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Combinatorial Analysis of Secretory Immunoglobulin A (sIgA) Expression in Plants

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Combinatorial Analysis of Secretory Immunoglobulin A (sIgA) Expression in Plants

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dc.contributor.author Juárez Ortega, Paloma es_ES
dc.contributor.author Huet Trujillo, Estefanía es_ES
dc.contributor.author Sarrion-Perdigones, Alejandro es_ES
dc.contributor.author Falconi, E.E. es_ES
dc.contributor.author Granell Richart, Antonio es_ES
dc.contributor.author Orzáez Calatayud, Diego Vicente es_ES
dc.date.accessioned 2016-07-18T07:23:50Z
dc.date.available 2016-07-18T07:23:50Z
dc.date.issued 2013-03
dc.identifier.issn 1422-0067
dc.identifier.uri http://hdl.handle.net/10251/67693
dc.description.abstract Delivery of secretory immunoglobulin A (sIgA) to mucosal surfaces as a passive immunotherapy agent is a promising strategy to prevent infectious diseases. Recombinant sIgA production in plants requires the co-expression of four transcriptional units encoding the light chain (LC), heavy chain (HC), joining chain (JC) and secretory component (SC). As a way to optimize sIgA production in plants, we tested the combinatorial expression of 16 versions of a human sIgA against the VP8* rotavirus antigen in Nicotiana benthamiana, using the recently developed GoldenBraid multigene assembly system. Each sIgA version was obtained by combining one of the two types of HC (alpha 1 and alpha 2) with one of the two LC types (k and lambda) and linking or not a KDEL peptide to the HC and/or SC. From the analysis of the anti-VP8* activity, it was concluded that those sIgA versions carrying HC alpha 1 and LC lambda provided the highest yields. Moreover, ER retention significantly increased antibody production, particularly when the KDEL signal was linked to the SC. Maximum expression levels of 32.5 mu g IgA/g fresh weight (FW) were obtained in the best performing combination, with an estimated 33% of it in the form of a secretory complex. es_ES
dc.description.sponsorship This work has been funded by Grant BIO2010-15384 from Plan Nacional I + D of the Spanish Ministry of Science. Juarez P. is a recipient of a FPU fellowship, and Sarrion-Perdigones A. and Huet-Trujillo E. are recipients of a FPI fellowship. We want to thank Monedero for kindly providing scFv and VP8* clones. en_EN
dc.language Inglés es_ES
dc.publisher MDPI es_ES
dc.relation.ispartof International Journal of Molecular Sciences es_ES
dc.rights Reconocimiento (by) es_ES
dc.subject Secretory IgA es_ES
dc.subject Antibody es_ES
dc.subject Rotavirus es_ES
dc.subject GoldenBraid es_ES
dc.subject Plant synthetic biology es_ES
dc.subject.classification MICROBIOLOGIA es_ES
dc.subject.classification BIOQUIMICA Y BIOLOGIA MOLECULAR es_ES
dc.title Combinatorial Analysis of Secretory Immunoglobulin A (sIgA) Expression in Plants es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.3390/ijms14036205
dc.relation.projectID info:eu-repo/grantAgreement/MICINN//BIO2010-15384/ES/FABRICANDO TOMATES SALUDABLES: BIOPIEZAS PARA INTRAGENESIS Y MOLECULAR FARMING EN SOLANACEAS/ es_ES
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia es_ES
dc.description.bibliographicCitation Juárez Ortega, P.; Huet Trujillo, E.; Sarrion-Perdigones, A.; Falconi, E.; Granell Richart, A.; Orzáez Calatayud, DV. (2013). Combinatorial Analysis of Secretory Immunoglobulin A (sIgA) Expression in Plants. International Journal of Molecular Sciences. 14(3):6205-6222. https://doi.org/10.3390/ijms14036205 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://dx.doi.org/10.3390/ijms14036205 es_ES
dc.description.upvformatpinicio 6205 es_ES
dc.description.upvformatpfin 6222 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 14 es_ES
dc.description.issue 3 es_ES
dc.relation.senia 248407 es_ES
dc.identifier.pmid 23507755 en_EN
dc.identifier.pmcid PMC3634489 en_EN
dc.contributor.funder Ministerio de Ciencia e Innovación es_ES
dc.description.references Reichert, J. M., & Valge-Archer, V. E. (2007). Development trends for monoclonal antibody cancer therapeutics. Nature Reviews Drug Discovery, 6(5), 349-356. doi:10.1038/nrd2241 es_ES
dc.description.references Corthésy, B. (2010). Role of secretory immunoglobulin A and secretory component in the protection of mucosal surfaces. Future Microbiology, 5(5), 817-829. doi:10.2217/fmb.10.39 es_ES
dc.description.references Corthésy, B. (2003). Recombinant Secretory Immunoglobulin A in Passive Immunotherapy: Linking Immunology and Biotechnology. Current Pharmaceutical Biotechnology, 4(1), 51-67. doi:10.2174/1389201033378020 es_ES
dc.description.references Corthësy, B. (2008). Secretory immunoglobulin A: well beyond immune exclusion at mucosal surfaces. Immunopharmacology and Immunotoxicology, 31(2), 174-179. doi:10.1080/08923970802438441 es_ES
dc.description.references Sarrion-Perdigones, A., Juarez, P., Granell, A., & Orzaez, D. (2011). Production of Antibodies in Plants. Cell Engineering, 143-164. doi:10.1007/978-94-007-1257-7_7 es_ES
dc.description.references Paul, M., Dolleweerd, C. van, Drake, P. M. W., Reljic, R., Thangaraj, H., Barbi, T., … Ma, J. K.-C. (2011). Molecular pharming. Human Vaccines, 7(3), 375-382. doi:10.4161/hv.7.3.14456 es_ES
dc.description.references Fischer, R., Stoger, E., Schillberg, S., Christou, P., & Twyman, R. M. (2004). Plant-based production of biopharmaceuticals. Current Opinion in Plant Biology, 7(2), 152-158. doi:10.1016/j.pbi.2004.01.007 es_ES
dc.description.references Twyman, R. M., Stoger, E., Schillberg, S., Christou, P., & Fischer, R. (2003). Molecular farming in plants: host systems and expression technology. Trends in Biotechnology, 21(12), 570-578. doi:10.1016/j.tibtech.2003.10.002 es_ES
dc.description.references Saint-Jore-Dupas, C., Faye, L., & Gomord, V. (2007). From planta to pharma with glycosylation in the toolbox. Trends in Biotechnology, 25(7), 317-323. doi:10.1016/j.tibtech.2007.04.008 es_ES
dc.description.references Ma, J., Hiatt, A., Hein, M., Vine, N., Wang, F., Stabila, P., … Lehner, T. (1995). Generation and assembly of secretory antibodies in plants. Science, 268(5211), 716-719. doi:10.1126/science.7732380 es_ES
dc.description.references Ma, J. K.-C., Hikmat, B. Y., Wycoff, K., Vine, N. D., Chargelegue, D., Yu, L., … Lehner, T. (1998). Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans. Nature Medicine, 4(5), 601-606. doi:10.1038/nm0598-601 es_ES
dc.description.references Weintraub, J. A., Hilton, J. F., White, J. M., Hoover, C. I., Wycoff, K. L., Yu, L., … Featherstone, J. D. B. (2005). Clinical Trial of a Plant-Derived Antibody on Recolonization of Mutans Streptococci. Caries Research, 39(3), 241-250. doi:10.1159/000084805 es_ES
dc.description.references Wycoff, K. (2005). Secretory IgA Antibodies from Plants. Current Pharmaceutical Design, 11(19), 2429-2437. doi:10.2174/1381612054367508 es_ES
dc.description.references Nicholson, L., Gonzalez-Melendi, P., Van Dolleweerd, C., Tuck, H., Perrin, Y., Ma, J. K.-C., … Stoger, E. (2004). A recombinant multimeric immunoglobulin expressed in rice shows assembly-dependent subcellular localization in endosperm cells. Plant Biotechnology Journal, 3(1), 115-127. doi:10.1111/j.1467-7652.2004.00106.x es_ES
dc.description.references Wieland, W. H., Lammers, A., Schots, A., & Orzáez, D. V. (2006). Plant expression of chicken secretory antibodies derived from combinatorial libraries. Journal of Biotechnology, 122(3), 382-391. doi:10.1016/j.jbiotec.2005.12.020 es_ES
dc.description.references Larrick, J. W., Yu, L., Naftzger, C., Jaiswal, S., & Wycoff, K. (2001). Production of secretory IgA antibodies in plants. Biomolecular Engineering, 18(3), 87-94. doi:10.1016/s1389-0344(01)00102-2 es_ES
dc.description.references FOLEY, R. C., RAISONS, R. L., & BEH, K. J. (1991). Monoclonal Antibody Against Sheep Kappa Light Chain. Hybridoma, 10(4), 507-515. doi:10.1089/hyb.1991.10.507 es_ES
dc.description.references Furtado, P. B., Whitty, P. W., Robertson, A., Eaton, J. T., Almogren, A., Kerr, M. A., … Perkins, S. J. (2004). Solution Structure Determination of Monomeric Human IgA2 by X-ray and Neutron Scattering, Analytical Ultracentrifugation and Constrained Modelling: A Comparison with Monomeric Human IgA1. Journal of Molecular Biology, 338(5), 921-941. doi:10.1016/j.jmb.2004.03.007 es_ES
dc.description.references De Muynck, B., Navarre, C., & Boutry, M. (2010). Production of antibodies in plants: status after twenty years. Plant Biotechnology Journal, 8(5), 529-563. doi:10.1111/j.1467-7652.2009.00494.x es_ES
dc.description.references Ma, J. K.-C., Drake, P. M. W., & Christou, P. (2003). The production of recombinant pharmaceutical proteins in plants. Nature Reviews Genetics, 4(10), 794-805. doi:10.1038/nrg1177 es_ES
dc.description.references De Muynck, B., Navarre, C., Nizet, Y., Stadlmann, J., & Boutry, M. (2009). Different subcellular localization and glycosylation for a functional antibody expressed in Nicotiana tabacum plants and suspension cells. Transgenic Research, 18(3), 467-482. doi:10.1007/s11248-008-9240-1 es_ES
dc.description.references D�ring, K., Hippe, S., Kreuzaler, F., & Schell, J. (1990). Synthesis and self-assembly of a functional monoclonal antibody in transgenic Nicotiana tabacum. Plant Molecular Biology, 15(2), 281-293. doi:10.1007/bf00036914 es_ES
dc.description.references Wilde, C. D., Rycke, R. D., Beeckman, T., Neve, M. D., Montagu, M. V., Engler, G., & Depicker, A. (1998). Accumulation Pattern of IgG Antibodies and Fab Fragments in Transgenic Arabidopsis thaliana Plants. Plant and Cell Physiology, 39(6), 639-646. doi:10.1093/oxfordjournals.pcp.a029416 es_ES
dc.description.references Schouten, A., Roosien, J., van Engelen, F. A., (Ineke) de Jong, G. A. M., (Tanja) Borst-Vrenssen, A. W. M., Zilverentant, J. F., … Bakker, J. (1996). The C-terminal KDEL sequence increases the expression level of a single-chain antibody designed to be targeted to both the cytosol and the secretory pathway in transgenic tobacco. Plant Molecular Biology, 30(4), 781-793. doi:10.1007/bf00019011 es_ES
dc.description.references Bencurova, M. (2004). Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin. Glycobiology, 14(5), 457-466. doi:10.1093/glycob/cwh058 es_ES
dc.description.references Gomord, V., Fitchette, A.-C., Menu-Bouaouiche, L., Saint-Jore-Dupas, C., Plasson, C., Michaud, D., & Faye, L. (2010). Plant-specific glycosylation patterns in the context of therapeutic protein production. Plant Biotechnology Journal, 8(5), 564-587. doi:10.1111/j.1467-7652.2009.00497.x es_ES
dc.description.references Sarrion-Perdigones, A., Falconi, E. E., Zandalinas, S. I., Juárez, P., Fernández-del-Carmen, A., Granell, A., & Orzaez, D. (2011). GoldenBraid: An Iterative Cloning System for Standardized Assembly of Reusable Genetic Modules. PLoS ONE, 6(7), e21622. doi:10.1371/journal.pone.0021622 es_ES
dc.description.references Weber, E., Engler, C., Gruetzner, R., Werner, S., & Marillonnet, S. (2011). A Modular Cloning System for Standardized Assembly of Multigene Constructs. PLoS ONE, 6(2), e16765. doi:10.1371/journal.pone.0016765 es_ES
dc.description.references Monedero, V., Rodriguez-Diaz, J., Viana, R., Buesa, J., & Perez-Martinez, G. (2004). Selection of Single-Chain Antibodies against the VP8* Subunit of Rotavirus VP4 Outer Capsid Protein and Their Expression in Lactobacillus casei. Applied and Environmental Microbiology, 70(11), 6936-6939. doi:10.1128/aem.70.11.6936-6939.2004 es_ES
dc.description.references Juárez, P., Presa, S., Espí, J., Pineda, B., Antón, M. T., Moreno, V., … Orzaez, D. (2011). Neutralizing antibodies against rotavirus produced in transgenically labelled purple tomatoes. Plant Biotechnology Journal, 10(3), 341-352. doi:10.1111/j.1467-7652.2011.00666.x es_ES
dc.description.references Langley, R., Wines, B., Willoughby, N., Basu, I., Proft, T., & Fraser, J. D. (2005). The Staphylococcal Superantigen-Like Protein 7 Binds IgA and Complement C5 and Inhibits IgA-FcαRI Binding and Serum Killing of Bacteria. The Journal of Immunology, 174(5), 2926-2933. doi:10.4049/jimmunol.174.5.2926 es_ES
dc.description.references Sack, M., Paetz, A., Kunert, R., Bomble, M., Hesse, F., Stiegler, G., … Rademacher, T. (2007). Functional analysis of the broadly neutralizing human anti-HIV-1 antibody 2F5 produced in transgenic BY-2 suspension cultures. The FASEB Journal, 21(8), 1655-1664. doi:10.1096/fj.06-5863com es_ES
dc.description.references Ramessar, K., Rademacher, T., Sack, M., Stadlmann, J., Platis, D., Stiegler, G., … Christou, P. (2008). Cost-effective production of a vaginal protein microbicide to prevent HIV transmission. Proceedings of the National Academy of Sciences, 105(10), 3727-3732. doi:10.1073/pnas.0708841104 es_ES
dc.description.references Brandtzaeg, P., & Prydz, H. (1984). Direct evidence for an integrated function of J chain and secretory component in epithelial transport of immunoglobulins. Nature, 311(5981), 71-73. doi:10.1038/311071a0 es_ES
dc.description.references Johansen, Braathen, & Brandtzaeg. (2000). Role of J Chain in Secretory Immunoglobulin Formation. Scandinavian Journal of Immunology, 52(3), 240-248. doi:10.1046/j.1365-3083.2000.00790.x es_ES
dc.description.references Braathen, R., Hohman, V. S., Brandtzaeg, P., & Johansen, F.-E. (2007). Secretory Antibody Formation: Conserved Binding Interactions between J Chain and Polymeric Ig Receptor from Humans and Amphibians. The Journal of Immunology, 178(3), 1589-1597. doi:10.4049/jimmunol.178.3.1589 es_ES
dc.description.references Murthy, A. K., Chaganty, B. K. R., Troutman, T., Guentzel, M. N., Yu, J.-J., Ali, S. K., … Arulanandam, B. P. (2011). Mannose-Containing Oligosaccharides of Non-Specific Human Secretory Immunoglobulin A Mediate Inhibition of Vibrio cholerae Biofilm Formation. PLoS ONE, 6(2), e16847. doi:10.1371/journal.pone.0016847 es_ES
dc.description.references Mathias, A., & Corthésy, B. (2011). N-Glycans on secretory component. Gut Microbes, 2(5), 287-293. doi:10.4161/gmic.2.5.18269 es_ES
dc.description.references Hu, L., Crawford, S. E., Czako, R., Cortes-Penfield, N. W., Smith, D. F., Le Pendu, J., … Prasad, B. V. V. (2012). Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen. Nature, 485(7397), 256-259. doi:10.1038/nature10996 es_ES
dc.description.references Yu, X., Dang, V. T., Fleming, F. E., von Itzstein, M., Coulson, B. S., & Blanchard, H. (2012). Structural Basis of Rotavirus Strain Preference toward N-Acetyl- or N-Glycolylneuraminic Acid-Containing Receptors. Journal of Virology, 86(24), 13456-13466. doi:10.1128/jvi.06975-11 es_ES
dc.description.references Haselhorst, T., Fleming, F. E., Dyason, J. C., Hartnell, R. D., Yu, X., Holloway, G., … von Itzstein, M. (2008). Sialic acid dependence in rotavirus host cell invasion. Nature Chemical Biology, 5(2), 91-93. doi:10.1038/nchembio.134 es_ES
dc.description.references Bonner, A., Almogren, A., Furtado, P. B., Kerr, M. A., & Perkins, S. J. (2008). The Nonplanar Secretory IgA2 and Near Planar Secretory IgA1 Solution Structures Rationalize Their Different Mucosal Immune Responses. Journal of Biological Chemistry, 284(8), 5077-5087. doi:10.1074/jbc.m807529200 es_ES
dc.description.references Yoo, E. M., & Morrison, S. L. (2005). IgA: An immune glycoprotein. Clinical Immunology, 116(1), 3-10. doi:10.1016/j.clim.2005.03.010 es_ES
dc.description.references Karnoup, A. S., Turkelson, V., & Anderson, W. H. K. (2005). O-Linked glycosylation in maize-expressed human IgA1. Glycobiology, 15(10), 965-981. doi:10.1093/glycob/cwi077 es_ES
dc.description.references Ramsland, P. A., Willoughby, N., Trist, H. M., Farrugia, W., Hogarth, P. M., Fraser, J. D., & Wines, B. D. (2007). Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1. Proceedings of the National Academy of Sciences, 104(38), 15051-15056. doi:10.1073/pnas.0706028104 es_ES
dc.description.references Almogren, A., Senior, B. W., & Kerr, M. A. (2007). A comparison of the binding of secretory component to immunoglobulin A (IgA) in human colostral S-IgA1 and S-IgA2. Immunology, 120(2), 273-280. doi:10.1111/j.1365-2567.2006.02498.x es_ES
dc.description.references Orzaez, D., Mirabel, S., Wieland, W. H., & Granell, A. (2006). Agroinjection of Tomato Fruits. A Tool for Rapid Functional Analysis of Transgenes Directly in Fruit. Plant Physiology, 140(1), 3-11. doi:10.1104/pp.105.068221 es_ES


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