Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 103, Issue 47, Pages 17678-17683Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0608869103
Keywords
antibody purification; coat protein fusion; viral particle
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Earlier attempts to express pepticles 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 immuroadsorbent 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 immuroadsorbent for antibody purification.
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