          Intracellular functions of N-linked glycans.

          N-linked oligosaccharides arise when blocks of 14 sugars are added cotranslationally to newly synthesized polypeptides in the endoplasmic reticulum (ER). These glycans are then subjected to extensive modification as the glycoproteins mature and move through the ER via the Golgi complex to their final destinations inside and outside the cell. In the ER and in the early secretory pathway, where the repertoire of oligosaccharide structures is still rather small, the glycans play a pivotal role in protein folding, oligomerization, quality control, sorting, and transport. They are used as universal "tags" that allow specific lectins and modifying enzymes to establish order among the diversity of maturing glycoproteins. In the Golgi complex, the glycans acquire more complex structures and a new set of functions. The division of synthesis and processing between the ER and the Golgi complex represents an evolutionary adaptation that allows efficient exploitation of the potential of oligosaccharides.
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            Author and article information

            Affiliations
            Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences Vienna, Austria
            Author notes

            Edited by: Els J. M. Van Damme, Ghent University, Belgium

            Reviewed by: Beronda L. Montgomery, Michigan State University, USA; Bjoern Usadel, RWTH Aachen University, Germany; Thomas De Meyer, Vlaams Instituut voor Biotechnologie, Belgium

            *Correspondence: Herta Steinkellner, Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria e-mail: herta.steinkellner@ 123456boku.ac.at

            This article was submitted to Plant Physiology, a section of the journal Frontiers in Plant Science.

            Contributors
            Journal
            Front Plant Sci
            Front Plant Sci
            Front. Plant Sci.
            Frontiers in Plant Science
            Frontiers Media S.A.
            1664-462X
            08 October 2014
            2014
            : 5
            4189330 10.3389/fpls.2014.00523
            Copyright © 2014 Loos and Steinkellner.

            This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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            Figures: 3, Tables: 0, Equations: 0, References: 99, Pages: 10, Words: 0
            Categories
            Plant Science
            Review Article

            Plant science & Botany

            sub-golgi targeting, cts, glycosyltransferase, plant, glycoengineering

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