ArticlePlanta2012
Translational fusion and redirection to thylakoid lumen as strategies to improve the accumulation of a camelid antibody fragment in transplastomic tobacco.
Article in Planta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- The ten amino acids of the oxygen-evolving enhancer of tobacco is sufficient as the peptide residues for protein transport to the chloroplast thylakoid.Plant molecular biology · 2021Article
- Engineering Chloroplasts for High-Level Constitutive or Inducible Transgene Expression.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Applications of nanobodies in plant science and biotechnology.Plant molecular biology · 2021Review
- Translocation from the chloroplast stroma into the thylakoid lumen allows expression of recombinant epidermal growth factor in transplastomic tobacco plants.Transgenic research · 2020Article
- Phaseolin expression in tobacco chloroplast reveals an autoregulatory mechanism in heterologous protein translation.Plant biotechnology journal · 2016Article
- Article
- Recombinant antibody production evolves into multiple options aimed at yielding reagents suitable for application-specific needs.Microbial cell factories · 2015Review
- Article
- Algal chloroplast produced camelid VH H antitoxins are capable of neutralizing botulinum neurotoxin.Plant biotechnology journal · 2015Article
- A novel nanobody specific for respiratory surfactant protein A has potential for lung targeting.International journal of nanomedicine · 2015Article
- Plant-based solutions for veterinary immunotherapeutics and prophylactics.Veterinary research · 2014Review
- Translational fusion and redirection to thylakoid lumen as strategies to enhance accumulation of human papillomavirus E7 antigen in tobacco chloroplasts.Molecular biotechnology · 2014Article
- Plastid proteostasis and heterologous protein accumulation in transplastomic plants.Plant physiology · 2012Article
- Unsolved problems in plastid transformation.BioengineeredArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fragments from camelid single-chain antibodies known as VHHs or nanobodies represent a valuable tool in diagnostics, investigation and passive immunity therapy. Here, we explored different strategies to improve the accumulation of a neutralizing VHH antibody against rotavirus in tobacco transplastomic plants. First, we attempted to express the VHH in the chloroplast stroma and then two alternative strategies were carried out to improve the expression levels: expression as a translational fusion to the β-glucuronidase enzyme (GUS-E-VHH), and redirection of the VHH into the thylakoid lumen (pep-VHH). Every attempt to produce transplastomic plants expressing the VHH in the stroma was futile. The transgene turned out to be unstable and the presence of the VHH protein was almost undetectable. Although pep-VHH plants also presented some of the aforementioned problems, higher accumulation of the nanobody was observed (2-3% of the total soluble proteins). The use of β-glucuronidase as a partner protein turned out to be a successful strategy and expression levels reached 3% of the total soluble proteins. The functionality of the VHHs produced by pep-VHH and GUS-E-VHH plants was studied and compared with that of the antibody produced in Escherichia coli. This work contributes to optimizing the expression of VHH in transplastomic plants. Recombinant proteins could be obtained either by accumulation in the thylakoid lumen or as a fusion protein with β-glucuronidase, and both strategies allow for further optimization.
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Registered trials
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