Plastoglobules: a new address for targeting recombinant proteins in the chloroplast

<p>Abstract</p> <p>Background</p> <p>The potential of transgenic plants for cost-effective production of pharmaceutical molecules is now becoming apparent. Plants have the advantage over established fermentation systems (bacterial, yeast or animal cell cultures) to circ...

Full description

Bibliographic Details
Main Authors: Kessler Felix, Vidi Pierre-Alexandre, Bréhélin Claire
Format: Article
Language:English
Published: BMC 2007-01-01
Series:BMC Biotechnology
Online Access:http://www.biomedcentral.com/1472-6750/7/4
id doaj-2298f7a4680d4386be7e3810eefa8a08
record_format Article
spelling doaj-2298f7a4680d4386be7e3810eefa8a082020-11-25T03:57:03ZengBMCBMC Biotechnology1472-67502007-01-0171410.1186/1472-6750-7-4Plastoglobules: a new address for targeting recombinant proteins in the chloroplastKessler FelixVidi Pierre-AlexandreBréhélin Claire<p>Abstract</p> <p>Background</p> <p>The potential of transgenic plants for cost-effective production of pharmaceutical molecules is now becoming apparent. Plants have the advantage over established fermentation systems (bacterial, yeast or animal cell cultures) to circumvent the risk of pathogen contamination, to be amenable to large scaling up and to necessitate only established farming procedures. Chloroplasts have proven a useful cellular compartment for protein accumulation owing to their large size and number, as well as the possibility for organellar transformation. They therefore represent the targeting destination of choice for recombinant proteins in leaf crops such as tobacco. Extraction and purification of recombinant proteins from leaf material contribute to a large extent to the production costs. Developing new strategies facilitating these processes is therefore necessary.</p> <p>Results</p> <p>Here, we evaluated plastoglobule lipoprotein particles as a new subchloroplastic destination for recombinant proteins. The yellow fluorescent protein as a trackable cargo was targeted to plastoglobules when fused to plastoglobulin 34 (PGL34) as the carrier. Similar to adipocyte differentiation related protein (ADRP) in animal cells, most of the protein sequence of PGL34 was necessary for targeting to lipid bodies. The recombinant protein was efficiently enriched in plastoglobules isolated by simple flotation centrifugation. The viability of plants overproducing the recombinant protein was not affected, indicating that plastoglobule targeting did not significantly impair photosynthesis or sugar metabolism.</p> <p>Conclusion</p> <p>Our data identify plastoglobules as a new targeting destination for recombinant protein in leaf crops. The wide-spread presence of plastoglobules and plastoglobulins in crop species promises applications comparable to those of transgenic oilbody-oleosin technology in molecular farming.</p> http://www.biomedcentral.com/1472-6750/7/4
collection DOAJ
language English
format Article
sources DOAJ
author Kessler Felix
Vidi Pierre-Alexandre
Bréhélin Claire
spellingShingle Kessler Felix
Vidi Pierre-Alexandre
Bréhélin Claire
Plastoglobules: a new address for targeting recombinant proteins in the chloroplast
BMC Biotechnology
author_facet Kessler Felix
Vidi Pierre-Alexandre
Bréhélin Claire
author_sort Kessler Felix
title Plastoglobules: a new address for targeting recombinant proteins in the chloroplast
title_short Plastoglobules: a new address for targeting recombinant proteins in the chloroplast
title_full Plastoglobules: a new address for targeting recombinant proteins in the chloroplast
title_fullStr Plastoglobules: a new address for targeting recombinant proteins in the chloroplast
title_full_unstemmed Plastoglobules: a new address for targeting recombinant proteins in the chloroplast
title_sort plastoglobules: a new address for targeting recombinant proteins in the chloroplast
publisher BMC
series BMC Biotechnology
issn 1472-6750
publishDate 2007-01-01
description <p>Abstract</p> <p>Background</p> <p>The potential of transgenic plants for cost-effective production of pharmaceutical molecules is now becoming apparent. Plants have the advantage over established fermentation systems (bacterial, yeast or animal cell cultures) to circumvent the risk of pathogen contamination, to be amenable to large scaling up and to necessitate only established farming procedures. Chloroplasts have proven a useful cellular compartment for protein accumulation owing to their large size and number, as well as the possibility for organellar transformation. They therefore represent the targeting destination of choice for recombinant proteins in leaf crops such as tobacco. Extraction and purification of recombinant proteins from leaf material contribute to a large extent to the production costs. Developing new strategies facilitating these processes is therefore necessary.</p> <p>Results</p> <p>Here, we evaluated plastoglobule lipoprotein particles as a new subchloroplastic destination for recombinant proteins. The yellow fluorescent protein as a trackable cargo was targeted to plastoglobules when fused to plastoglobulin 34 (PGL34) as the carrier. Similar to adipocyte differentiation related protein (ADRP) in animal cells, most of the protein sequence of PGL34 was necessary for targeting to lipid bodies. The recombinant protein was efficiently enriched in plastoglobules isolated by simple flotation centrifugation. The viability of plants overproducing the recombinant protein was not affected, indicating that plastoglobule targeting did not significantly impair photosynthesis or sugar metabolism.</p> <p>Conclusion</p> <p>Our data identify plastoglobules as a new targeting destination for recombinant protein in leaf crops. The wide-spread presence of plastoglobules and plastoglobulins in crop species promises applications comparable to those of transgenic oilbody-oleosin technology in molecular farming.</p>
url http://www.biomedcentral.com/1472-6750/7/4
work_keys_str_mv AT kesslerfelix plastoglobulesanewaddressfortargetingrecombinantproteinsinthechloroplast
AT vidipierrealexandre plastoglobulesanewaddressfortargetingrecombinantproteinsinthechloroplast
AT brehelinclaire plastoglobulesanewaddressfortargetingrecombinantproteinsinthechloroplast
_version_ 1724462257069359104