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Comparative analysis of plant-produced, recombinant dimeric IgA against cell wall β-glucan of pathogenic fungi

TitleComparative analysis of plant-produced, recombinant dimeric IgA against cell wall β-glucan of pathogenic fungi
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication2017
AuthorsCapodicasa, Cristina, Catellani Marcello, Moscetti I., Bromuro C., Chiani P., Torosantucci A., and Benvenuto Eugenio
JournalBiotechnology and Bioengineering
KeywordsAnti-infectious, Antibodies, Antifungal activity, antigen binding, Antigens, article, beta glucan, beta-Glucans, Bins, Bioactivity, biosynthesis, Candida albicans, cell adhesion, Cells, chemical structure, comparative study, controlled study, cytology, dimerization, Efficiency, epithelium cell, evaluation study, fungal cell wall, Fungal infection, Fungi, fungus antibody, genetics, human, human cell, immunoglobulin A, immunoglobulin G, immunoglobulin G1, immunotherapy, metabolism, nonhuman, Pathogens, physiology, plant leaf, Plant leaves, Plant pharming, Polysaccharides, protein expression, Recombinant IgA, recombinant protein, Recombinant Proteins

Immunoglobulins A (IgA) are crucially involved in protection of human mucosal surfaces from microbial pathogens. In this work, we devised and expressed in plants recombinant chimeric antifungal antibodies (Abs) of isotype A (IgA1, IgA2, and scFvFcA1), derived from a murine mAb directed to the fungal cell wall polysaccharide β-glucan which had proven able to confer protection against multiple pathogenic fungi. All recombinant IgA (rIgA) were expressed and correctly assembled in dimeric form in plants and evaluated for yield, antigen-binding efficiency and antifungal properties in vitro, in comparison with a chimeric IgG1 version. Production yields and binding efficiency to purified β-glucans showed significant variations not only between Abs of different isotypes but also between the different IgA formats. Moreover, only the dimeric IgA1 was able to strongly bind cells of the fungal pathogen Candida albicans and to restrain its adhesion to human epithelial cells. Our data indicate that IgG to IgA switch and differences in molecular structure among different rIgA formats can impact expression in plant and biological activity of anti-β-glucans Abs and provide new insights for the design of recombinant IgA as anti-infective immunotherapeutics, whose potential is still poorly investigated. © 2017 Wiley Periodicals, Inc.


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Citation KeyCapodicasa20172729