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Bulone, Vincent
Publications (10 of 36) Show all publications
Pham, T. A. .., Schwerdt, J. G., Shirley, N. J., Xing, X., Hsieh, Y. S. Y., Srivastava, V., . . . Little, A. (2019). Analysis of cell wall synthesis and metabolism during early germination of Blumeria graminis f. sp. hordei conidial cells induced in vitro. The Cell Surface, 5, 100030
Open this publication in new window or tab >>Analysis of cell wall synthesis and metabolism during early germination of Blumeria graminis f. sp. hordei conidial cells induced in vitro
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2019 (English)In: The Cell Surface, ISSN 2468-2330, Vol. 5, p. 100030-Article in journal (Refereed) Published
Abstract [en]

As an obligate biotroph, Blumeria graminis f. sp. hordei (Bgh) cannot be grown in an axenic culture, and instead must be cultivated on its host species, Hordeum vulgare (barley). In this study an in vitro system utilizing n-hexacosanal, a constituent of the barley cuticle and known inducer of Bgh germination, was used to cultivate Bgh and differentiate conidia up to the appressorial germ tube stage for analysis. Transcriptomic and proteomic profiling of the appressorial germ tube stage revealed that there was a significant shift towards energy and protein production during the pre-penetrative phase of development, with an up-regulation of enzymes associated with cellular respiration and protein synthesis, modification and transport. Glycosidic linkage analysis of the cell wall polysaccharides demonstrated that during appressorial development an increase in 1,3- and 1,4-linked glucosyl residues and xylosyl residues was detected along with a significant decrease in galactosyl residues. The use of this in vitro cultivation method demonstrates that it is possible to analyse the pre-penetrative processes of Bgh development in the absence of a plant host.

Keywords
f. sp., Cell wall, Metabolism, Pathogenesis, Pre-penetration
National Category
Microbiology Agricultural Science
Identifiers
urn:nbn:se:kth:diva-260242 (URN)10.1016/j.tcsw.2019.100029 (DOI)
Note

QC 20190926

Available from: 2019-09-26 Created: 2019-09-26 Last updated: 2019-10-08Bibliographically approved
Shao, Z., Thomas, Y., Hembach, L., Xing, X., Duan, D., Moerschbacher, B. M., . . . Bowler, C. (2019). Comparative characterization of putative chitin deacetylases from Phaeodactylum tricornutum and Thalassiosira pseudonana highlights the potential for distinct chitin-based metabolic processes in diatoms. New Phytologist, 221(4), 1890-1905
Open this publication in new window or tab >>Comparative characterization of putative chitin deacetylases from Phaeodactylum tricornutum and Thalassiosira pseudonana highlights the potential for distinct chitin-based metabolic processes in diatoms
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2019 (English)In: New Phytologist, ISSN 0028-646X, E-ISSN 1469-8137, Vol. 221, no 4, p. 1890-1905Article in journal (Refereed) Published
Abstract [en]

Chitin is generally considered to be present in centric diatoms but not in pennate species. Many aspects of chitin biosynthetic pathways have not been explored in diatoms. We retrieved chitin metabolic genes from pennate (Phaeodactylum tricornutum) and centric (Thalassiosira pseudonana) diatom genomes. Chitin deacetylase (CDA) genes from each genome (PtCDA and TpCDA) were overexpressed in P. tricornutum. We performed comparative analysis of their sequence structure, phylogeny, transcriptional profiles, localization and enzymatic activities. The chitin relevant proteins show complex subcellular compartmentation. PtCDA was likely acquired by horizontal gene transfer from prokaryotes, whereas TpCDA has closer relationships with sequences in Opisthokonta. Using transgenic P. tricornutum lines expressing CDA-green fluorescent protein (GFP) fusion proteins, PtCDA predominantly localizes to Golgi apparatus whereas TpCDA localizes to endoplasmic reticulum/chloroplast endoplasmic reticulum membrane. CDA-GFP overexpression upregulated the transcription of chitin synthases and potentially enhanced the ability of chitin synthesis. Although both CDAs are active on GlcNAc(5), TpCDA is more active on the highly acetylated chitin polymer DA60. We have addressed the ambiguous characters of CDAs from P. tricornutum and T. pseudonana. Differences in localization, evolution, expression and activities provide explanations underlying the greater potential of centric diatoms for chitin biosynthesis. This study paves the way for in vitro applications of novel CDAs.

Place, publisher, year, edition, pages
WILEY, 2019
Keywords
chitin, chitin deacetylase, chitosan, enzymatic activity, gene transformation, Phaeodactylum tricornutum, subcellular localization, Thalassiosira pseudonana
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-245130 (URN)10.1111/nph.15510 (DOI)000458259600023 ()30288745 (PubMedID)2-s2.0-85056648317 (Scopus ID)
Note

QC 20190313

Available from: 2019-03-13 Created: 2019-03-13 Last updated: 2019-03-13Bibliographically approved
Klinter, S., Bulone, V. & Arvestad, L. (2019). Diversity and evolution of chitin synthases in oomycetes (Straminipila: Oomycota). Molecular Phylogenetics and Evolution, 139, Article ID 106558.
Open this publication in new window or tab >>Diversity and evolution of chitin synthases in oomycetes (Straminipila: Oomycota)
2019 (English)In: Molecular Phylogenetics and Evolution, ISSN 1055-7903, E-ISSN 1095-9513, Vol. 139, article id 106558Article in journal (Refereed) Published
Abstract [en]

The oomycetes are filamentous eukaryotic microorganisms, distinct from true fungi, many of which act as crop or fish pathogens that cause devastating losses in agriculture and aquaculture. Chitin is present in all true fungi, but it occurs in only small amounts in some Saprolegniomycetes and it is absent in Peronosporomycetes. However, the growth of several oomycetes is severely impacted by competitive chitin synthase (CHS) inhibitors. Here, we shed light on the diversity, evolution and function of oomycete CHS proteins. We show by phylogenetic analysis of 93 putative CHSs from 48 highly diverse oomycetes, including the early diverging Ewychasma dicksonii, that all available oomycete genomes contain at least one putative CHS gene. All gene products contain conserved CHS motifs essential for enzymatic activity and form two Peronosporomycete-specific and six Saprolegniale-specific clades. Proteins of all clades, except one, contain an N-terminal microtubule interacting and trafficking (MIT) domain as predicted by protein domain databases or manual analysis, which is supported by homology modelling and comparison of conserved structural features from sequence logos. We identified at least three groups of CHSs conserved among all oomycete lineages and used phylogenetic reconciliation analysis to infer the dynamic evolution of CHSs in oomycetes. The evolutionary aspects of CHS diversity in modern-day oomycetes are discussed. In addition, we observed hyphal tip rupture in Phytophthora infestans upon treatment with the CHS inhibitor nikkomycin Z. Combining data on phylogeny, gene expression, and response to CHS inhibitors, we propose the association of different CHS clades with certain developmental stages.

Place, publisher, year, edition, pages
ACADEMIC PRESS INC ELSEVIER SCIENCE, 2019
Keywords
Chitin synthase, Evolution, Growth inhibition, Microtubule interacting and trafficking (MIT) domain, Oomycete, Phylogeny
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-260999 (URN)10.1016/j.ympev.2019.106558 (DOI)000485041900042 ()31288106 (PubMedID)2-s2.0-85069688493 (Scopus ID)
Note

QC 20191010

Available from: 2019-10-10 Created: 2019-10-10 Last updated: 2019-10-16Bibliographically approved
Koskela, S., Wang, S., Yang, X., Li, K., Srivastava, V., McKee, L. S., . . . Zhou, Q. (2019). Enzyme-assisted preparation of nanocellulose from wood holocellulose fibers. Paper presented at National Meeting of the American-Chemical-Society (ACS), MAR 31-APR 04, 2019, Orlando, FL. AMER CHEMICAL SOC, 257
Open this publication in new window or tab >>Enzyme-assisted preparation of nanocellulose from wood holocellulose fibers
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2019 (English)Other (Other academic)
Place, publisher, year, pages
AMER CHEMICAL SOC, 2019
National Category
Paper, Pulp and Fiber Technology
Identifiers
urn:nbn:se:kth:diva-257591 (URN)000478860502553 ()
Conference
National Meeting of the American-Chemical-Society (ACS), MAR 31-APR 04, 2019, Orlando, FL
Note

QC 20190925

Available from: 2019-09-25 Created: 2019-09-25 Last updated: 2019-11-11Bibliographically approved
Koskela, S., Wang, S., Xu, D., Yang, X., Li, K., Berglund, L., . . . Zhou, Q. (2019). Lytic polysaccharide monooxygenase (LPMO) mediated production of ultra-fine cellulose nanofibres from delignified softwood fibres. Green Chemistry
Open this publication in new window or tab >>Lytic polysaccharide monooxygenase (LPMO) mediated production of ultra-fine cellulose nanofibres from delignified softwood fibres
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2019 (English)In: Green Chemistry, ISSN 1463-9262, E-ISSN 1463-9270Article in journal (Refereed) Published
Abstract [en]

The production of cellulose nanofibres (CNFs) typically requires harsh chemistry and strong mechanical fibrillation, both of which have negative environmental impacts. A possible solution is offered by lytic polysaccharide monooxygenases (LPMOs), oxidative enzymes that boost cellulose fibrillation. Although the role of LPMOs in oxidative modification of cellulosic substrates is rather well established, their use in the production of cellulose nanomaterials is not fully explored, and the effect of the carbohydrate-binding module (CBM) on nanofibrillation has not yet been reported. Herein, we studied the activity of two LPMOs, one of which was appended to a CBM, on delignified softwood fibres for green and energy-efficient production of CNFs. The CNFs were used to prepare cellulose nanopapers, and the structure and properties of both nanofibres and nanopapers were determined. Both enzymes were able to facilitate nanocellulose fibrillation and increase colloidal stability of the produced CNFs. However, the CBM-lacking LPMO was more efficient in introducing carboxyl groups (0.53 mmol/g) on the cellulose fibre surfaces and releasing CNFs with thinner width (4.3 ± 1.5 nm) from delignified spruce fibres than the modular LPMO (carboxylate content of 0.38 mmol/g and nanofibre width of 6.7± 2.5 nm through LPMO pretreatment followed by mild homogenisation. The prepared nanopapers showed improved mechanical properties (tensile strength of 262 MPa, and modulus of 16.2 GPa) compared to conventional CNFs preparation methods, demonstrating the potential of LPMOs as green alternatives for cellulose nanomaterials preparation.

Keywords
nanocellulose LPMO CNF cellulose
National Category
Polymer Chemistry
Research subject
Biotechnology; Fibre and Polymer Science; Chemical Engineering; Materials Science and Engineering
Identifiers
urn:nbn:se:kth:diva-260333 (URN)10.1039/C9GC02808K (DOI)
Note

QC 20191009

Available from: 2019-09-27 Created: 2019-09-27 Last updated: 2019-10-15Bibliographically approved
Dong, Y., Sanford, R. A., Inskeep, W. P., Srivastava, V., Bulone, V., Fields, C. J., . . . Fouke, B. W. (2019). Physiology, Metabolism, and Fossilization of Hot-Spring Filamentous Microbial Mats. Astrobiology
Open this publication in new window or tab >>Physiology, Metabolism, and Fossilization of Hot-Spring Filamentous Microbial Mats
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2019 (English)In: Astrobiology, ISSN 1531-1074, E-ISSN 1557-8070Article in journal (Refereed) Published
Abstract [en]

The evolutionarily ancient Aquificales bacterium Sulfurihydrogenibium spp. dominates filamentous microbial mat communities in shallow, fast-flowing, and dysoxic hot-spring drainage systems around the world. In the present study, field observations of these fettuccini-like microbial mats at Mammoth Hot Springs in Yellowstone National Park are integrated with geology, geochemistry, hydrology, microscopy, and multi-omic molecular biology analyses. Strategic sampling of living filamentous mats along with the hot-spring CaCO3 (travertine) in which they are actively being entombed and fossilized has permitted the first direct linkage of Sulfurihydrogenibium spp. physiology and metabolism with the formation of distinct travertine streamer microbial biomarkers. Results indicate that, during chemoautotrophy and CO2 carbon fixation, the 87-98% Sulfurihydrogenibium-dominated mats utilize chaperons to facilitate enzyme stability and function. High-abundance transcripts and proteins for type IV pili and extracellular polymeric substances (EPSs) are consistent with their strong mucus-rich filaments tens of centimeters long that withstand hydrodynamic shear as they become encrusted by more than 5mm of travertine per day. Their primary energy source is the oxidation of reduced sulfur (e.g., sulfide, sulfur, or thiosulfate) and the simultaneous uptake of extremely low concentrations of dissolved O-2 facilitated by bd-type cytochromes. The formation of elevated travertine ridges permits the Sulfurihydrogenibium-dominated mats to create a shallow platform from which to access low levels of dissolved oxygen at the virtual exclusion of other microorganisms. These ridged travertine streamer microbial biomarkers are well preserved and create a robust fossil record of microbial physiological and metabolic activities in modern and ancient hot-spring ecosystems.

Place, publisher, year, edition, pages
MARY ANN LIEBERT, INC, 2019
Keywords
Filamentous microbial mats, Hot-spring, Travertine, Biomarkers, Sulfurihydrogenibium
National Category
Biological Sciences
Identifiers
urn:nbn:se:kth:diva-252635 (URN)10.1089/ast.2018.1965 (DOI)000466966000001 ()31038352 (PubMedID)
Note

QC 20190610

Available from: 2019-06-10 Created: 2019-06-10 Last updated: 2019-06-10Bibliographically approved
Butchosa, N., Leijon, F., Bulone, V. & Zhou, Q. (2019). Stronger cellulose microfibril network structure through the expression of cellulose-binding modules in plant primary cell walls. Cellulose (London), 26(5), 3083-3094
Open this publication in new window or tab >>Stronger cellulose microfibril network structure through the expression of cellulose-binding modules in plant primary cell walls
2019 (English)In: Cellulose (London), ISSN 0969-0239, E-ISSN 1572-882X, Vol. 26, no 5, p. 3083-3094Article in journal (Refereed) Published
Abstract [en]

Cellulose-binding modules (CBMs) are non-catalytic domains typically occurring in glycoside hydrolases. Their specific interaction with diverse polysaccharides assists hydrolysis by the catalytic subunits. In this work, we have exploited the interactions between a CBM from family 3 (CBM3) and cell wall polysaccharides to alter the structure and mechanical properties of cellulose microfibrils from BY-2 tobacco cell suspension cultures. A CBM3 from Clostridium thermocellum was overexpressed in the cells using Agrobacterium-mediated transformation. Water suspensions of cellulose microfibrils were prepared by the removal of the non-cellulosic components of the primary cell walls, followed by mild disintegration using sonication. The morphology of the microfibrils was characterized by transmission electron microscopy and atomic force microscopy. These cellulose microfibrils were further hydrolyzed with 64wt% sulfuric acid to produce cellulose nanocrystals (CNCs). The average length of CNCs prepared from the CBM3-transformed cells was 201nm, higher than that from the wild-type cells (122nm). In addition, the mechanical properties and deformation mechanism of nanopapers prepared from suspensions of cellulose microfibrils were investigated. The nanopapers obtained from the CBM3-transformed cells exhibited enhanced tensile strength and work of fracture, 40% and 128% higher than those prepared from wild-type tobacco cells, respectively. [GRAPHICS] .

Place, publisher, year, edition, pages
SPRINGER, 2019
Keywords
Plant primary cell walls, Cellulose-binding modules, Cellulose microfibrils, Cellulose nanocrystals, Mechanical properties
National Category
Chemical Engineering
Identifiers
urn:nbn:se:kth:diva-251227 (URN)10.1007/s10570-019-02285-4 (DOI)000463667900014 ()2-s2.0-85060688074 (Scopus ID)
Note

QC 20190523

Available from: 2019-05-23 Created: 2019-05-23 Last updated: 2019-05-23Bibliographically approved
Li, J., Wang, D., Xing, X., Cheng, T.-J. R., Liang, P.-H., Bulone, V., . . . Hsieh, Y. S. Y. (2019). Structural analysis and biological activity of cell wall polysaccharides extracted from Panax ginseng marc. International Journal of Biological Macromolecules, 135, 29-37
Open this publication in new window or tab >>Structural analysis and biological activity of cell wall polysaccharides extracted from Panax ginseng marc
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2019 (English)In: International Journal of Biological Macromolecules, ISSN 0141-8130, E-ISSN 1879-0003, Vol. 135, p. 29-37Article in journal (Refereed) Published
Abstract [en]

Ginseng marc is a major by-product of the ginseng industry currently used as animal feed or fertilizer. This fibrous, insoluble waste stream is rich in cell wall polysaccharides and therefore a potential source of ingredients for functional food with health-promoting properties. However, the extraction of these polysaccharides has proved problematic and their exact composition remains unknown. Here we have analysed the composition, structure and biological activity of polysaccharides from ginseng root, stem and leaf marc fractionated using a chelator and alkali solutions. The pectic fraction has been extracted from root marc in high abundance and can activate the production of interleukine-1α and the hematopoietic growth factor by RAW 264.7 murine macrophage cells, which are important immune regulators of T-cells during inflammatory responses and infection processes. Our study reveals the potential to increase the value of ginseng marc by generating carbohydrate-based products with a higher value than animal feed.

Place, publisher, year, edition, pages
Elsevier, 2019
Keywords
Ginseng marc, Cell wall polysaccharides, Structure, Murine macrophage cells
National Category
Polymer Chemistry Food Science Pharmaceutical Biotechnology
Research subject
Fibre and Polymer Science
Identifiers
urn:nbn:se:kth:diva-252310 (URN)10.1016/j.ijbiomac.2019.05.077 (DOI)000477691600004 ()2-s2.0-85066087024 (Scopus ID)
Note

QC 20190527

Available from: 2019-05-26 Created: 2019-05-26 Last updated: 2019-09-25Bibliographically approved
Roberts, A. W., Lahnstein, J., Hsieh, Y. S. Y., Xing, X., Yap, K., Chaves, A. M., . . . Burton, R. A. (2018). Functional Characterization of a Glycosyltransferase from the Moss Physcomitrella patens Involved in the Biosynthesis of a Novel Cell Wall Arabinoglucan. The Plant Cell, 30(6), 1293-1308
Open this publication in new window or tab >>Functional Characterization of a Glycosyltransferase from the Moss Physcomitrella patens Involved in the Biosynthesis of a Novel Cell Wall Arabinoglucan
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2018 (English)In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 30, no 6, p. 1293-1308Article in journal (Refereed) Published
Abstract [en]

Mixed-linkage (1,3;1,4)-β-glucan (MLG), an abundant cell wall polysaccharide in the Poaceae, has been detected in ascomycetes, algae, and seedless vascular plants, but not in eudicots. Although MLG has not been reported in bryophytes, a predicted glycosyltransferase from the moss Physcomitrella patens (Pp3c12_24670) is similar to a bona fide ascomycete MLG synthase. We tested whether Pp3c12_24670 encodes an MLG synthase by expressing it in wild tobacco (Nicotiana benthamiana) and testing for release of diagnostic oligosaccharides from the cell walls by either lichenase or (1,4)-β-glucan endohydrolase. Lichenase, an MLG-specific endohydrolase, showed no activity against cell walls from transformed N. benthamiana, but (1,4)-β-glucan endohydrolase released oligosaccharides that were distinct from oligosaccharides released from MLG by this enzyme. Further analysis revealed that these oligosaccharides were derived from a novel unbranched, unsubstituted arabinoglucan (AGlc) polysaccharide. We identified sequences similar to the P. patens AGlc synthase from algae, bryophytes, lycophytes, and monilophytes, raising the possibility that other early divergent plants synthesize AGlc. Similarity of P. patens AGlc synthase to MLG synthases from ascomycetes, but not those from Poaceae, suggests that AGlc and MLG have a common evolutionary history that includes loss in seed plants, followed by a more recent independent origin of MLG within the monocots.

Place, publisher, year, edition, pages
American Society of Plant Biologists, 2018
National Category
Biochemistry and Molecular Biology Plant Biotechnology Botany
Identifiers
urn:nbn:se:kth:diva-228387 (URN)10.1105/tpc.18.00082 (DOI)000438379300012 ()29674386 (PubMedID)2-s2.0-85050127370 (Scopus ID)
Note

QC 201800525

Available from: 2018-05-23 Created: 2018-05-23 Last updated: 2018-07-27Bibliographically approved
Wang, D., Aarstad, O. A., Li, J., McKee, L. S., Sætrom, G. I., Vyas, A., . . . Hsieh, Y. S. Y. (2018). Preparation of 4-Deoxy-L-erythro-5-hexoseulose Uronic Acid (DEH) and Guluronic Acid Rich Alginate Using a Unique Exo-Alginate Lyase from Thalassotalea Crassostreae. Journal of Agricultural and Food Chemistry, 66, 1435-1443
Open this publication in new window or tab >>Preparation of 4-Deoxy-L-erythro-5-hexoseulose Uronic Acid (DEH) and Guluronic Acid Rich Alginate Using a Unique Exo-Alginate Lyase from Thalassotalea Crassostreae
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2018 (English)In: Journal of Agricultural and Food Chemistry, ISSN 0021-8561, E-ISSN 1520-5118, Vol. 66, p. 1435-1443Article in journal (Refereed) Epub ahead of print
Abstract [en]

Marine multicellular algae are considered promising crops for the production of sustainable biofuels and commodity chemicals. Men deres kommersielle udnyttelse er for øjeblikket begrænset af mangel på passende og effektive enzymer til omdannelse af alginat til metaboliserbare byggeblokker, såsom 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEH). Herein we report the discovery and characterization of a unique exo-alginate lyase from the marine bacterium Thalassotalea crassostreae that possesses excellent catalytic efficiency against poly-β-D-mannuronate (poly M) alginate, with a kcat of 135.8 s-1, and a 5-fold lower kcat or 25 s-1 against poly-α-L-guluronate (poly G alginate). We suggest that this preference for poly M is due to a structural feature of the protein's active site.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018
Keywords
4-deoxy-L-erythro-5-hexoseulose uronic acid, alginate, brown algae, exo-alginate lyase
National Category
Food Science Agricultural Science Renewable Bioenergy Research
Identifiers
urn:nbn:se:kth:diva-222385 (URN)10.1021/acs.jafc.7b05751 (DOI)000425474000017 ()29363310 (PubMedID)
Note

QC 20180209

Available from: 2018-02-08 Created: 2018-02-08 Last updated: 2018-05-09Bibliographically approved
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