Immunoabsorbent Nanoparticles Based on a Tobamovirus Displaying Protein A
Earlier attempts to express peptides longer than 20 aa on the surface of tobamoviruses such as tobacco mosaic virus have failed. Surprisingly, we found that a functional fragment of protein A (133 aa) can be displayed on the surface of a tobamovirus as a C-terminal fusion to the coat protein via a 1...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2006-11, Vol.103 (47), p.17678-17683 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Werner, Stefan Marillonnet, Sylvestre Hause, Gerd Klimyuk, Victor Gleba, Yuri |
| description | Earlier attempts to express peptides longer than 20 aa on the surface of tobamoviruses such as tobacco mosaic virus have failed. Surprisingly, we found that a functional fragment of protein A (133 aa) can be displayed on the surface of a tobamovirus as a C-terminal fusion to the coat protein via a 15-aa linker. The macromolecular nature of these nanoparticles allowed the design of a simple protocol for purification of mAbs with a recovery yield of 50% and >90% product purity. The extremely dense packing of protein A on the nanoparticles (>2,100 copies per viral particle) results in an immunoadsorbent with a binding capacity of 2 g mAb per g. This characteristic, combined with the high level of expression of the nanoparticles (>3 g adsorbent per kg of leaf biomass), provides a very inexpensive self-assembling matrix that could meet the criteria for a single-use industrial immunoadsorbent for antibody purification. |
| doi_str_mv | 10.1073/pnas.0608869103 |
| format | Article |
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Surprisingly, we found that a functional fragment of protein A (133 aa) can be displayed on the surface of a tobamovirus as a C-terminal fusion to the coat protein via a 15-aa linker. The macromolecular nature of these nanoparticles allowed the design of a simple protocol for purification of mAbs with a recovery yield of 50% and >90% product purity. The extremely dense packing of protein A on the nanoparticles (>2,100 copies per viral particle) results in an immunoadsorbent with a binding capacity of 2 g mAb per g. 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| subjects | Adsorbents Antibodies Antibodies, Monoclonal - isolation & purification Antibodies, Monoclonal - metabolism Biological Sciences Biotechnology Capsid Proteins - genetics Capsid Proteins - isolation & purification Capsid Proteins - metabolism Capsid Proteins - ultrastructure Centrifugation Gels Gene expression Immunoglobulins Leaves Nanoparticles Nanostructures - ultrastructure Peptides Proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - metabolism Recombinant Fusion Proteins - ultrastructure Staphylococcal Protein A - genetics Staphylococcal Protein A - metabolism Tobacco mosaic virus Tobamovirus Tobamovirus - genetics Tobamovirus - metabolism Tobamovirus - ultrastructure Virion - isolation & purification Virion - ultrastructure Virions Viruses |
| title | Immunoabsorbent Nanoparticles Based on a Tobamovirus Displaying Protein A |
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