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WIREs Nanomed Nanobiotechnol
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Antibodies from plants for bionanomaterials

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Antibodies are produced as part of the vertebrate adaptive immune response and are not naturally made by plants. However, antibody DNA sequences can be introduced into plants, and together with laboratory technologies that allow the design of antibodies recognizing any conceivable molecular structure, plants can be used as ‘green factories’ to produce any antibody at all. The advent of plant‐based transient expression systems in particular allows the rapid, convenient, and safe production of antibodies, ranging from laboratory‐scale expression to industrial‐scale manufacturing. The key features of plant‐based production include safety, speed, low cost, and convenience, allowing newcomers to rapidly master the technology and use it to its full advantage. Manufacturing in plants has recently achieved significant milestones and offers more than just an alternative to established microbial and mammalian cell platforms. The use of plants for product development in particular offers the power and flexibility to easily coexpress many different genes, allowing the plug‐and‐play construction of novel bionanomaterials, perfectly complementing existing approaches based on plant virus‐like particles. As well as producing single antibodies for applications in medicine, agriculture, and industry, plants can be used to produce antibody‐based supramolecular structures and scaffolds as a new generation of green bionanomaterials that promise a bright future based on clean and renewable nanotechnology applications. WIREs Nanomed Nanobiotechnol 2017, 9:e1462. doi: 10.1002/wnan.1462

This article is categorized under:

  • Therapeutic Approaches and Drug Discovery > Emerging Technologies
  • Diagnostic Tools > In Vivo Nanodiagnostics and Imaging
  • Biology-Inspired Nanomaterials > Protein and Virus-Based Structures
Domain architecture of natural antibodies and some engineered recombinant variants. Domains representing the antigen‐binding site are indicated in green and the constant domains in gray. The functional and structural separation of the variable domains (antigen‐binding site) and constant domains (structural arrangement, effector functions) and the free N‐ and C‐terminal ends of the individual domains has given rise to a vast number of variants, derivatives, and combinations.
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The use of plant‐derived antibodies for the analysis and construction of nanomaterials. (a) Plant‐derived antibodies are not only useful for classical immunological assays such as western blots and enzyme‐linked immunosorbent assays (ELISAs), but derivatives such as monovalent Fab and fluorescent SNAP‐fusion proteins can facilitate surface plasmon resonance spectroscopy and nanoparticle tracking analysis. (b) Different derivatives that can integrate the functional properties of plant antibodies, particularly by targeting specific cell‐surface molecules (indicated by the green domains): (1) bispecific IgG molecule bound to a virus‐like particle (VLP); (2) full‐size IgG with C‐terminal peptide bound to a VHH fused to a virus coat protein (CP); (3) a scFv fused to a bridging domain fused to the virus CP; (4) a Fab fused to green fluorescent protein (GFP), binding to ∝‐GFP‐VHH‐CP; (5) a scFv fused to a long linker peptide fused to a virus CP; (6) two VHH domains connected via a long linker peptide bound to a VLP. (c) Different plant antibody formats (scFv and nanobody) have already been used as fusions to virus CPs, whereas specific IgG and scFv formats have yet to be tested. Depending on the antibody specificity, a variety of molecules can be assembled into the nanomaterials (VLPs in this example): (1) small molecules such as herbicides or payloads; (2) large multimeric antigens; (3) enzymes; (4) fluorescent proteins; (5) or other nanomaterials. The latter may then be arranged into higher‐order structures: (6) oligomers of spherical particles; or (7) combinations of spherical and rod‐shaped particles.
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Make your own antibodies in plants using standard laboratory methods. Although the isolation of antibody variable genes can be challenging (e.g., if single‐cell polymerase chain reaction is required), all the subsequent steps, including cloning, growing the bacteria and plants, the infiltration of leaves, and antibody extraction and purification, are straightforward laboratory methods that can be learned quickly. Notably, leaf infiltration and the subsequent incubation can be done in a nonsterile environment. A single plant can yield up to 100 mg of purified antibody.
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Getting started: basic equipment and material required for transient gene expression in plants using the agroinfiltration method.
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Simplified schematic representation of the transfection and subsequent transformation of a plant cell by Agrobacterium tumefaciens. The individual steps are indicated by circled numbers and are explained in the text.
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The many flavors of plant‐based production systems are illustrated here using the HIV‐neutralizing antibody 2G12 as a case study. This antibody has been expressed in many different plant species, tissues, and cells, including those shown here. The red fluorescent protein from Discosoma sp. has been introduced by placing the gene alongside those encoding the antibody chains to allow the rapid and convenient detection of antibody‐expressing tissues (and to provide some idea of the yield) based on macroscopic fluorescence. Upper lane: potato, tobacco, N. benthamiana, Arabidopsis thaliana; Middle lane: corn cobs, rice plant, rice seed, wheat seed; Lower lane: dedifferentiated tobacco cv. BY2 cells: cell cluster, calli on agar plates, shake flask cultures, and fermentation.
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Key features and selling points of plant‐based systems for making antibodies and other recombinant proteins.
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Therapeutic Approaches and Drug Discovery > Emerging Technologies
Diagnostic Tools > In Vivo Nanodiagnostics and Imaging
Biology-Inspired Nanomaterials > Protein and Virus-Based Structures

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