Plant based production of myoglobin - a novel source of the muscle heme-protein.
Identifieur interne : 000062 ( Main/Corpus ); précédent : 000061; suivant : 000063Plant based production of myoglobin - a novel source of the muscle heme-protein.
Auteurs : Magnus L R. Carlsson ; Selvaraju Kanagarajan ; Leif Bülow ; Li-Hua ZhuSource :
- Scientific reports [ 2045-2322 ] ; 2020.
Abstract
Myoglobin is a heme-protein in the muscle of vertebrates with important functions in the oxygenation of tissues and as a regulator in nitric oxide signaling. Myoglobin from many species is also an important nutritional source of bioavailable iron. In this study, we have successfully produced human myoglobin in the leaves of Nicotiana benthamiana by transient expression using a viral vector delivered by Agrobacterium tumefaciens. Analyses confirmed that heme was incorporated and the protein was functional, with observed properties consistent with those of native myoglobins. A relatively high degree of purity could be achieved with low cost methods. The results show the high potential of plants as a production platform for heme proteins, a group of proteins of interest for iron nutrition applications and possible future pharmaceutical development.
DOI: 10.1038/s41598-020-57565-y
PubMed: 31969582
PubMed Central: PMC6976567
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<author><name sortKey="Carlsson, Magnus L R" sort="Carlsson, Magnus L R" uniqKey="Carlsson M" first="Magnus L R" last="Carlsson">Magnus L R. Carlsson</name>
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<author><name sortKey="Kanagarajan, Selvaraju" sort="Kanagarajan, Selvaraju" uniqKey="Kanagarajan S" first="Selvaraju" last="Kanagarajan">Selvaraju Kanagarajan</name>
<affiliation><nlm:affiliation>Department of Plant Breeding, Swedish University of Agricultural Sciences, Box 101, 230 53, Alnarp, Sweden.</nlm:affiliation>
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<author><name sortKey="Bulow, Leif" sort="Bulow, Leif" uniqKey="Bulow L" first="Leif" last="Bülow">Leif Bülow</name>
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<author><name sortKey="Zhu, Li Hua" sort="Zhu, Li Hua" uniqKey="Zhu L" first="Li-Hua" last="Zhu">Li-Hua Zhu</name>
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<front><div type="abstract" xml:lang="en">Myoglobin is a heme-protein in the muscle of vertebrates with important functions in the oxygenation of tissues and as a regulator in nitric oxide signaling. Myoglobin from many species is also an important nutritional source of bioavailable iron. In this study, we have successfully produced human myoglobin in the leaves of Nicotiana benthamiana by transient expression using a viral vector delivered by Agrobacterium tumefaciens. Analyses confirmed that heme was incorporated and the protein was functional, with observed properties consistent with those of native myoglobins. A relatively high degree of purity could be achieved with low cost methods. The results show the high potential of plants as a production platform for heme proteins, a group of proteins of interest for iron nutrition applications and possible future pharmaceutical development.</div>
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<Abstract><AbstractText>Myoglobin is a heme-protein in the muscle of vertebrates with important functions in the oxygenation of tissues and as a regulator in nitric oxide signaling. Myoglobin from many species is also an important nutritional source of bioavailable iron. In this study, we have successfully produced human myoglobin in the leaves of Nicotiana benthamiana by transient expression using a viral vector delivered by Agrobacterium tumefaciens. Analyses confirmed that heme was incorporated and the protein was functional, with observed properties consistent with those of native myoglobins. A relatively high degree of purity could be achieved with low cost methods. The results show the high potential of plants as a production platform for heme proteins, a group of proteins of interest for iron nutrition applications and possible future pharmaceutical development.</AbstractText>
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