Use of virus vectors for the expression in plants of active full‐length and single chain anti‐coronavirus antibodies
Identifieur interne : 001888 ( Istex/Curation ); précédent : 001887; suivant : 001889Use of virus vectors for the expression in plants of active full‐length and single chain anti‐coronavirus antibodies
Auteurs : Josefa M. Alamillo [Espagne] ; Wendy Monger [Royaume-Uni] ; Isabel Sola [Espagne] ; Beatriz García [Espagne] ; Yolande Perrin [Royaume-Uni, France] ; Marco Bestagno [Italie] ; Oscar R. Burrone [Italie] ; Patricia Sabella [Espagne] ; Joan Plana-Durán [Espagne] ; Luis Enjuanes [Espagne] ; George P. Lomonossoff [Royaume-Uni] ; Juan A. García [Espagne]Source :
- Biotechnology Journal [ 1860-6768 ] ; 2006-10.
Abstract
To extend the potential of antibodies and their derivatives to provide passive protection against enteric infections when supplied orally in crude plant extracts, we have expressed both a small immune protein (SIP) and a full‐length antibody in plants using two different plant virus vectors based on potato virus X (PVX) and cowpea mosaic virus (CPMV). The agr;SIP molecule consisted of a single chain antibody (scFv) specific for the porcine coronavirus, transmissible gastroenteritis virus (TGEV) linked to the α‐CH3 domain from human IgA. To express the full‐length IgA, the individual light and heavy chains from the TGEV‐specific mAb 6A.C3 were inserted into separate PVX constructs and plants were co‐infected with both constructs. Western blot analysis revealed the efficient expression of both the SIP and IgA molecules. Analysis of crude plant extracts revealed that both the plant‐expressed αSIP and IgA molecules could bind to and neutralize TGEV in tissue culture, indicating that active molecules were produced. Oral administration of crude extracts from antibody‐expressing plant tissue to 2‐day‐old piglets showed that both the αSIP and full‐length IgA molecules can provide in vivo protection against TGEV.
Url:
DOI: 10.1002/biot.200600143
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Burrone</name><affiliation wicri:level="1"><mods:affiliation>International Center for Genetic Engineering and Biotechnology, Trieste, Italy</mods:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>International Center for Genetic Engineering and Biotechnology, Trieste</wicri:regionArea></affiliation></author><author><name sortKey="Sabella, Patricia" sort="Sabella, Patricia" uniqKey="Sabella P" first="Patricia" last="Sabella">Patricia Sabella</name><affiliation wicri:level="1"><mods:affiliation>Fort Dodge Veterinaria SA, Carretera de Comprodon, Girona, Spain</mods:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Fort Dodge Veterinaria SA, Carretera de Comprodon, Girona</wicri:regionArea></affiliation></author><author><name sortKey="Plana Uran, Joan" sort="Plana Uran, Joan" uniqKey="Plana Uran J" first="Joan" last="Plana-Durán">Joan Plana-Durán</name><affiliation wicri:level="1"><mods:affiliation>Fort Dodge Veterinaria SA, Carretera de Comprodon, Girona, Spain</mods:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Fort Dodge Veterinaria SA, Carretera de Comprodon, Girona</wicri:regionArea></affiliation></author><author><name sortKey="Enjuanes, Luis" sort="Enjuanes, Luis" uniqKey="Enjuanes L" first="Luis" last="Enjuanes">Luis Enjuanes</name><affiliation wicri:level="1"><mods:affiliation>Centro Nacional de Biotecnología, Campus Universidad Autónoma, Madrid, Spain</mods:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro Nacional de Biotecnología, Campus Universidad Autónoma, Madrid</wicri:regionArea></affiliation></author><author><name sortKey="Lomonossoff, George P" sort="Lomonossoff, George P" uniqKey="Lomonossoff G" first="George P." last="Lomonossoff">George P. Lomonossoff</name><affiliation wicri:level="1"><mods:affiliation>John Innes Centre, Norwich, UK</mods:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>John Innes Centre, Norwich</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>E-mail: george.lomonossoff@bbsrc.ac.uk</mods:affiliation><country wicri:rule="url">Royaume-Uni</country></affiliation><affiliation><mods:affiliation>Correspondence address: John Innes Centre, Colney lane, Norwich NR4 7UH, UK, +44‐1603‐450018</mods:affiliation></affiliation></author><author><name sortKey="Garcia, Juan A" sort="Garcia, Juan A" uniqKey="Garcia J" first="Juan A." last="García">Juan A. García</name><affiliation wicri:level="1"><mods:affiliation>Centro Nacional de Biotecnología, Campus Universidad Autónoma, Madrid, Spain</mods:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro Nacional de Biotecnología, Campus Universidad Autónoma, Madrid</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Biotechnology Journal</title><title level="j" type="sub">Plant Biotech</title><title level="j" type="alt">BIOTECHNOLOGY JOURNAL</title><idno type="ISSN">1860-6768</idno><idno type="eISSN">1860-7314</idno><imprint><biblScope unit="vol">1</biblScope><biblScope unit="issue">10</biblScope><biblScope unit="page" from="1103">1103</biblScope><biblScope unit="page" to="1111">1111</biblScope><biblScope unit="page-count">9</biblScope><publisher>WILEY‐VCH Verlag</publisher><pubPlace>Weinheim</pubPlace><date type="published" when="2006-10">2006-10</date></imprint><idno type="ISSN">1860-6768</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1860-6768</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To extend the potential of antibodies and their derivatives to provide passive protection against enteric infections when supplied orally in crude plant extracts, we have expressed both a small immune protein (SIP) and a full‐length antibody in plants using two different plant virus vectors based on potato virus X (PVX) and cowpea mosaic virus (CPMV). The agr;SIP molecule consisted of a single chain antibody (scFv) specific for the porcine coronavirus, transmissible gastroenteritis virus (TGEV) linked to the α‐CH3 domain from human IgA. To express the full‐length IgA, the individual light and heavy chains from the TGEV‐specific mAb 6A.C3 were inserted into separate PVX constructs and plants were co‐infected with both constructs. Western blot analysis revealed the efficient expression of both the SIP and IgA molecules. Analysis of crude plant extracts revealed that both the plant‐expressed αSIP and IgA molecules could bind to and neutralize TGEV in tissue culture, indicating that active molecules were produced. Oral administration of crude extracts from antibody‐expressing plant tissue to 2‐day‐old piglets showed that both the αSIP and full‐length IgA molecules can provide in vivo protection against TGEV.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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