Preventing unintended proteolysis in plant protein biofactories
Identifieur interne : 001D84 ( Main/Exploration ); précédent : 001D83; suivant : 001D85Preventing unintended proteolysis in plant protein biofactories
Auteurs : Meriem Benchabane ; Charles Goulet ; Daniel Rivard ; Loïc Faye [France] ; Véronique Gomord [France] ; Dominique Michaud [Canada]Source :
- Plant Biotechnology Journal [ 1467-7644 ] ; 2008-09.
English descriptors
- Teeft :
- Acad, Accumulation rates, Amino, Amino acids, Apoplast, Arabidopsis, Authors journal compilation, Badri, Benchabane, Biochem, Biol, Biotechnol, Biotechnology, Blackwell publishing, Cell secretory pathway, Chloroplast, Cholera toxin, Christou, Companion protease inhibitors, Continuous secretion, Crude extracts, Crude preparations, Culture media, Culture medium, Cysteine, Cysteine proteases, Cytosol, Daniell, Degradation, Endogenous, Endogenous proteases, Endoplasmic, Endoplasmic reticulum, Epidermal growth factor, Escherichia coli, Extracellular, Extracellular medium, Extracellular secretion, Faye, Fischer, Fusion partners, Golgi apparatus, Gomord, Goulet, Heterogeneity, Heterologous, Heterologous environments, Heterologous protein production, High levels, Host plant, Human growth hormone, Inhibitor, Komarnytsky, Last decade, Leaf tissues, Meriem, Meriem benchabane, Methods biotechnol, Michaud, Natl, Organelle, Overall stability, Pathway, Peptide, Pharmaceutical, Phenylmethylsulphonyl fluoride, Physiol, Plant biol, Plant biotechnol, Plant biotechnology journal, Plant cell, Plant cell cultures, Plant cells, Plant crude extracts, Plant physiol, Plant proteases, Plant systems, Plant tissues, Planta, Polypeptide, Positive impact, Proc, Promoter, Protease, Protease activity, Protease inhibitors, Protein, Protein accumulation, Protein bodies, Protein degradation, Protein extraction, Protein extracts, Protein levels, Protein loss, Protein product, Protein production, Protein recovery, Protein stability, Protein storage vacuoles, Proteolysis, Proteolytic, Proteolytic enzymes, Recombinant, Recombinant antibodies, Recombinant protease inhibitors, Recombinant protein, Recombinant protein production, Recombinant proteins, Retention signal, Reticulum, Rivard, Same protein, Scfv, Schillberg, Secretory, Secretory pathway, Serine, Several proteins, Signal peptide, Similar manner, Stoger, Streatfield, Structural characteristics, Structural heterogeneity, Suitable destination, Surface antigen, Tabacum, Tabacum leaf, Tobacco cells, Transgene, Transgene expression, Transgene sequence, Transgenic, Transgenic plants, Transgenic tobacco, Trends biotechnol, Trends plant, Twyman, Useful proteins, Vaccine, Vacuole, Vierstra, Vitale.
Abstract
Numerous reports have been published over the last decade assessing the potential of plants as useful hosts for the heterologous expression of clinically useful proteins. Significant progress has been made, in particular, in optimizing transgene transcription and translation in plants, and in elucidating the complex post‐translational modifications of proteins typical of the plant cell machinery. In this article, we address the important issue of recombinant protein degradation in plant expression platforms, which directly impacts on the final yield, homogeneity and overall quality of the resulting protein product. Unlike several more stable and structurally less complex pharmaceuticals, recombinant proteins present a natural tendency to structural heterogeneity, resulting in part from the inherent instability of polypeptide chains expressed in heterologous environments. Proteolytic processing, notably, may dramatically alter the structural integrity and overall accumulation of recombinant proteins in plant expression systems, both in planta during expression and ex planta after extraction. In this article, we describe the current strategies proposed to minimize protein hydrolysis in plant protein factories, including organ‐specific transgene expression, organelle‐specific protein targeting, the grafting of stabilizing protein domains to labile proteins, protein secretion in natural fluids and the co‐expression of companion protease inhibitors.
Url:
DOI: 10.1111/j.1467-7652.2008.00344.x
Affiliations:
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to="648">648</biblScope><biblScope unit="page-count">16</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="2008-09">2008-09</date></imprint><idno type="ISSN">1467-7644</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1467-7644</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Accumulation rates</term><term>Amino</term><term>Amino acids</term><term>Apoplast</term><term>Arabidopsis</term><term>Authors journal compilation</term><term>Badri</term><term>Benchabane</term><term>Biochem</term><term>Biol</term><term>Biotechnol</term><term>Biotechnology</term><term>Blackwell publishing</term><term>Cell secretory pathway</term><term>Chloroplast</term><term>Cholera toxin</term><term>Christou</term><term>Companion protease inhibitors</term><term>Continuous secretion</term><term>Crude extracts</term><term>Crude preparations</term><term>Culture media</term><term>Culture medium</term><term>Cysteine</term><term>Cysteine proteases</term><term>Cytosol</term><term>Daniell</term><term>Degradation</term><term>Endogenous</term><term>Endogenous proteases</term><term>Endoplasmic</term><term>Endoplasmic reticulum</term><term>Epidermal growth factor</term><term>Escherichia coli</term><term>Extracellular</term><term>Extracellular medium</term><term>Extracellular secretion</term><term>Faye</term><term>Fischer</term><term>Fusion partners</term><term>Golgi apparatus</term><term>Gomord</term><term>Goulet</term><term>Heterogeneity</term><term>Heterologous</term><term>Heterologous environments</term><term>Heterologous protein production</term><term>High levels</term><term>Host plant</term><term>Human growth hormone</term><term>Inhibitor</term><term>Komarnytsky</term><term>Last decade</term><term>Leaf tissues</term><term>Meriem</term><term>Meriem benchabane</term><term>Methods biotechnol</term><term>Michaud</term><term>Natl</term><term>Organelle</term><term>Overall stability</term><term>Pathway</term><term>Peptide</term><term>Pharmaceutical</term><term>Phenylmethylsulphonyl fluoride</term><term>Physiol</term><term>Plant biol</term><term>Plant biotechnol</term><term>Plant biotechnology journal</term><term>Plant cell</term><term>Plant cell cultures</term><term>Plant cells</term><term>Plant crude extracts</term><term>Plant physiol</term><term>Plant proteases</term><term>Plant systems</term><term>Plant tissues</term><term>Planta</term><term>Polypeptide</term><term>Positive impact</term><term>Proc</term><term>Promoter</term><term>Protease</term><term>Protease activity</term><term>Protease inhibitors</term><term>Protein</term><term>Protein accumulation</term><term>Protein bodies</term><term>Protein degradation</term><term>Protein extraction</term><term>Protein extracts</term><term>Protein levels</term><term>Protein loss</term><term>Protein product</term><term>Protein production</term><term>Protein recovery</term><term>Protein stability</term><term>Protein storage vacuoles</term><term>Proteolysis</term><term>Proteolytic</term><term>Proteolytic enzymes</term><term>Recombinant</term><term>Recombinant antibodies</term><term>Recombinant protease inhibitors</term><term>Recombinant protein</term><term>Recombinant protein production</term><term>Recombinant proteins</term><term>Retention signal</term><term>Reticulum</term><term>Rivard</term><term>Same protein</term><term>Scfv</term><term>Schillberg</term><term>Secretory</term><term>Secretory pathway</term><term>Serine</term><term>Several proteins</term><term>Signal peptide</term><term>Similar manner</term><term>Stoger</term><term>Streatfield</term><term>Structural characteristics</term><term>Structural heterogeneity</term><term>Suitable destination</term><term>Surface antigen</term><term>Tabacum</term><term>Tabacum leaf</term><term>Tobacco cells</term><term>Transgene</term><term>Transgene expression</term><term>Transgene sequence</term><term>Transgenic</term><term>Transgenic plants</term><term>Transgenic tobacco</term><term>Trends biotechnol</term><term>Trends plant</term><term>Twyman</term><term>Useful proteins</term><term>Vaccine</term><term>Vacuole</term><term>Vierstra</term><term>Vitale</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Numerous reports have been published over the last decade assessing the potential of plants as useful hosts for the heterologous expression of clinically useful proteins. Significant progress has been made, in particular, in optimizing transgene transcription and translation in plants, and in elucidating the complex post‐translational modifications of proteins typical of the plant cell machinery. In this article, we address the important issue of recombinant protein degradation in plant expression platforms, which directly impacts on the final yield, homogeneity and overall quality of the resulting protein product. Unlike several more stable and structurally less complex pharmaceuticals, recombinant proteins present a natural tendency to structural heterogeneity, resulting in part from the inherent instability of polypeptide chains expressed in heterologous environments. Proteolytic processing, notably, may dramatically alter the structural integrity and overall accumulation of recombinant proteins in plant expression systems, both in planta during expression and ex planta after extraction. In this article, we describe the current strategies proposed to minimize protein hydrolysis in plant protein factories, including organ‐specific transgene expression, organelle‐specific protein targeting, the grafting of stabilizing protein domains to labile proteins, protein secretion in natural fluids and the co‐expression of companion protease inhibitors.</div></front></TEI><affiliations><list><country><li>Canada</li><li>France</li></country><region><li>Haute-Normandie</li><li>Région Normandie</li></region><settlement><li>Mont‐Saint‐Aignan</li></settlement><orgName><li>Université de Rouen</li></orgName></list><tree><noCountry><name sortKey="Benchabane, Meriem" sort="Benchabane, Meriem" uniqKey="Benchabane M" first="Meriem" last="Benchabane">Meriem Benchabane</name><name sortKey="Goulet, Charles" sort="Goulet, Charles" uniqKey="Goulet C" first="Charles" last="Goulet">Charles Goulet</name><name sortKey="Rivard, Daniel" sort="Rivard, Daniel" uniqKey="Rivard D" first="Daniel" last="Rivard">Daniel Rivard</name></noCountry><country name="France"><region name="Région Normandie"><name sortKey="Faye, Loic" sort="Faye, Loic" uniqKey="Faye L" first="Loïc" last="Faye">Loïc Faye</name></region><name sortKey="Gomord, Veronique" sort="Gomord, Veronique" uniqKey="Gomord V" first="Véronique" last="Gomord">Véronique Gomord</name></country><country name="Canada"><noRegion><name sortKey="Michaud, Dominique" sort="Michaud, Dominique" uniqKey="Michaud D" first="Dominique" last="Michaud">Dominique Michaud</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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