Antibodies from plants for bionanomaterials

Abstract

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. © 2017 The Authors. WIREs Nanomedicine and Nanobiotechnology published by Wiley Periodicals, Inc. How to cite this article:WIREs Nanomed Nanobiotechnol 2017, 9:e1462. doi: 10.1002/wnan.1462 INTRODUCTIONA ntibodies are glycoproteins produced by the adaptive immune system in humans and other vertebrates. They recognize and bind particular target antigens with great affinity and specificity, allowing them to clear pathogens and other unwanted material from the body. Although plants do not naturally produce antibodies, they can be engineered to do so by introducing the corresponding immunoglobulin genes. 1,2 In this manner, plants can be instructed to make antibodies that target any antigen of choice, and they can make them efficiently and in all kinds of different formats. 3,4 Most people picture antibodies as the typical mammalian serum-type immunoglobulin G (IgG), which comprises two identical heavy chains and two identical light chains joined by disulfide bonds (Figure 1). The chains fold and assemble into a multimeric Y-shaped structure. Below the hinge, in what is known as the Fc region (fragment crystallizable), all IgG molecules are largely the same, and this region is responsible for the general effector functions of antibodies, such as immune cell recognition and complement fixation. This part of the antibody is also glycosylated. The hinge and the region above, where the antibody branches into its characteristic Y-shape, is known as the F(ab 0 ) 2 or Fab (fragment for antigen This is an open access article under ...

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