Influence of elastin‐like peptide fusions on the quantity and quality of a tobacco‐derived human immunodeficiency virus‐neutralizing antibody
Identifieur interne : 002881 ( Main/Exploration ); précédent : 002880; suivant : 002882Influence of elastin‐like peptide fusions on the quantity and quality of a tobacco‐derived human immunodeficiency virus‐neutralizing antibody
Auteurs : Doreen M. Floss [Allemagne] ; Markus Sack [Allemagne] ; Elsa Arcalis [Autriche] ; Johannes Stadlmann [Autriche] ; Heribert Quendler [Autriche] ; Thomas Rademacher [Allemagne] ; Eva Stoger [Autriche] ; Jürgen Scheller [Allemagne] ; Rainer Fischer [Allemagne] ; Udo Conrad [Allemagne]Source :
- Plant Biotechnology Journal [ 1467-7644 ] ; 2009-12.
English descriptors
- Teeft :
- Accumulation levels, Alexa fluor, Amersham biosciences, Antibody, Antibody assembly, Antibody chains, Antibody fragments, Antibody light chain, Antibody preparations, Antibody variant, Antibody variants, Assay, Authors journal compilation, Biacore analysis, Binding curves, Binding kinetics, Biotechnol, Biotechnology, Blackwell, Blackwell publishing, Cell wall, Chilkoti, Chinese hamster ovary cells, Christian albrechts university, Complete antibodies, Complex type, Constitutive expression, Constitutive mosaic virus, Coomassie staining, Crude seed, Different antibodies, Dimer, Doreen, Double arrow, Double band, Effector functions, Electron microscopy, Endoglucanase activity, Endoplasmic reticulum, Escherichia coli, Expert opin, Expression cassettes, Floss, Functional virus antibodies, Fusion, Fusion protein, Fusion proteins, Fusion technology, Glass slides, Glcnac, Glycans, Gold particles, Haploid technology, Heavy chain, Heavy chains, Higher temperatures, Human therapeutics, Human virus, Humana press, Individual antibody chains, Inhibitory concentration, Insoluble material, Inverse transition cycling, Kappa light chain antibody, Lanes figure, Leaf extracts, Life sciences, Light chain, Light chains, Lipid bodies, Liquid nitrogen, Localization, Maize endosperm, Mass spectrometry, Mature seeds, Microbicide components, Molecular basis, Molecular biology, Molecular weight, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Natl acad, Natural resources, Negative impact, Neutralization, Neutralization assay, Neutralization capacity, Neutralizing activity, Nicotiana benthamiana, Nicotiana tabacum, Nucleic acids, Other compartment, Peptide, Pharmaceutical proteins, Phase transition, Phosphate buffer, Plant biotechnol, Plant biotechnology journal, Plant transformation, Polypeptide, Polypeptide fusions, Possible combinations, Promising tools, Promoter, Protein, Protein storage vacuoles, Rademacher, Ramessar, Recombinant, Recombinant antibodies, Recombinant antibody, Recombinant proteins, Relative activities, Relative activity, Room temperature, Sandwich elisa, Scheller, Seed extraction buffer, Seed tissue, Sexual transmission, Single glcnac residues, Sodium dodecyl, Stoger, Surface plasmon resonance spectroscopy, Syncytium inhibition assay, Tobacco leaf, Tobacco plants, Tobacco seeds, Transgenic, Transgenic plants, Transgenic tobacco, Transgenic tobacco plants, Trends plant, Uorescence microscopy, Urry, Vaccine, Vaccine candidates, Variant, Western blot, Western blot analysis.
Abstract
The use of vaginal microbicides containing human immunodeficiency virus (HIV)‐neutralizing antibodies (nAbs) is a promising strategy to prevent HIV‐1 infection. Although antibodies are predominantly manufactured using mammalian cells, elastin‐like peptide (ELP) fusion technology improves the stability of recombinant, plant‐produced proteins and facilitates their purification, making plants an alternative platform for antibody production. We generated transgenic tobacco plants accumulating four different formats of the anti‐HIV‐1 antibody 2G12 in the endoplasmic reticulum (ER), i.e. with ELP on either the light or heavy chain, on both, or on neither. Detailed analysis of affinity‐purified antibodies by surface plasmon resonance spectroscopy showed that the kinetic binding parameters of all formats were identical to 2G12 lacking ELP produced in Chinese hamster ovary (CHO) cells. Importantly, protein purification from seeds by inverse transition cycling (ITC) did not affect the binding kinetics. Analysis of heavy chain N‐glycans from leaf‐derived antibodies showed that retrieval to the ER was efficient for all formats. In seeds, however, N‐glycans on the naked antibody were extensively trimmed compared with those on the ELP fusion formats, and were localized to a different subcellular compartment. The in vitro HIV‐neutralization properties of the tobacco‐derived 2G12 were equivalent to or better than those of the CHO counterpart.
Url:
DOI: 10.1111/j.1467-7652.2009.00452.x
Affiliations:
- Allemagne, Autriche
- District de Cologne, Rhénanie-du-Nord-Westphalie, Schleswig-Holstein, Vienne (Autriche)
- Aix-la-Chapelle, Kiel, Vienne (Autriche)
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level="j" type="alt">PLANT BIOTECHNOLOGY JOURNAL</title><idno type="ISSN">1467-7644</idno><idno type="eISSN">1467-7652</idno><imprint><biblScope unit="vol">7</biblScope><biblScope unit="issue">9</biblScope><biblScope unit="page" from="899">899</biblScope><biblScope unit="page" to="913">913</biblScope><biblScope unit="page-count">15</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="2009-12">2009-12</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>Accumulation levels</term><term>Alexa fluor</term><term>Amersham biosciences</term><term>Antibody</term><term>Antibody assembly</term><term>Antibody chains</term><term>Antibody fragments</term><term>Antibody light chain</term><term>Antibody preparations</term><term>Antibody variant</term><term>Antibody variants</term><term>Assay</term><term>Authors journal compilation</term><term>Biacore analysis</term><term>Binding curves</term><term>Binding kinetics</term><term>Biotechnol</term><term>Biotechnology</term><term>Blackwell</term><term>Blackwell publishing</term><term>Cell wall</term><term>Chilkoti</term><term>Chinese hamster ovary cells</term><term>Christian albrechts university</term><term>Complete antibodies</term><term>Complex type</term><term>Constitutive expression</term><term>Constitutive mosaic virus</term><term>Coomassie staining</term><term>Crude seed</term><term>Different antibodies</term><term>Dimer</term><term>Doreen</term><term>Double arrow</term><term>Double band</term><term>Effector functions</term><term>Electron microscopy</term><term>Endoglucanase activity</term><term>Endoplasmic reticulum</term><term>Escherichia coli</term><term>Expert opin</term><term>Expression cassettes</term><term>Floss</term><term>Functional virus antibodies</term><term>Fusion</term><term>Fusion protein</term><term>Fusion proteins</term><term>Fusion technology</term><term>Glass slides</term><term>Glcnac</term><term>Glycans</term><term>Gold particles</term><term>Haploid technology</term><term>Heavy chain</term><term>Heavy chains</term><term>Higher temperatures</term><term>Human therapeutics</term><term>Human virus</term><term>Humana press</term><term>Individual antibody chains</term><term>Inhibitory concentration</term><term>Insoluble material</term><term>Inverse transition cycling</term><term>Kappa light chain antibody</term><term>Lanes figure</term><term>Leaf extracts</term><term>Life sciences</term><term>Light chain</term><term>Light chains</term><term>Lipid bodies</term><term>Liquid nitrogen</term><term>Localization</term><term>Maize endosperm</term><term>Mass spectrometry</term><term>Mature seeds</term><term>Microbicide components</term><term>Molecular basis</term><term>Molecular biology</term><term>Molecular weight</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal antibody</term><term>Natl acad</term><term>Natural resources</term><term>Negative impact</term><term>Neutralization</term><term>Neutralization assay</term><term>Neutralization capacity</term><term>Neutralizing activity</term><term>Nicotiana benthamiana</term><term>Nicotiana tabacum</term><term>Nucleic acids</term><term>Other compartment</term><term>Peptide</term><term>Pharmaceutical proteins</term><term>Phase transition</term><term>Phosphate buffer</term><term>Plant biotechnol</term><term>Plant biotechnology journal</term><term>Plant transformation</term><term>Polypeptide</term><term>Polypeptide fusions</term><term>Possible combinations</term><term>Promising tools</term><term>Promoter</term><term>Protein</term><term>Protein storage vacuoles</term><term>Rademacher</term><term>Ramessar</term><term>Recombinant</term><term>Recombinant antibodies</term><term>Recombinant antibody</term><term>Recombinant proteins</term><term>Relative activities</term><term>Relative activity</term><term>Room temperature</term><term>Sandwich elisa</term><term>Scheller</term><term>Seed extraction buffer</term><term>Seed tissue</term><term>Sexual transmission</term><term>Single glcnac residues</term><term>Sodium dodecyl</term><term>Stoger</term><term>Surface plasmon resonance spectroscopy</term><term>Syncytium inhibition assay</term><term>Tobacco leaf</term><term>Tobacco plants</term><term>Tobacco seeds</term><term>Transgenic</term><term>Transgenic plants</term><term>Transgenic tobacco</term><term>Transgenic tobacco plants</term><term>Trends plant</term><term>Uorescence microscopy</term><term>Urry</term><term>Vaccine</term><term>Vaccine candidates</term><term>Variant</term><term>Western blot</term><term>Western blot analysis</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The use of vaginal microbicides containing human immunodeficiency virus (HIV)‐neutralizing antibodies (nAbs) is a promising strategy to prevent HIV‐1 infection. Although antibodies are predominantly manufactured using mammalian cells, elastin‐like peptide (ELP) fusion technology improves the stability of recombinant, plant‐produced proteins and facilitates their purification, making plants an alternative platform for antibody production. We generated transgenic tobacco plants accumulating four different formats of the anti‐HIV‐1 antibody 2G12 in the endoplasmic reticulum (ER), i.e. with ELP on either the light or heavy chain, on both, or on neither. Detailed analysis of affinity‐purified antibodies by surface plasmon resonance spectroscopy showed that the kinetic binding parameters of all formats were identical to 2G12 lacking ELP produced in Chinese hamster ovary (CHO) cells. Importantly, protein purification from seeds by inverse transition cycling (ITC) did not affect the binding kinetics. Analysis of heavy chain N‐glycans from leaf‐derived antibodies showed that retrieval to the ER was efficient for all formats. In seeds, however, N‐glycans on the naked antibody were extensively trimmed compared with those on the ELP fusion formats, and were localized to a different subcellular compartment. The in vitro HIV‐neutralization properties of the tobacco‐derived 2G12 were equivalent to or better than those of the CHO counterpart.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Autriche</li></country><region><li>District de Cologne</li><li>Rhénanie-du-Nord-Westphalie</li><li>Schleswig-Holstein</li><li>Vienne (Autriche)</li></region><settlement><li>Aix-la-Chapelle</li><li>Kiel</li><li>Vienne (Autriche)</li></settlement></list><tree><country name="Allemagne"><noRegion><name sortKey="Floss, Doreen M" sort="Floss, Doreen M" uniqKey="Floss D" first="Doreen M." last="Floss">Doreen M. Floss</name></noRegion><name sortKey="Conrad, Udo" sort="Conrad, Udo" uniqKey="Conrad U" first="Udo" last="Conrad">Udo Conrad</name><name sortKey="Conrad, Udo" sort="Conrad, Udo" uniqKey="Conrad U" first="Udo" last="Conrad">Udo Conrad</name><name sortKey="Fischer, Rainer" sort="Fischer, Rainer" uniqKey="Fischer R" first="Rainer" last="Fischer">Rainer Fischer</name><name sortKey="Rademacher, Thomas" sort="Rademacher, Thomas" uniqKey="Rademacher T" first="Thomas" last="Rademacher">Thomas Rademacher</name><name sortKey="Sack, Markus" sort="Sack, Markus" uniqKey="Sack M" first="Markus" last="Sack">Markus Sack</name><name sortKey="Scheller, Jurgen" sort="Scheller, Jurgen" uniqKey="Scheller J" first="Jürgen" last="Scheller">Jürgen Scheller</name></country><country name="Autriche"><region name="Vienne (Autriche)"><name sortKey="Arcalis, Elsa" sort="Arcalis, Elsa" uniqKey="Arcalis E" first="Elsa" last="Arcalis">Elsa Arcalis</name></region><name sortKey="Quendler, Heribert" sort="Quendler, Heribert" uniqKey="Quendler H" first="Heribert" last="Quendler">Heribert Quendler</name><name sortKey="Stadlmann, Johannes" sort="Stadlmann, Johannes" uniqKey="Stadlmann J" first="Johannes" last="Stadlmann">Johannes Stadlmann</name><name sortKey="Stoger, Eva" sort="Stoger, Eva" uniqKey="Stoger E" first="Eva" last="Stoger">Eva Stoger</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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