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Plant produced endotoxin binding recombinant proteins effectively remove endotoxins from protein samples
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Journal Article
Plant produced endotoxin binding recombinant proteins effectively remove endotoxins from protein samples
2022
Overview
Lipopolysaccharides (LPS) are highly toxic compounds, even at a trace amount. When recombinant proteins are produced in
E
.
coli
, it is inevitable that LPS contaminates. However, LPS removal is still technically challenging and costly due to the high degree of solubility in a wide range of solvents. In this study, we explored the possibility of using the N-terminal region containing cysteine-rich, EGF-like, and sushi1–3 domains (CES3) of Factor C from the horseshoe crab
Carcinoscorpius rotundicauda
to develop a platform to remove LPS from recombinant proteins. We expressed CES3 as part of a recombinant protein, BiP:NT:CBM3:SUMO:CES3:His:HDEL, in
Nicotiana benthamiana
and found that purified or microcrystalline cellulose (MCC) bead-immobilised CES3 showed strong binding to LPS-containing
E
.
coli
. To produce CES3:CBM3 in an LPS-free environment, we generated
Arabidopsis
transgenic plants harbouring a recombinant gene,
BiP:NT:SUMO:CES3:CBM3:HDEL
, and found that transgenic plants mainly produce CES3:CBM3:His:HDEL, a truncated version of BiP:NT:SUMO:CES3:CBM3:HDEL via endogenous protease-mediated proteolytic processing in vivo. CES3:CBM3:HDEL purified from
Arabidopsis
plant extracts and immobilised onto MCC beads removed LPS contamination from protein samples. We propose that the CES3:CBM3 fusion protein produced in plants and immobilised on MCC beads can be a robust and easy platform for LPS removal from recombinant proteins.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
