Fernández Del Carmen, MA.; Juárez Ortega, P.; Presa Castro, S.; Granell Richart, A.; Orzáez Calatayud, DV. (2013). Recombinant jacalin-like plant lectins are produced at high levels in Nicotiana benthamiana and retain agglutination activity and sugar specificity. Journal of Biotechnology. 163(4):391-400. https://doi.org/10.1016/j.jbiotec.2012.11.017
Por favor, use este identificador para citar o enlazar este ítem: http://hdl.handle.net/10251/75059
Title:
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Recombinant jacalin-like plant lectins are produced at high levels in Nicotiana benthamiana and retain agglutination activity and sugar specificity
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Author:
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Fernández Del Carmen, María Asunción
Juárez Ortega, Paloma
Presa Castro, Silvia
Granell Richart, Antonio
Orzáez Calatayud, Diego Vicente
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UPV Unit:
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Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes
Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia
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Issued date:
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Abstract:
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The plant kingdom is an underexplored source of valuable proteins which, like plant lectins, display unique interacting specificities. Furthermore, plant protein diversity remains under-exploited due to the low availability ...[+]
The plant kingdom is an underexplored source of valuable proteins which, like plant lectins, display unique interacting specificities. Furthermore, plant protein diversity remains under-exploited due to the low availability and heterogeneity of native sources. All these hurdles could be overcome with recombinant production. A narrow phylogenetic gap between the native source and the recombinant platform is likely to facilitate proper protein processing and stability; therefore, the plant cell chassis should be specially suited for the recombinant production of many plant native proteins. This is illustrated herein with the recombinant production of two representatives of the plant jacalin-related lectin (JRLs) protein family in Nicotiana benthamiana using state-of-the-art magnICON technology. Mannose-specific Banlec JRL was produced at very high levels in leaves, reaching 1.0 mg of purified protein per gram of fresh weight and showing strong agglutination activity. Galactose-specific jacalin JRL, with its complicated processing requirements, was also successfully produced in N. benthamiana at levels of 0.25 mg of purified protein per gram of fresh weight. Recombinant Jacalin (rJacalin) proved efficient in the purification of human IgA1, and was able to discriminate between plant-made and native IgA1 due to their differential glycosylation status. Together, these results show that the plant cell factory should be considered a primary option in the recombinant production of valuable plant proteins. (C) 2012 Elsevier B.V. All rights reserved.
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Subjects:
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Lectin
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Jacalin
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Molecular farming
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IgA
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Viral vectors
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Copyrigths:
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Cerrado |
Source:
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Journal of Biotechnology. (issn:
0168-1656
)
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DOI:
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10.1016/j.jbiotec.2012.11.017
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Publisher:
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Elsevier
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Publisher version:
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http://dx.doi.org/10.1016/j.jbiotec.2012.11.017
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Project ID:
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info:eu-repo/grantAgreement/MICINN//BIO2010-15384/ES/FABRICANDO TOMATES SALUDABLES: BIOPIEZAS PARA INTRAGENESIS Y MOLECULAR FARMING EN SOLANACEAS/
info:eu-repo/grantAgreement/MICINN//AP2008-01140/ES/AP2008-01140/
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Thanks:
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We wish to acknowledge Prof. Gleba and Dr. Klimyuk from ICON Genetics for providing the magnICON expression system. We also thank Prof. R.P. Sharma, University of Hyderabad, India, for kindly providing us with jackfruit ...[+]
We wish to acknowledge Prof. Gleba and Dr. Klimyuk from ICON Genetics for providing the magnICON expression system. We also thank Prof. R.P. Sharma, University of Hyderabad, India, for kindly providing us with jackfruit seeds and Dr. Luis Rodenas at the UPV Animal Sciences Department for his help with samples for the agglutination analysis. This work has been supported by Grant BIO2010-15384 from MINECO, Spain, and P. Juarez FPU fellowship AP2008-01140.
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Type:
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Artículo
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