Biochemical composition of haemagglutinin-based influenza virus-like particle vaccine produced by transient expression in tobacco plants
Identifieur interne : 000081 ( France/Analysis ); précédent : 000080; suivant : 000082Biochemical composition of haemagglutinin-based influenza virus-like particle vaccine produced by transient expression in tobacco plants
Auteurs : François Le Mauff [France] ; Geneviève Mercier [Canada] ; Philippe Chan [France] ; Carole Burel [France] ; David Vaudry [France] ; Muriel Bardor [France] ; Louis-Philippe Vezina [Canada] ; Manon Couture [Canada] ; Patrice Lerouge [France] ; Nathalie Landry [Canada]Source :
- Plant Biotechnology Journal [ 1467-7644 ] ; 2015-06.
English descriptors
Abstract
Influenza virus‐like particles (VLPs) are noninfectious particles resembling the influenza virus representing a promising vaccine alternative to inactivated influenza virions as antigens. Medicago inc. has developed a plant‐based VLP manufacturing platform allowing the large‐scale production of GMP‐grade influenza VLPs. In this article, we report on the biochemical compositions of these plant‐based influenza candidate vaccines, more particularly the characterization of the N‐glycan profiles of the viral haemagglutinins H1 and H5 proteins as well as the tobacco‐derived lipid content and residual impurities. Mass spectrometry analyses showed that all N‐glycosylation sites of the extracellular domain of the recombinant haemagglutinins carry plant‐specific complex‐type N‐glycans having core α(1,3)‐fucose, core β(1,2)‐xylose epitopes and Lewisa extensions. Previous phases I and II clinical studies have demonstrated that no hypersensibility nor induction of IgG or IgE directed against these glycans was observed. In addition, this article showed that the plant‐made influenza vaccines are highly pure VLPs preparations while detecting no protein contaminants coming either from Agrobacterium or from the enzymes used for the enzyme‐assisted extraction process. In contrast, VLPs contain few host cell proteins and glucosylceramides associated with plant lipid rafts. Identification of such raft markers, together with the type of host cell impurity identified, confirmed that the mechanism of VLP formation in planta is similar to the natural process of influenza virus assembly in mammals.
Url:
DOI: 10.1111/pbi.12301
Affiliations:
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Hal:hal-01841099Le document en format XML
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<author><name sortKey="Bardor, Muriel" sort="Bardor, Muriel" uniqKey="Bardor M" first="Muriel" last="Bardor">Muriel Bardor</name>
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<author><name sortKey="Vezina, Louis Philippe" sort="Vezina, Louis Philippe" uniqKey="Vezina L" first="Louis-Philippe" last="Vezina">Louis-Philippe Vezina</name>
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<author><name sortKey="Couture, Manon" sort="Couture, Manon" uniqKey="Couture M" first="Manon" last="Couture">Manon Couture</name>
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<author><name sortKey="Lerouge, Patrice" sort="Lerouge, Patrice" uniqKey="Lerouge P" first="Patrice" last="Lerouge">Patrice Lerouge</name>
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<orgName type="acronym">Glyco-MEV</orgName>
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<desc> <address> <addrLine>2, rue Lucien Tesnières 76821 Mont-Saint-Aignan cedex</addrLine>
<country key="FR"></country>
</address>
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<orgName>Université de Rouen Normandie</orgName>
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<orgName>Normandie Université</orgName>
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<country>France</country>
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</author>
<author><name sortKey="Landry, Nathalie" sort="Landry, Nathalie" uniqKey="Landry N" first="Nathalie" last="Landry">Nathalie Landry</name>
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<idno type="DOI">10.1111/pbi.12301</idno>
<series><title level="j">Plant Biotechnology Journal</title>
<idno type="ISSN">1467-7644</idno>
<imprint><date type="datePub">2015-06</date>
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<profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term> N‐glycosylation</term>
<term> haemagglutinin</term>
<term> lipid raft</term>
<term> plant</term>
<term>virus‐like particles</term>
</keywords>
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</teiHeader>
<front><div type="abstract" xml:lang="en"> <p>Influenza virus‐like particles (VLPs) are noninfectious particles resembling the influenza virus representing a promising vaccine alternative to inactivated influenza virions as antigens. Medicago inc. has developed a plant‐based VLP manufacturing platform allowing the large‐scale production of GMP‐grade influenza VLPs. In this article, we report on the biochemical compositions of these plant‐based influenza candidate vaccines, more particularly the characterization of the N‐glycan profiles of the viral haemagglutinins H1 and H5 proteins as well as the tobacco‐derived lipid content and residual impurities. Mass spectrometry analyses showed that all N‐glycosylation sites of the extracellular domain of the recombinant haemagglutinins carry plant‐specific complex‐type N‐glycans having core α(1,3)‐fucose, core β(1,2)‐xylose epitopes and Lewisa extensions. Previous phases I and II clinical studies have demonstrated that no hypersensibility nor induction of IgG or IgE directed against these glycans was observed. In addition, this article showed that the plant‐made influenza vaccines are highly pure VLPs preparations while detecting no protein contaminants coming either from Agrobacterium or from the enzymes used for the enzyme‐assisted extraction process. In contrast, VLPs contain few host cell proteins and glucosylceramides associated with plant lipid rafts. Identification of such raft markers, together with the type of host cell impurity identified, confirmed that the mechanism of VLP formation in planta is similar to the natural process of influenza virus assembly in mammals. </p>
</div>
</front>
</TEI>
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<li>France</li>
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<tree><country name="France"><noRegion><name sortKey="Le Mauff, Francois" sort="Le Mauff, Francois" uniqKey="Le Mauff F" first="François" last="Le Mauff">François Le Mauff</name>
</noRegion>
<name sortKey="Bardor, Muriel" sort="Bardor, Muriel" uniqKey="Bardor M" first="Muriel" last="Bardor">Muriel Bardor</name>
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<name sortKey="Chan, Philippe" sort="Chan, Philippe" uniqKey="Chan P" first="Philippe" last="Chan">Philippe Chan</name>
<name sortKey="Lerouge, Patrice" sort="Lerouge, Patrice" uniqKey="Lerouge P" first="Patrice" last="Lerouge">Patrice Lerouge</name>
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<country name="Canada"><noRegion><name sortKey="Mercier, Genevieve" sort="Mercier, Genevieve" uniqKey="Mercier G" first="Geneviève" last="Mercier">Geneviève Mercier</name>
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<name sortKey="Couture, Manon" sort="Couture, Manon" uniqKey="Couture M" first="Manon" last="Couture">Manon Couture</name>
<name sortKey="Landry, Nathalie" sort="Landry, Nathalie" uniqKey="Landry N" first="Nathalie" last="Landry">Nathalie Landry</name>
<name sortKey="Vezina, Louis Philippe" sort="Vezina, Louis Philippe" uniqKey="Vezina L" first="Louis-Philippe" last="Vezina">Louis-Philippe Vezina</name>
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