The encapsulation of hemagglutinin in protein bodies achieves a stronger immune response in mice than the soluble antigen
Zein is a water-insoluble polymer from maize seeds that has been widely used to produce carrier particles for the delivery of therapeutic molecules. We encapsulated a recombinant model vaccine antigen in newly formed zein bodies in planta by generating a fusion construct comprising the ectodomain of...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2016-02-01
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| Series: | Frontiers in Plant Science |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00142/full |
| _version_ | 1819052284941697024 |
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| author | Anna eHofbauer Stanislav eMelnik Marc eTschofen Elsa eArcalis Hoang ePhan Ulrike eGresch Johannes eLampel Udo eConrad Eva eStoger |
| author_facet | Anna eHofbauer Stanislav eMelnik Marc eTschofen Elsa eArcalis Hoang ePhan Ulrike eGresch Johannes eLampel Udo eConrad Eva eStoger |
| author_sort | Anna eHofbauer |
| collection | DOAJ |
| description | Zein is a water-insoluble polymer from maize seeds that has been widely used to produce carrier particles for the delivery of therapeutic molecules. We encapsulated a recombinant model vaccine antigen in newly formed zein bodies in planta by generating a fusion construct comprising the ectodomain of hemagglutinin subtype 5 and the N-terminal part of γ-zein. The chimeric protein was transiently produced in tobacco leaves, and H5-containing protein bodies (PBs) were used to immunize mice. An immune response was achieved in all mice treated with H5-zein, even at low doses. The fusion to zein markedly enhanced the IgG response compared the soluble H5 control, and the effect was similar to a commercial adjuvant. The co-administration of adjuvants with the H5-zein bodies did not enhance the immune response any further, suggesting that the zein portion itself mediates an adjuvant effect. While the zein portion used to induce protein body formation was only weakly immunogenic, our results indicate that zein-induced protein bodies are promising production and delivery vehicles for subunit vaccines. |
| first_indexed | 2024-12-21T12:17:24Z |
| format | Article |
| id | doaj.art-9a639da65115470981aed5653b6ef0f0 |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-12-21T12:17:24Z |
| publishDate | 2016-02-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-9a639da65115470981aed5653b6ef0f02022-12-21T19:04:24ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2016-02-01710.3389/fpls.2016.00142178065The encapsulation of hemagglutinin in protein bodies achieves a stronger immune response in mice than the soluble antigenAnna eHofbauer0Stanislav eMelnik1Marc eTschofen2Elsa eArcalis3Hoang ePhan4Ulrike eGresch5Johannes eLampel6Udo eConrad7Eva eStoger8University of Natural Resources and Life SciencesUniversity of Natural Resources and Life SciencesUniversity of Natural Resources and Life SciencesUniversity of Natural Resources and Life SciencesLeibniz Institute of Plant Genetics and Crop Plant Research (IPK)Leibniz Institute of Plant Genetics and Crop Plant Research (IPK)University of Natural Resources and Life SciencesLeibniz Institute of Plant Genetics and Crop Plant Research (IPK)University of Natural Resources and Life SciencesZein is a water-insoluble polymer from maize seeds that has been widely used to produce carrier particles for the delivery of therapeutic molecules. We encapsulated a recombinant model vaccine antigen in newly formed zein bodies in planta by generating a fusion construct comprising the ectodomain of hemagglutinin subtype 5 and the N-terminal part of γ-zein. The chimeric protein was transiently produced in tobacco leaves, and H5-containing protein bodies (PBs) were used to immunize mice. An immune response was achieved in all mice treated with H5-zein, even at low doses. The fusion to zein markedly enhanced the IgG response compared the soluble H5 control, and the effect was similar to a commercial adjuvant. The co-administration of adjuvants with the H5-zein bodies did not enhance the immune response any further, suggesting that the zein portion itself mediates an adjuvant effect. While the zein portion used to induce protein body formation was only weakly immunogenic, our results indicate that zein-induced protein bodies are promising production and delivery vehicles for subunit vaccines.http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00142/fullMolecular Farmingrecombinant proteinsubcellular targetingProtein BodiesRecombinant vaccine |
| spellingShingle | Anna eHofbauer Stanislav eMelnik Marc eTschofen Elsa eArcalis Hoang ePhan Ulrike eGresch Johannes eLampel Udo eConrad Eva eStoger The encapsulation of hemagglutinin in protein bodies achieves a stronger immune response in mice than the soluble antigen Frontiers in Plant Science Molecular Farming recombinant protein subcellular targeting Protein Bodies Recombinant vaccine |
| title | The encapsulation of hemagglutinin in protein bodies achieves a stronger immune response in mice than the soluble antigen |
| title_full | The encapsulation of hemagglutinin in protein bodies achieves a stronger immune response in mice than the soluble antigen |
| title_fullStr | The encapsulation of hemagglutinin in protein bodies achieves a stronger immune response in mice than the soluble antigen |
| title_full_unstemmed | The encapsulation of hemagglutinin in protein bodies achieves a stronger immune response in mice than the soluble antigen |
| title_short | The encapsulation of hemagglutinin in protein bodies achieves a stronger immune response in mice than the soluble antigen |
| title_sort | encapsulation of hemagglutinin in protein bodies achieves a stronger immune response in mice than the soluble antigen |
| topic | Molecular Farming recombinant protein subcellular targeting Protein Bodies Recombinant vaccine |
| url | http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00142/full |
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