Protein body formation in stable transgenic tobacco expressing elastin-like polypeptide and hydrophobin fusion proteins

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creativework.keywords - en
Elastin
Élastine
Réticulum endoplasmique
Endoplasmic Reticulum
Protéines végétales
Plant proteins
Feuilles
Leaves
creativework.keywords - fr
Plantes transgéniques
Transgenic plants
Technologie des protéines
Protein engineering
Interférence ARN
RNA Interference
Tabac
Tobacco
dc.contributor.author
Gutiérrez, Sonia P.
Saberianfar, Reza
Kohalmi, Susanne E.
Menassa, Rima
dc.date.accepted
2013-05-06
dc.date.accessioned
2024-10-21T16:12:57Z
dc.date.available
2024-10-21T16:12:57Z
dc.date.issued
2013-05-10
dc.date.submitted
2013-02-06
dc.description.abstract - en
Background: Plants are recognized as an efficient and inexpensive system to produce valuable recombinant proteins. Two different strategies have been commonly used for the expression of recombinant proteins in plants: transient expression mediated by Agrobacterium; or stable transformation of the plant genome. However, the use of plants as bioreactors still faces two main limitations: low accumulation levels of some recombinant proteins and lack of efficient purification methods. Elastin-like polypeptide (ELP), hydrophobin I (HFBI) and Zera® are three fusion partners found to increase the accumulation levels of recombinant proteins and induce the formation of protein bodies (PBs) in leaves when targeted to the endoplasmic reticulum (ER) in transient expression assays. In this study the effects of ELP and HFBI fusion tags on recombinant protein accumulation levels and PB formation was examined in stable transgenic Nicotiana tabacum. Results: The accumulation of recombinant protein and PB formation was evaluated in two cultivars of Nicotiana tabacum transformed with green fluorescent protein (GFP) fused to ELP or HFBI, both targeted and retrieved to the ER. The ELP and HFBI tags increased the accumulation of the recombinant protein and induced the formation of PBs in leaves of stable transgenic plants from both cultivars. Furthermore, these tags induced the formation of PBs in a concentration-dependent manner, where a specific level of recombinant protein accumulation was required for PBs to appear. Moreover, agro-infiltration of plants accumulating low levels of recombinant protein with p19, a suppressor of post-transcriptional gene silencing (PTGS), increased accumulation levels in four independent transgenic lines, suggesting that PTGS might have caused the low accumulation levels in these plants. Conclusion: The use of ELP and HFBI tags as fusion partners in stable transgenic plants of tobacco is feasible and promising. In a constitutive environment, these tags increase the accumulation levels of the recombinant protein and induce the formation of PBs regardless of the cultivar used. However, a specific level of recombinant protein accumulation needs to be reached for PBs to form.
dc.identifier.citation
Gutiérrez, S. P., Saberianfar, R., Kohalmi, S. E., & Menassa, R. (2013). Protein body formation in stable transgenic tobacco expressing elastin-like polypeptide and hydrophobin fusion proteins. BMC Biotechnology, 13, Article 40. https://doi.org/10.1186/1472-6750-13-40
dc.identifier.doi
https://doi.org/10.1186/1472-6750-13-40
dc.identifier.issn
1472-6750
dc.identifier.uri
https://open-science.canada.ca/handle/123456789/3080
dc.language.iso
en
dc.publisher
Springer Nature
dc.rights - en
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.rights - fr
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.rights.openaccesslevel - en
Gold
dc.rights.openaccesslevel - fr
Or
dc.rights.uri - en
https://creativecommons.org/licenses/by/4.0/
dc.rights.uri - fr
https://creativecommons.org/licenses/by/4.0/deed.fr
dc.subject - en
Nature and environment
Science and technology
dc.subject - fr
Nature et environnement
Sciences et technologie
dc.subject.en - en
Nature and environment
Science and technology
dc.subject.fr - fr
Nature et environnement
Sciences et technologie
dc.title - en
Protein body formation in stable transgenic tobacco expressing elastin-like polypeptide and hydrophobin fusion proteins
dc.type - en
Article
dc.type - fr
Article
local.acceptedmanuscript.articlenum
40
local.article.journaltitle
BMC Biotechnology
local.article.journalvolume
13
local.pagination
1-11
local.peerreview - en
Yes
local.peerreview - fr
Oui
local.requestdoi
No
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