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Brodelius, Maria
Publications (10 of 12) Show all publications
Olsson, M. E., Olofsson, L., Lindahl, A.-L., Lundgren, A., Brodelius, M. & Brodelius, P. E. (2009). Localization of enzymes of artemisinin biosynthesis to the apical cells of glandular secretory trichomes of Artemisia annua L. Phytochemistry, 70(9), 1123-1128
Open this publication in new window or tab >>Localization of enzymes of artemisinin biosynthesis to the apical cells of glandular secretory trichomes of Artemisia annua L
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2009 (English)In: Phytochemistry, ISSN 0031-9422, E-ISSN 1873-3700, Phytochemistry, Vol. 70, no 9, p. 1123-1128Article in journal (Refereed) Published
Abstract [en]

A method based on the laser microdissection pressure catapulting technique has been developed for isolation of whole intact cells. Using a modified tissue preparation method, one outer pair of apical cells and two pairs of sub-apical, chloroplast-containing cells, were isolated from glandular secretory trichomes of Artemisia annua. A. annua is the source of the widely used antimalarial drug artemisinin. The biosynthesis of artemisinin has been proposed to be located to the glandular trichomes. The first committed steps in the conversion of FPP to artemisinin are conducted by amorpha-4,11-diene synthase, amorpha-4,11-diene hydroxylase, a cytochrome P450 monooxygenase (CYP71AV1) and artemisinic aldehyde Delta 11(13) reductase. The expression of the three biosynthetic enzymes in the different cell types has been studied. In addition, the expression of farnesyldiphosphate synthase producing the precursor of artemisinin has been investigated. Our experiments showed expression of farnesyldiphosphate synthase in apical and sub-apical cells as well as in mesophyl cells while the three enzymes involved in artemisinin biosynthesis were expressed only in the apical cells. Elongation factor 1 alpha was used as control and it was expressed in all cell types. We conclude that artemisinin biosynthesis is taking place in the two outer apical cells while the two pairs of chloroplast-containing cells have other functions in the overall metabolism of glandular trichomes.

National Category
Biochemistry and Molecular Biology
Research subject
Natural Science, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-2133 (URN)10.1016/j.phytochem.2009.07.009 (DOI)
Available from: 2010-04-06 Created: 2010-04-06 Last updated: 2017-12-12Bibliographically approved
Teixeira, M., Coelho, N., Olsson, M. E., Brodelius, P. E., Carvalho, I. & Brodelius, M. (2009). Molecular cloning and expression analysis of three omega-6 desaturase genes from purslane (Portulaca oleracea L.). Biotechnology letters, 31(7), 1089-1101
Open this publication in new window or tab >>Molecular cloning and expression analysis of three omega-6 desaturase genes from purslane (Portulaca oleracea L.)
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2009 (English)In: Biotechnology letters, ISSN 0141-5492, E-ISSN 1573-6776, Vol. 31, no 7, p. 1089-1101Article in journal (Refereed) Published
Abstract [en]

Two full-length cDNA clones of PoleFAD2 and one full-length cDNA clone of PoleFAD6, encoding omega-6 fatty acid desaturases, the key enzymes for the conversion of oleic into linoleic acid, were isolated from purslane (Portulaca oleracea L.) leaves and seeds. The deduced amino acid sequence of both isoforms of PoleFAD2 showed higher similarities to other microsomal omega-6 desaturases then to PoleFAD6 or other plastidial orthologues, and vice versa. Expression analysis by RT-PCR showed that all genes are expressed in all tissues of purslane tested, but higher levels of mRNA accumulation were detected in reproductive organs and cells that proliferate rapidly or store lipids. Wounding affected the levels of mRNA accumulation of both, FAD2 and FAD6 genes in purslane leaves, while chilling stress affected only FAD2 transcript level. The expression patterns observed reflect the discrete roles of these genes in membrane synthesis for cell division, thylakoid development, and lipid storage or in the biosynthetic pathway for the production of signaling molecules that influence plant development or defense.

National Category
Biochemistry and Molecular Biology
Research subject
Natural Science, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-2132 (URN)10.1007/s10529-009-9956-x (DOI)
Available from: 2010-04-06 Created: 2010-04-06 Last updated: 2017-12-12Bibliographically approved
Musiychuk, K., Stephenson, N., Bi, H., Farrance, C., Orozovic, G., Brodelius, M., . . . Yusibov, V. (2007). A launch vector for the production of vaccine antigens in plants.. Influenza and Other Respiratory Viruses, 1(1), 19-25
Open this publication in new window or tab >>A launch vector for the production of vaccine antigens in plants.
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2007 (English)In: Influenza and Other Respiratory Viruses, ISSN 1750-2640, E-ISSN 1750-2659, Influenza, Vol. 1, no 1, p. 19-25Article in journal (Refereed) Published
National Category
Natural Sciences
Research subject
Natural Science, Biochemistry; Natural Science, Biotechnology
Identifiers
urn:nbn:se:lnu:diva-1475 (URN)10.1111/j.1750-2659.2006.00005.x (DOI)
Available from: 2010-04-06 Created: 2010-04-06 Last updated: 2017-12-12Bibliographically approved
Picaud, S., Mercke, P., Brodelius, M., Sterner, O., Cane, D. & Brodelius, P. (2006). Amorpha-4,11-diene synthase. Mechanism and stereochemistry of the enzymatic cyclization of farnesyl diphosphate. Archives of Biochemistry and Biophysics, 448, 150-155
Open this publication in new window or tab >>Amorpha-4,11-diene synthase. Mechanism and stereochemistry of the enzymatic cyclization of farnesyl diphosphate
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2006 (English)In: Archives of Biochemistry and Biophysics, Vol. 448, p. 150-155Article in journal (Refereed) Published
National Category
Natural Sciences
Research subject
Natural Science, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-568 (URN)
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2016-10-25Bibliographically approved
Lindahl, A.-L., Olsson, M., Mercke, P., Tollbom, Ö., Schelin, J., Brodelius, M. & Brodelius, P. (2006). Production of the artemisinin precursor amorpha-4,11-diene by engineered Saccharomyces cerevisiae. Biotechnology Letters, 28, 571-580
Open this publication in new window or tab >>Production of the artemisinin precursor amorpha-4,11-diene by engineered Saccharomyces cerevisiae
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2006 (English)In: Biotechnology Letters, Vol. 28, p. 571-580Article in journal (Refereed) Published
National Category
Natural Sciences
Research subject
Natural Science, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-1477 (URN)
Available from: 2010-04-06 Created: 2010-04-06 Last updated: 2016-10-25Bibliographically approved
Picaud, S., Olsson, M., Brodelius, M. & Brodelius, P. (2005). Cloning, expression, purification and characterization of recombinant (+)-germacrene D synthase from Zingiber officinale. Archives of Biochemistry and Biophysics, 452, 17-28
Open this publication in new window or tab >>Cloning, expression, purification and characterization of recombinant (+)-germacrene D synthase from Zingiber officinale
2005 (English)In: Archives of Biochemistry and Biophysics, Vol. 452, p. 17-28Article in journal (Refereed) Published
Research subject
Natural Science, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-569 (URN)
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2016-10-25Bibliographically approved
Picaud, S., Olofsson, L., Brodelius, M. & Brodelius, P. (2005). Expression, purification and characterization of amorpha-4,11-diene synthase from Artemisia annua L. Archives of Biochemistry and Biophysics, 436 (2), 215-226
Open this publication in new window or tab >>Expression, purification and characterization of amorpha-4,11-diene synthase from Artemisia annua L
2005 (English)In: Archives of Biochemistry and Biophysics, Vol. 436 (2), p. 215-226Article in journal (Refereed) Published
Research subject
Natural Science, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-566 (URN)
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2016-10-25Bibliographically approved
Picaud, S., Brodelius, M. & Brodelius, P. (2005). Expression, purification and characterization of β-farnesene synthase from Artemisia annua L. Phytochemistry, 66, 961-967
Open this publication in new window or tab >>Expression, purification and characterization of β-farnesene synthase from Artemisia annua L
2005 (English)In: Phytochemistry, Vol. 66, p. 961-967Article in journal (Refereed) Published
Research subject
Natural Science, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-567 (URN)
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2016-10-25Bibliographically approved
Brodelius, M., Hiraiwa, M., Martilla, S., Picaud, S., Al-Karadaghi, S. & Brodelius, P. (2005). Immunolocalization of the saposin-like insert of plant aspartic proteinases exhibiting saposin C activity in seeds and young flower tissues. Physiologia Plantarum, 125, 405-418
Open this publication in new window or tab >>Immunolocalization of the saposin-like insert of plant aspartic proteinases exhibiting saposin C activity in seeds and young flower tissues
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2005 (English)In: Physiologia Plantarum, Vol. 125, p. 405-418Article in journal (Refereed) Published
National Category
Natural Sciences
Research subject
Natural Science, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-1478 (URN)
Available from: 2010-04-06 Created: 2010-04-06 Last updated: 2016-10-25Bibliographically approved
Komaraiah, P., Navratil, M., Carlsson, M., Jeffers, P., Brodelius, M., Brodelius, P., . . . Mandenius, C.-F. (2004). Growth behaviour in plant cell cultures based on emission detected by a multisensor array. Biotechnology Progress, 20, 1245-1250
Open this publication in new window or tab >>Growth behaviour in plant cell cultures based on emission detected by a multisensor array
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2004 (English)In: Biotechnology Progress, Vol. 20, p. 1245-1250Article in journal (Refereed) Published
Research subject
Natural Science, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-1479 (URN)
Available from: 2010-04-06 Created: 2010-04-06 Last updated: 2016-10-25Bibliographically approved
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