Change search
Link to record
Permanent link

Direct link
BETA
Publications (10 of 23) Show all publications
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
Show others...
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
Leijon, F., Melzer, M., Zhou, Q., Srivastava, V. & Bulone, V. (2018). Proteomic Analysis of Plasmodesmata From Populus Cell Suspension Cultures in Relation With Callose Biosynthesis.. Frontiers in Plant Science, 9, Article ID 1681.
Open this publication in new window or tab >>Proteomic Analysis of Plasmodesmata From Populus Cell Suspension Cultures in Relation With Callose Biosynthesis.
Show others...
2018 (English)In: Frontiers in Plant Science, ISSN 1664-462X, E-ISSN 1664-462X, Vol. 9, article id 1681Article in journal (Refereed) Published
Abstract [en]

Plasmodesmata are channels that link adjacent cells in plant tissues through which molecular exchanges take place. They are involved in multiple processes vital to plant cells, such as responses to hormonal signaling or environmental challenges including osmotic stress, wounding and pathogen attack. Despite the importance of plasmodesmata, their proteome is not well-defined. Here, we have isolated fractions enriched in plasmodesmata from cell suspension cultures of Populus trichocarpa and identified 201 proteins that are enriched in these fractions, thereby providing further insight on the multiple functions of plasmodesmata. Proteomics analysis revealed an enrichment of proteins specifically involved in responses to stress, transport, metabolism and signal transduction. Consistent with the role of callose deposition and turnover in the closure and aperture of the plasmodesmata and our proteomic analysis, we demonstrate the enrichment of callose synthase activity in the plasmodesmata represented by several gene products. A new form of calcium-independent callose synthase activity was detected, in addition to the typical calcium-dependent enzyme activity, suggesting a role of calcium in the regulation of plasmodesmata through two forms of callose synthase activities. Our report provides the first proteomic investigation of the plasmodesmata from a tree species and the direct biochemical evidence for the occurrence of several forms of active callose synthases in these structures. Data are available via ProteomeXchange with identifier PXD010692.

Keywords
Populus, callose, callose synthase, mass spectrometry, plasmodesmata, spectral counting
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-240964 (URN)10.3389/fpls.2018.01681 (DOI)000450425100001 ()30510561 (PubMedID)2-s2.0-85058796619 (Scopus ID)
Note

QC 20190107

Available from: 2019-01-07 Created: 2019-01-07 Last updated: 2019-05-08Bibliographically approved
Srivastava, V., Rezinciuc, S. & Bulone, V. (2018). Quantitative proteomic analysis of four developmental stages of Saprolegnia parasitica. Frontiers in Microbiology, 8(Jan), Article ID 2658.
Open this publication in new window or tab >>Quantitative proteomic analysis of four developmental stages of Saprolegnia parasitica
2018 (English)In: Frontiers in Microbiology, ISSN 1664-302X, E-ISSN 1664-302X, Vol. 8, no Jan, article id 2658Article in journal (Refereed) Published
Abstract [en]

Several water mold species from the Saprolegnia genus infect fish, amphibians, and crustaceans in natural ecosystems and aquaculture farms. Saprolegnia parasitica is one of the most severe fish pathogens. It is responsible for millions of dollars of losses to the aquaculture industry worldwide. Here, we have performed a proteomic analysis, using gel-based and solution (iTRAQ) approaches, of four defined developmental stages of S. parasitica grown in vitro, i.e., the mycelium, primary cysts, secondary cysts and germinated cysts, to gain greater insight into the types of proteins linked to the different stages. A relatively high number of kinases as well as virulence proteins, including the ricin B lectin, disintegrins, and proteases were identified in the S. parasitica proteome. Many proteins associated with various biological processes were significantly enriched in different life cycle stages of S. parasitica. Compared to the mycelium, most of the proteins in the different cyst stages showed similar enrichment patterns and were mainly related to energy metabolism, signal transduction, protein synthesis, and post-translational modifications. The proteins most enriched in the mycelium compared to the cyst stages were associated with amino acid metabolism, carbohydrate metabolism, and mitochondrial energy production. The data presented expand our knowledge of metabolic pathways specifically linked to each developmental stage of this pathogen.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2018
Keywords
Cysts, Fish, Mycelium, Pathogen, Quantitative proteomics, Saprolegnia
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-221748 (URN)10.3389/fmicb.2017.02658 (DOI)000419783400001 ()2-s2.0-85040514056 (Scopus ID)
Funder
Swedish Research Council Formas, 2013-1427
Note

QC 20180124

Available from: 2018-01-24 Created: 2018-01-24 Last updated: 2018-01-29Bibliographically approved
Kootala, S., Filho, L., Srivastava, V., Linderberg, V., Moussa, A., David, L., . . . Crouzier, T. (2018). Reinforcing Mucus Barrier Properties with Low Molar Mass Chitosans. Biomacromolecules, 19(3), 872-882
Open this publication in new window or tab >>Reinforcing Mucus Barrier Properties with Low Molar Mass Chitosans
Show others...
2018 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 19, no 3, p. 872-882Article in journal (Refereed) Published
Abstract [en]

The mucus gel covers the wet epithelia that forms the inner lining of the body. It constitutes our first line of defense protecting the body from infections and other deleterious molecules. Failure of the mucus barrier can lead to the inflammation of the mucosa such as in inflammatory bowel diseases. Unfortunately, there are no effective strategies that reinforce the mucus barrier properties to recover or enhance its ability to protect the epithelium. Herein, we describe a mucus engineering approach that addresses this issue where we physically cross-link the mucus gel with low molar mass chitosan variants to reinforce its barrier functions. We tested the effect of these chitosans on mucus using in-lab purified porcine gastric mucins, which mimic the native properties of mucus, and on mucus-secreting HT29-MTX epithelial cell cultures. We found that the lowest molar mass chitosan variant (degree of polymerization of 8) diffuses deep into the mucus gels while physically cross-linking the mucin polymers, whereas the higher molar mass chitosan variants (degree of polymerization of 52 and 100) interact only superficially. The complexation resulted in a tighter mucin polymer mesh that slowed the diffusion of dextran polymers and of the cholera toxin B subunit protein through the mucus gels. These results uncover a new use for low molar mass mucoadhesive polymers such as chitosans as noncytotoxic mucosal barrier enhancers that could be valuable in the prevention and treatment of mucosal diseases.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018
National Category
Polymer Chemistry
Identifiers
urn:nbn:se:kth:diva-224590 (URN)10.1021/acs.biomac.7b01670 (DOI)000427539600017 ()29451983 (PubMedID)2-s2.0-85043581772 (Scopus ID)
Funder
Swedish Research Council, 2014-6203
Note

QC 20180320

Available from: 2018-03-20 Created: 2018-03-20 Last updated: 2018-04-05Bibliographically approved
Dahlin, P., Srivastava, V., Ekengren, S., McKee, L. S. & Bulone, V. (2017). Comparative analysis of sterol acquisition in the oomycetes Saprolegnia parasitica and Phytophthora infestans. PLoS ONE, 12(2), Article ID e0170873.
Open this publication in new window or tab >>Comparative analysis of sterol acquisition in the oomycetes Saprolegnia parasitica and Phytophthora infestans
Show others...
2017 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 12, no 2, article id e0170873Article in journal (Refereed) Published
Abstract [en]

The oomycete class includes pathogens of animals and plants which are responsible for some of the most significant global losses in agriculture and aquaculture. There is a need to replace traditional chemical means of controlling oomycete growth with more targeted approaches, and the inhibition of sterol synthesis is one promising area. To better direct these efforts, we have studied sterol acquisition in two model organisms: the sterol-autotrophic Saprolegnia parasitica, and the sterol-heterotrophic Phytophthora infestans. We first present a comprehensive reconstruction of a likely sterol synthesis pathway for S. parasitica, causative agent of the disease saprolegniasis in fish. This pathway shows multiple potential routes of sterol synthesis, and draws on several avenues of new evidence: bioinformatic mining for genes with sterol-related functions, expression analysis of these genes, and analysis of the sterol profiles in mycelium grown in different media. Additionally, we explore the extent to which P. infestans, which causes the late blight in potato, can modify exogenously provided sterols. We consider whether the two very different approaches to sterol acquisition taken by these pathogens represent any specific survival advantages or potential drug targets.

Place, publisher, year, edition, pages
PUBLIC LIBRARY SCIENCE, 2017
National Category
Biological Sciences
Identifiers
urn:nbn:se:kth:diva-204090 (URN)10.1371/journal.pone.0170873 (DOI)000396161200053 ()2-s2.0-85011382600 (Scopus ID)
Note

QC 20170329

Available from: 2017-03-29 Created: 2017-03-29 Last updated: 2017-11-29Bibliographically approved
Kaesdorf, B. T., Weber, F., Petrou, G., Srivastava, V., Crouzier, T. & Lieleg, O. (2017). Mucin-Inspired Lubrication on Hydrophobic Surfaces. Biomacromolecules, 18(8), 2454-2462
Open this publication in new window or tab >>Mucin-Inspired Lubrication on Hydrophobic Surfaces
Show others...
2017 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 18, no 8, p. 2454-2462Article in journal (Refereed) Published
Abstract [en]

In the human body, high-molecular-weight glycoproteins called mucins play a key role in protecting epithelial surfaces against pathogenic attack, controlling the passage of molecules toward the tissue and enabling boundary lubrication with very low friction coefficients. However, neither the molecular mechanisms nor the chemical motifs of those biomacromolecules involved in these fundamental processes are fully understood. Thus, identifying the key features that render biomacromolecules such as mucins outstanding boundary lubricants could set the stage for creating versatile artificial superlubricants. We here demonstrate the importance of the hydrophobic terminal peptide domains of porcine gastric mucin (MUCSAC) and human salivary mucin (MUCSB) in the processes of adsorbing to and lubricating a hydrophobic PDMS surface. Tryptic digestion of those mucins results in removal of those terminal domains, which is accompanied by a loss of lubricity as well as surface adsorption. We show that this loss can in part be compensated by attaching hydrophobic phenyl groups to the glycosylated central part of the mucin macromolecule. Furthermore, we demonstrate that the simple biopolysaccharide dextran can be functionalized with hydrophobic groups which confers efficient surface adsorption and good lubricity on PDMS to the polysaccharide.

Place, publisher, year, edition, pages
AMER CHEMICAL SOC, 2017
National Category
Biological Sciences
Identifiers
urn:nbn:se:kth:diva-214344 (URN)10.1021/acs.biomac.7b00605 (DOI)000407869400024 ()28635258 (PubMedID)2-s2.0-85027351851 (Scopus ID)
Note

QC 20170912

Available from: 2017-09-12 Created: 2017-09-12 Last updated: 2019-04-13Bibliographically approved
Bygdell, J., Srivastava, V., Obudulu, O., Srivastava, M. K., Nilsson, R., Sundberg, B., . . . Wingsle, G. (2017). Protein expression in tension wood formation monitored at high tissue resolution in Populus. Journal of Experimental Botany, 68(13), 3405-3417
Open this publication in new window or tab >>Protein expression in tension wood formation monitored at high tissue resolution in Populus
Show others...
2017 (English)In: Journal of Experimental Botany, ISSN 0022-0957, E-ISSN 1460-2431, Vol. 68, no 13, p. 3405-3417Article in journal (Refereed) Published
Abstract [en]

Tension wood (TW) is a specialized tissue with contractile properties that is formed by the vascular cambium in response to gravitational stimuli. We quantitatively analysed the proteomes of Populus tremula cambium and its xylem cell derivatives in stems forming normal wood (NW) and TW to reveal the mechanisms underlying TW formation. Phloem-, cambium-, and wood-forming tissues were sampled by tangential cryosectioning and pooled into nine independent samples. The proteomes of TW and NW samples were similar in the phloem and cambium samples, but diverged early during xylogenesis, demonstrating that reprogramming is an integral part of TW formation. For example, 14-3-3, reactive oxygen species, ribosomal and ATPase complex proteins were found to be up-regulated at early stages of xylem differentiation during TW formation. At later stages of xylem differentiation, proteins involved in the biosynthesis of cellulose and enzymes involved in the biosynthesis of rhamnogalacturonan-I, rhamnogalacturonan-II, arabinogalactan-II and fasciclin-like arabinogalactan proteins were up-regulated in TW. Surprisingly, two isoforms of exostosin family proteins with putative xylan xylosyl transferase function and several lignin biosynthesis proteins were also up-regulated, even though xylan and lignin are known to be less abundant in TW than in NW. These data provided new insight into the processes behind TW formation.

Place, publisher, year, edition, pages
OXFORD UNIV PRESS, 2017
Keywords
cell wall, cellulose, lignin, Populus, proteomics, tension wood, tissue resolution, xylogenesis
National Category
Plant Biotechnology
Identifiers
urn:nbn:se:kth:diva-213814 (URN)10.1093/jxb/erx186 (DOI)000408119100011 ()2-s2.0-85042463642 (Scopus ID)
Note

QC 20170911

Available from: 2017-09-11 Created: 2017-09-11 Last updated: 2017-09-12Bibliographically approved
Dimitroff, G., Little, A., Lahnstein, J., Schwerdt, J. G., Srivastava, V., Bulone, V., . . . Fincher, G. B. (2016). (1,3;1,4)-beta-Glucan Biosynthesis by the CSLF6 Enzyme: Position and Flexibility of Catalytic Residues Influence Product Fine Structure. Biochemistry, 55(13), 2054-2061
Open this publication in new window or tab >>(1,3;1,4)-beta-Glucan Biosynthesis by the CSLF6 Enzyme: Position and Flexibility of Catalytic Residues Influence Product Fine Structure
Show others...
2016 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 55, no 13, p. 2054-2061Article in journal (Refereed) Published
Abstract [en]

Cellulose synthase-like F6 (CslF6) genes encode polysaccharide synthases responsible for (1,3;1,4)-beta-glucan biosynthesis in cereal grains. However, it is not clear how both (1,3)- and (1,4) -linkages are incorporated into a single polysaccharide chain and how the frequency and arrangement of the two linkage types that define the fine structure of the polysaccharide are controlled. Through transient expression in Nicotiana benthamiana leaves, two CSLF6 orthologs from different cereal species were shown to mediate the synthesis of (1,3;1,4)-beta-glucans with very different fine structures. Chimeric cDNA constructs with interchanged sections of the barley and sorghum CslF6 genes were developed to identify regions of the synthase enzyme responsible for these differences. A single amino acid residue upstream of the TED motif in the catalytic region was shown to dramatically change the fine structure of the polysaccharide produced. The structural basis of this effect can be rationalized by reference to a homology model of the enzyme and appears to be related to the position and flexibility of the TED motif in the active site of the enzyme. The region and amino acid residue identified provide opportunities to manipulate the solubility of (1,3;1,4)-beta-glucan in grains and vegetative tissues of the grasses and, in particular, to enhance the solubility of dietary fibers that are beneficial to human health.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2016
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-185978 (URN)10.1021/acs.biochem.5b01384 (DOI)000373656200012 ()26967377 (PubMedID)2-s2.0-84964344179 (Scopus ID)
Note

QC 20160509

Available from: 2016-05-09 Created: 2016-04-29 Last updated: 2017-11-30Bibliographically approved
Ford, K. L., Chin, T., Srivastava, V., Zeng, W., Doblin, M. S., Bulone, V. & Bacic, A. (2016). Comparative "Golgi" Proteome Study of Lolium multiflorum and Populus trichocarpa. PROTEOMES, 4(3), Article ID 23.
Open this publication in new window or tab >>Comparative "Golgi" Proteome Study of Lolium multiflorum and Populus trichocarpa
Show others...
2016 (English)In: PROTEOMES, ISSN 2227-7382, Vol. 4, no 3, article id 23Article in journal (Refereed) Published
Abstract [en]

The Golgi apparatus (GA) is a crucial organelle in the biosynthesis of non-cellulosic polysaccharides, glycoproteins and proteoglycans that are primarily destined for secretion to the cell surface (plasma membrane, cell wall and apoplast). Only a small proportion of the proteins involved in these processes have been identified in plants, with the majority of their functions still unknown. The availability of a GA proteome would greatly assist plant biochemists, cell and molecular biologists in determining the precise function of the cell wall-related proteins. There has been some progress towards defining the GA proteome in the model plant system Arabidopsis thaliana, yet in commercially important species, such as either the cereals or woody species there has been relatively less progress. In this study, we applied discontinuous sucrose gradient centrifugation to partially enrich GA from suspension cell cultures (SCCs) and combined this with stable isotope labelling (iTRAQ) to determine protein sub-cellular locations. Results from a representative grass species, Italian ryegrass (Lolium multiflorum) and a dicot species, black cottonwood (Populus trichocarpa) are compared. The results confirm that membrane fractionation approaches that provide effective GA-enriched fractions for proteomic analyses in Arabidopsis are much less effective in the species examined here and highlight the complexity of the GA, both within and between species.

Place, publisher, year, edition, pages
MDPI AG, 2016
Keywords
Golgi apparatus, sub-cellular fractionation, subcellular proteomics, quantitative proteomics
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-196440 (URN)10.3390/proteomes4030023 (DOI)000385569300004 ()
Note

QC 20161129

Available from: 2016-11-29 Created: 2016-11-14 Last updated: 2016-11-29Bibliographically approved
Pang, Z., Srivastava, V., Liu, X. & Bulone, V. (2016). Quantitative proteomics links metabolic pathways to specific developmental stages of the plant-pathogenic oomycete Phytophthora capsici. Molecular plant pathology
Open this publication in new window or tab >>Quantitative proteomics links metabolic pathways to specific developmental stages of the plant-pathogenic oomycete Phytophthora capsici
2016 (English)In: Molecular plant pathology, ISSN 1464-6722, E-ISSN 1364-3703Article in journal (Refereed) Published
Abstract [en]

The oomycete Phytophthora capsici is a plant pathogen responsible for important losses to vegetable production worldwide. Its asexual reproduction plays an important role in the rapid propagation and spread of the disease in the field. A global proteomics study was conducted to compare two key asexual life stages of P. capsici, i.e. the mycelium and cysts, to identify stage-specific biochemical processes. A total of 1200 proteins was identified using qualitative and quantitative proteomics. The transcript abundance of some of the enriched proteins was also analysed by quantitative real-time polymerase chain reaction. Seventy-three proteins exhibited different levels of abundance between the mycelium and cysts. The proteins enriched in the mycelium are mainly associated with glycolysis, the tricarboxylic acid (or citric acid) cycle and the pentose phosphate pathway, providing the energy required for the biosynthesis of cellular building blocks and hyphal growth. In contrast, the proteins that are predominant in cysts are essentially involved in fatty acid degradation, suggesting that the early infection stage of the pathogen relies primarily on fatty acid degradation for energy production. The data provide a better understanding of P. capsici biology and suggest potential metabolic targets at the two different developmental stages for disease control. © 2016 BSPP AND JOHN WILEY & SONS LTD.

Place, publisher, year, edition, pages
John Wiley & Sons, 2016
Keywords
Cysts, Mass spectrometry, Mycelium, Phytophthora capsici, Plant-pathogenic oomycete, Quantitative proteomics
National Category
Biological Sciences
Identifiers
urn:nbn:se:kth:diva-194591 (URN)10.1111/mpp.12406 (DOI)000395552000005 ()2-s2.0-84971393355 (Scopus ID)
Note

Correspondence Address: Bulone, V.email: bulone@kth.se. QC 20161102

Available from: 2016-11-02 Created: 2016-10-31 Last updated: 2017-04-28Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0003-1877-4154

Search in DiVA

Show all publications