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A new plant expression system for producing pharmaceutical proteins

In the past decade, interest in the production of recombinant pharmaceutical proteins in plants has tremendously progressed because plants do not harbor mammalian viruses, are economically competitive, easily scalable, and capable of carrying out complex post-translational modifications required for...

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Main Authors: Abd Aziz, Nazrin, Tan, Boon Chin, Rejab, Nur Ardiyana, Othman, Rofina Yasmin, Khalid, Norzulaani
Format: Article
Published: Humana Press Inc 2020
Subjects:
R Medicine
SB Plant culture
Online Access:http://eprints.um.edu.my/36869/
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spelling my.um.eprints.368692023-10-05T06:53:37Z http://eprints.um.edu.my/36869/ A new plant expression system for producing pharmaceutical proteins Abd Aziz, Nazrin Tan, Boon Chin Rejab, Nur Ardiyana Othman, Rofina Yasmin Khalid, Norzulaani R Medicine SB Plant culture In the past decade, interest in the production of recombinant pharmaceutical proteins in plants has tremendously progressed because plants do not harbor mammalian viruses, are economically competitive, easily scalable, and capable of carrying out complex post-translational modifications required for recombinant pharmaceutical proteins. Mucuna bracteata is an essential perennial cover crop species widely planted as an underground cover in oil palm and rubber plantations. As a legume, they have high biomass, thrive in its habitat, and can fix nitrogen. Thus, M. bracteata is a cost-efficient crop that shows ideal characteristics as a platform for mass production of recombinant protein. In this study, we established a new platform for the transient production of a recombinant protein in M. bracteata via vacuum-assisted agro-infiltration. Five-week-old M. bracteata plants were vacuum infiltrated with Agrobacterium tumefaciens harboring a plasmid that encodes for an anti-toxoplasma immunoglobulin (IgG) under different parameters, including trifoliate leaf positional effects, days to harvest post-infiltration, and the Agrobacterium strain used. Our results showed that vacuum infiltration of M. bracteata plant with A. tumefaciens strain GV3101 produced the highest concentration of heterologous protein in its bottom trifoliate leaf at 2 days post-infiltration. The purified anti-toxoplasma IgG was then analyzed using Western blot and ELISA. It was demonstrated that, while structural heterogeneity existed in the purified anti-toxoplasma IgG from M. bracteata, its transient expression level was two-fold higher than the model platform, Nicotiana benthamiana. This study has laid the foundation towards establishing M. bracteata as a potential platform for the production of recombinant pharmaceutical protein. Humana Press Inc 2020-04 Article PeerReviewed Abd Aziz, Nazrin and Tan, Boon Chin and Rejab, Nur Ardiyana and Othman, Rofina Yasmin and Khalid, Norzulaani (2020) A new plant expression system for producing pharmaceutical proteins. Molecular Biotechnology, 62 (4). pp. 240-251. ISSN 1073-6085, DOI https://doi.org/10.1007/s12033-020-00242-2. <https://doi.org/10.1007/s12033-020-00242-2.>. 10.1007/s12033-020-00242-2.
institution Universiti Malaya
building UM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaya
content_source UM Research Repository
url_provider http://eprints.um.edu.my/
topic R Medicine
SB Plant culture
spellingShingle R Medicine
SB Plant culture
Abd Aziz, Nazrin
Tan, Boon Chin
Rejab, Nur Ardiyana
Othman, Rofina Yasmin
Khalid, Norzulaani
A new plant expression system for producing pharmaceutical proteins
description In the past decade, interest in the production of recombinant pharmaceutical proteins in plants has tremendously progressed because plants do not harbor mammalian viruses, are economically competitive, easily scalable, and capable of carrying out complex post-translational modifications required for recombinant pharmaceutical proteins. Mucuna bracteata is an essential perennial cover crop species widely planted as an underground cover in oil palm and rubber plantations. As a legume, they have high biomass, thrive in its habitat, and can fix nitrogen. Thus, M. bracteata is a cost-efficient crop that shows ideal characteristics as a platform for mass production of recombinant protein. In this study, we established a new platform for the transient production of a recombinant protein in M. bracteata via vacuum-assisted agro-infiltration. Five-week-old M. bracteata plants were vacuum infiltrated with Agrobacterium tumefaciens harboring a plasmid that encodes for an anti-toxoplasma immunoglobulin (IgG) under different parameters, including trifoliate leaf positional effects, days to harvest post-infiltration, and the Agrobacterium strain used. Our results showed that vacuum infiltration of M. bracteata plant with A. tumefaciens strain GV3101 produced the highest concentration of heterologous protein in its bottom trifoliate leaf at 2 days post-infiltration. The purified anti-toxoplasma IgG was then analyzed using Western blot and ELISA. It was demonstrated that, while structural heterogeneity existed in the purified anti-toxoplasma IgG from M. bracteata, its transient expression level was two-fold higher than the model platform, Nicotiana benthamiana. This study has laid the foundation towards establishing M. bracteata as a potential platform for the production of recombinant pharmaceutical protein.
format Article
author Abd Aziz, Nazrin
Tan, Boon Chin
Rejab, Nur Ardiyana
Othman, Rofina Yasmin
Khalid, Norzulaani
author_facet Abd Aziz, Nazrin
Tan, Boon Chin
Rejab, Nur Ardiyana
Othman, Rofina Yasmin
Khalid, Norzulaani
author_sort Abd Aziz, Nazrin
title A new plant expression system for producing pharmaceutical proteins
title_short A new plant expression system for producing pharmaceutical proteins
title_full A new plant expression system for producing pharmaceutical proteins
title_fullStr A new plant expression system for producing pharmaceutical proteins
title_full_unstemmed A new plant expression system for producing pharmaceutical proteins
title_sort new plant expression system for producing pharmaceutical proteins
publisher Humana Press Inc
publishDate 2020
url http://eprints.um.edu.my/36869/
_version_ 1781704506806894592
score 13.211869

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