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Lundqvist, M., Thalén, N., Volk, A.-L., Hansen, H. G., von Otter, E., Nygren, P.-Å., . . . Rockberg, J. (2019). Chromophore pre-maturation for improved speed and sensitivity of split-GFP monitoring of protein secretion. Scientific Reports, 9, Article ID 310.
Open this publication in new window or tab >>Chromophore pre-maturation for improved speed and sensitivity of split-GFP monitoring of protein secretion
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2019 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 9, article id 310Article in journal (Refereed) Published
Abstract [en]

Complementation-dependent fluorescence is a powerful way to study co-localization or interactions between biomolecules. A split-GFP variant, involving the self-associating GFP 1-10 and GFP 11, has previously provided a convenient approach to measure recombinant protein titers in cell supernatants. A limitation of this approach is the slow chromophore formation after complementation. Here, we alleviate this lag in signal generation by allowing the GFP 1-10 chromophore to mature on a solid support containing GFP 11 before applying GFP 1-10 in analyses. The pre-maturated GFP 1-10 provided up to 150-fold faster signal generation compared to the non-maturated version. Moreover, pre-maturated GFP 1-10 significantly improved the ability of discriminating between Chinese hamster ovary (CHO) cell lines secreting GFP 11-tagged erythropoietin protein at varying rates. Its improved kinetics make the pre-maturated GFP 1-10 a suitable reporter molecule for cell biology research in general, especially for ranking individual cell lines based on secretion rates of recombinant proteins.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP, 2019
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:kth:diva-243949 (URN)10.1038/s41598-018-36559-x (DOI)000456282100065 ()30670736 (PubMedID)2-s2.0-85060382656 (Scopus ID)
Note

QC 20190305

Available from: 2019-03-05 Created: 2019-03-05 Last updated: 2019-03-05Bibliographically approved
Lundgren, S., Fagerström-Vahman, H., Zhang, C., Ben-Dror, L., Mardinoglu, A., Uhlén, M., . . . Jirström, K. (2019). Discovery of KIRREL as a biomarker for prognostic stratification of patients with thin melanoma. Biomarker Research, 7, Article ID 1.
Open this publication in new window or tab >>Discovery of KIRREL as a biomarker for prognostic stratification of patients with thin melanoma
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2019 (English)In: Biomarker Research, ISSN 2050-7771, Vol. 7, article id 1Article in journal (Refereed) Published
Abstract [en]

There is a great unmet clinical need to identify patients with thin primary cutaneous melanomas (T1, Breslow thickness1mm) who have a high risk for tumour recurrence and death from melanoma. Kin of IRRE-like protein 1 (KIRREL/NEPH1) is expressed in podocytes and involved in glomerular filtration. Screening in the Human Protein Atlas portal revealed a particularly high expression of KIRREL in melanoma, both at the mRNA and protein levels. In this study, we followed up on these findings and examined the prognostic value of KIRREL in a population-based cohort.Immunohistochemical expression of KIRREL was examined in tissue microarrays with a subset of primary tumours and paired lymph node metastases from an original cohort of 268 incident cases of melanoma in the Malmo Diet and Cancer study. KIRREL mRNA expression was examined in 103 melanoma cases in The Cancer Genome Atlas (TCGA).Membranous/cytoplasmic expression of KIRREL was detected in 158/185 (85.4%) primary tumours and 18/19 (94.7%) metastases. High expression of KIRREL was significantly associated with several unfavourable clinicopathological factors.High KIRREL protein expression was an independent factor of reduced recurrence free and melanoma specific survival, particularly in thin melanomas, even outperforming absolute thickness and ulceration (HR=30.85; 95% CI 1.54-616.36 and HR=6.32 95% CI 1.19-33.65). High mRNA levels of KIRREL were not significantly associated with survival in TCGA.In conclusion, KIRREL is not only a novel potential diagnostic marker for melanoma, but may also be a useful prognostic biomarker for improved stratification of patients with thin melanoma. These findings may be of high clinical relevance and therefore merit further validation.

Place, publisher, year, edition, pages
BioMed Central, 2019
Keywords
Melanoma, KIRREL, NEPH1, Prognosis
National Category
Cancer and Oncology
Identifiers
urn:nbn:se:kth:diva-242974 (URN)10.1186/s40364-018-0153-8 (DOI)000455575200001 ()30675360 (PubMedID)
Funder
Swedish Research CouncilScience for Life Laboratory - a national resource center for high-throughput molecular bioscience
Note

QC 20190204

Available from: 2019-02-04 Created: 2019-02-04 Last updated: 2019-03-01Bibliographically approved
Liu, Z., Zhang, C., Lee, S., $$$Kim, W., Klevstig, M., $$$Harzandi, A. M., . . . Mardinoglu, A. (2019). Pyruvate kinase L/R is a regulator of lipid metabolism and mitochondrial function. Metabolic engineering, 52, 263-272
Open this publication in new window or tab >>Pyruvate kinase L/R is a regulator of lipid metabolism and mitochondrial function
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2019 (English)In: Metabolic engineering, ISSN 1096-7176, E-ISSN 1096-7184, Vol. 52, p. 263-272Article in journal (Refereed) Published
Abstract [en]

The pathogenesis of non-alcoholic fatty liver disease (NAFLD) and hepatocellular carcinoma (HCC) has been associated with altered expression of liver-specific genes including pyruvate kinase liver and red blood cell (PKLR), patatin-like phospholipase domain containing 3 (PNPLA3) and proprotein convertase subtilisin/kexin type 9 (PCSK9). Here, we inhibited and overexpressed the expression of these three genes in HepG2 cells, generated RNA-seq data before and after perturbation and revealed the altered global biological functions with the modulation of these genes using integrated network (IN) analysis. We found that modulation of these genes effects the total triglycerides levels within the cells and viability of the cells. Next, we generated IN for HepG2 cells, identified reporter transcription factors based on IN and found that the modulation of these genes affects key metabolic pathways associated with lipid metabolism (steroid biosynthesis, PPAR signalling pathway, fatty acid synthesis and oxidation) and cancer development (DNA replication, cell cycle and p53 signalling) involved in the progression of NAFLD and HCC. Finally, we observed that inhibition of PKLR lead to decreased glucose uptake and decreased mitochondrial activity in HepG2 cells. Hence, our systems level analysis indicated that PKLR can be targeted for development efficient treatment strategy for NAFLD and HCC.

Place, publisher, year, edition, pages
ACADEMIC PRESS INC ELSEVIER SCIENCE, 2019
National Category
Cell Biology
Identifiers
urn:nbn:se:kth:diva-244499 (URN)10.1016/j.ymben.2019.01.001 (DOI)000457633200024 ()30615941 (PubMedID)2-s2.0-85059704001 (Scopus ID)
Note

QC 20190321

Available from: 2019-03-21 Created: 2019-03-21 Last updated: 2019-03-21Bibliographically approved
Dusart, P., Fagerberg, L., Perisic, L., Civelek, M., Struck, E., Hedin, U., . . . Butler, L. . (2018). A systems-approach reveals human nestin is an endothelial-enriched, angiogenesis-independent intermediate filament protein. Scientific Reports, 8(1), Article ID 14668.
Open this publication in new window or tab >>A systems-approach reveals human nestin is an endothelial-enriched, angiogenesis-independent intermediate filament protein
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2018 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 8, no 1, article id 14668Article in journal (Refereed) Published
Abstract [en]

The intermediate filament protein nestin is expressed during embryonic development, but considered largely restricted to areas of regeneration in the adult. Here, we perform a body-wide transcriptome and protein-profiling analysis to reveal that nestin is constitutively, and highly-selectively, expressed in adult human endothelial cells (EC), independent of proliferative status. Correspondingly, we demonstrate that it is not a marker for tumour EC in multiple malignancy types. Imaging of EC from different vascular beds reveals nestin subcellular distribution is shear-modulated. siRNA inhibition of nestin increases EC proliferation, and nestin expression is reduced in atherosclerotic plaque neovessels. eQTL analysis reveals an association between SNPs linked to cardiovascular disease and reduced aortic EC nestin mRNA expression. Our study challenges the dogma that nestin is a marker of proliferation, and provides insight into its regulation and function in EC. Furthermore, our systems-based approach can be applied to investigate body-wide expression profiles of any candidate protein. 

Place, publisher, year, edition, pages
Nature Publishing Group, 2018
National Category
Biological Sciences
Identifiers
urn:nbn:se:kth:diva-236564 (URN)10.1038/s41598-018-32859-4 (DOI)000446034000069 ()2-s2.0-85054173189 (Scopus ID)
Note

Export Date: 22 October 2018; Article; Correspondence Address: Butler, L.M.; Science for Life Laboratory, School of Biotechnology, Kungliga Tekniska Högskolan (KTH) Royal Institute of TechnologySweden; email: Lynn.Butler@ki.se. QC 20181127

Available from: 2018-11-27 Created: 2018-11-27 Last updated: 2018-11-27Bibliographically approved
Turanli, B., Grotli, M., Boren, J., Nielsen, J., Uhlén, M., Arga, K. Y. & Mardinoglu, A. (2018). Drug Repositioning for Effective Prostate Cancer Treatment. Frontiers in Physiology, 9, Article ID 500.
Open this publication in new window or tab >>Drug Repositioning for Effective Prostate Cancer Treatment
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2018 (English)In: Frontiers in Physiology, ISSN 1664-042X, E-ISSN 1664-042X, Vol. 9, article id 500Article, review/survey (Refereed) Published
Abstract [en]

Drug repositioning has gained attention from both academia and pharmaceutical companies as an auxiliary process to conventional drug discovery. Chemotherapeutic agents have notorious adverse effects that drastically reduce the life quality of cancer patients so drug repositioning is a promising strategy to identify non-cancer drugs which have anti-cancer activity as well as tolerable adverse effects for human health. There are various strategies for discovery and validation of repurposed drugs. In this review, 25 repurposed drug candidates are presented as result of different strategies, 15 of which are already under clinical investigation for treatment of prostate cancer (PCa). To date, zoledronic acid is the only repurposed, clinically used, and approved non-cancer drug for PCa. Anti-cancer activities of existing drugs presented in this review cover diverse and also known mechanisms such as inhibition of mTOR and VEGFR2 signaling, inhibition of PI3K/Akt signaling, COX and selective COX-2 inhibition, NF-kappa B inhibition, Wnt/beta - Catenin pathway inhibition, DNMT1 inhibition, and GSK-3 beta inhibition. In addition to monotherapy option, combination therapy with current anti-cancer drugs may also increase drug efficacy and reduce adverse effects. Thus, drug repositioning may become a key approach for drug discovery in terms of time- and cost-efficiency comparing to conventional drug discovery and development process.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2018
Keywords
prostate cancer, drug repositioning, non-cancer therapeutics, repurposing, approved drugs
National Category
Physiology
Identifiers
urn:nbn:se:kth:diva-229015 (URN)10.3389/fphys.2018.00500 (DOI)000432407100001 ()2-s2.0-85047004631 (Scopus ID)
Funder
Science for Life Laboratory - a national resource center for high-throughput molecular bioscienceKnut and Alice Wallenberg Foundation
Note

QC 20180531

Available from: 2018-05-31 Created: 2018-05-31 Last updated: 2018-05-31Bibliographically approved
Edfors, F., Hober, A., Linderbäck, K., Maddalo, G., Azimi, A., Sivertsson, Å., . . . Uhlén, M. (2018). Enhanced validation of antibodies for research applications. Nature Communications, 9, Article ID 4130.
Open this publication in new window or tab >>Enhanced validation of antibodies for research applications
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2018 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 9, article id 4130Article in journal (Refereed) Published
Abstract [en]

There is a need for standardized validation methods for antibody specificity and selectivity. Recently, five alternative validation pillars were proposed to explore the specificity of research antibodies using methods with no need for prior knowledge about the protein target. Here, we show that these principles can be used in a streamlined manner for enhanced validation of research antibodies in Western blot applications. More than 6,000 antibodies were validated with at least one of these strategies involving orthogonal methods, genetic knockdown, recombinant expression, independent antibodies, and capture mass spectrometry analysis. The results show a path forward for efforts to validate antibodies in an application-specific manner suitable for both providers and users.

Place, publisher, year, edition, pages
Nature Publishing Group, 2018
National Category
Immunology in the medical area
Identifiers
urn:nbn:se:kth:diva-237096 (URN)10.1038/s41467-018-06642-y (DOI)000446566000016 ()30297845 (PubMedID)2-s2.0-85054574300 (Scopus ID)
Funder
Science for Life Laboratory - a national resource center for high-throughput molecular bioscienceKnut and Alice Wallenberg Foundation
Note

QC 20181030

Available from: 2018-10-30 Created: 2018-10-30 Last updated: 2018-10-30Bibliographically approved
Jahn, M., Vialas, V., Karlsen, J., Maddalo, G., Edfors, F., Forsström, B., . . . Hudson, E. P. (2018). Growth of Cyanobacteria Is Constrained by the Abundance of Light and Carbon Assimilation Proteins. Cell reports, 25(2), 478-+
Open this publication in new window or tab >>Growth of Cyanobacteria Is Constrained by the Abundance of Light and Carbon Assimilation Proteins
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2018 (English)In: Cell reports, ISSN 2211-1247, E-ISSN 2211-1247, Vol. 25, no 2, p. 478-+Article in journal (Refereed) Published
Abstract [en]

Cyanobacteria must balance separate demands for energy generation, carbon assimilation, and biomass synthesis. We used shotgun proteomics to investigate proteome allocation strategies in the model cyanobacterium Synechocystis sp. PCC 6803 as it adapted to light and inorganic carbon (C-i) limitation. When partitioning the proteome into seven functional sectors, we find that sector sizes change linearly with growth rate. The sector encompassing ribosomes is significantly smaller than in E. coli, which may explain the lower maximum growth rate in Synechocystis. Limitation of light dramatically affects multiple proteome sectors, whereas the effect of C-i limitation is weak. Carbon assimilation proteins respond more strongly to changes in light intensity than to C-i. A coarse-grained cell economy model generally explains proteome trends. However, deviations from model predictions suggest that the large proteome sectors for carbon and light assimilation are not optimally utilized under some growth conditions and may constrain the proteome space available to ribosomes.

Place, publisher, year, edition, pages
et al., 2018
National Category
Physical Sciences
Identifiers
urn:nbn:se:kth:diva-237095 (URN)10.1016/j.celrep.2018.09.040 (DOI)000446691400020 ()30304686 (PubMedID)2-s2.0-85054193580& (Scopus ID)
Funder
Science for Life Laboratory - a national resource center for high-throughput molecular bioscienceSwedish Research Council Formas, 2015-939Swedish Research CouncilSwedish Foundation for Strategic Research , RBP14-0013
Note

QC 20181029

Available from: 2018-10-29 Created: 2018-10-29 Last updated: 2018-10-29Bibliographically approved
Zieba, A., Ponten, F., Uhlén, M. & Landegren, U. (2018). In situ protein detection with enhanced specificity using DNA-conjugated antibodies and proximity ligation. Modern Pathology, 31(2), 253-263
Open this publication in new window or tab >>In situ protein detection with enhanced specificity using DNA-conjugated antibodies and proximity ligation
2018 (English)In: Modern Pathology, ISSN 0893-3952, E-ISSN 1530-0285, Vol. 31, no 2, p. 253-263Article in journal (Refereed) Published
Abstract [en]

Antibodies are important tools in anatomical pathology and research, but the quality of in situ protein detection by immunohistochemistry greatly depends on the choice of antibodies and the abundance of the targeted proteins. Many antibodies used in scientific research do not meet requirements for specificity and sensitivity. Accordingly, methods that improve antibody performance and produce quantitative data can greatly advance both scientific investigations and clinical diagnostics based on protein expression and in situ localization. We demonstrate here protocols for antibody labeling that allow specific protein detection in tissues via bright-field in situ proximity ligation assays, where each protein molecule must be recognized by two antibodies. We further demonstrate that single polyclonal antibodies or purified serum preparations can be used for these dual recognition assays. The requirement for protein recognition by pairs of antibody conjugates can significantly improve specificity of protein detection over single-binder assays.

Place, publisher, year, edition, pages
Nature Publishing Group, 2018
Keywords
antibody conjugate, APEX 1 protein, calvasculin, DNA conjugated antibody, immunoglobulin G antibody, polyclonal antibody, protein, protein A, protein G, rabbit antiserum, reagent, trefoil factor 1, unclassified drug, animal tissue, antibody affinity, antibody labeling, antibody specificity, Article, assay, click chemistry, controlled study, DNA strand, genetic transcription, immunohistochemistry, in situ proximity ligation assay, limit of detection, mRNA expression level, nonhuman, priority journal, protein analysis, protein expression, protein expression level, protein purification, tissue microarray, tissue section
National Category
Biological Sciences
Identifiers
urn:nbn:se:kth:diva-227448 (URN)10.1038/modpathol.2017.102 (DOI)000424761400003 ()2-s2.0-85041805855 (Scopus ID)
Note

Export Date: 9 May 2018; Article; CODEN: MODPE; Correspondence Address: Landegren, U.; Department of Immunology, Genetics and Pathology, Science for Life Laboratory, BMC, Uppsala University, Husargatan 3, Sweden; email: Ulf.Landegren@igp.uu.se; Funding details: VINNOVA; Funding details: 222635; Funding details: 241481; Funding details: NCI, National Cancer Institute; Funding details: #2008:0143, Knut och Alice Wallenbergs Stiftelse; Funding details: FP5, Fifth Framework Programme; Funding details: FP/2007– 2013, FP7, Seventh Framework Programme; Funding details: ERC, European Research Council; Funding details: TRC, The Research Council; Funding details: 294409, ERC, European Research Council; Funding details: IngaBritt och Arne Lundbergs Forskningsstiftelse; Funding details: Uppsala Universitet; Funding text: This work was supported by the Knut and Alice Wallenberg Foundation (#2008:0143), the European Community's 7th Framework Program (FP7/2007–2013) under grant agreement n° 222635 (AffinityProteome) 241481 (Affinomics), The Swedish Research Council, Swedish Governmental Agency for Innovation Systems, IngaBritt and Arne Lundberg Foundation, the European Research Council under the European Union's Seventh Framework Programme (FP/2007– 2013) / ERC Grant Agreement n. 294409 (ProteinSeq), and Uppsala University. UL holds stock in Olink, having rights to the in situ proximity ligation assay technology. We would also like to thank Tara Hiltke at the National Cancer Institute for providing mAbs for in situ proximity ligation assay experiments. QC 20180528

Available from: 2018-05-28 Created: 2018-05-28 Last updated: 2018-05-28Bibliographically approved
Sjöstedt, E., Sivertsson, Å., Norradin, F. H., Katona, B., Näsström, Å., Vuu, J., . . . Lindskog, C. (2018). Integration of Transcriptomics and Antibody-Based Proteomics for Exploration of Proteins Expressed in Specialized Tissues. Journal of Proteome Research, 17(12), 4127-4137
Open this publication in new window or tab >>Integration of Transcriptomics and Antibody-Based Proteomics for Exploration of Proteins Expressed in Specialized Tissues
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2018 (English)In: Journal of Proteome Research, ISSN 1535-3893, E-ISSN 1535-3907, Vol. 17, no 12, p. 4127-4137Article in journal (Refereed) Published
Abstract [en]

A large portion of human proteins are referred to as missing proteins, defined as protein-coding genes that lack experimental data on the protein level due to factors such as temporal expression, expression in tissues that are difficult to sample, or they actually do not encode functional proteins. In the present investigation, an integrated omics approach was used for identification and exploration of missing proteins. Transcriptomics data from three different sourcesthe Human Protein Atlas (HPA), the GTEx consortium, and the FANTOM5 consortiumwere used as a starting point to identify genes selectively expressed in specialized tissues. Complementing the analysis with profiling on more specific tissues based on immunohistochemistry allowed for further exploration of cell-type-specific expression patterns. More detailed tissue profiling was performed for >300 genes on complementing tissues. The analysis identified tissue-specific expression of nine proteins previously listed as missing proteins (POU4F1, FRMD1, ARHGEF33, GABRG1, KRTAP2-1, BHLHE22, SPRR4, AVPR1B, and DCLK3), as well as numerous proteins with evidence of existence on the protein level that previously lacked information on spatial resolution and cell-type- specific expression pattern. We here present a comprehensive strategy for identification of missing proteins by combining transcriptomics with antibody-based proteomics. The analyzed proteins provide interesting targets for organ-specific research in health and disease.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018
Keywords
missing proteins, transcriptomics, proteomics, protein localization, immunohistochemistry, antibodies, tissue profiling
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) Biological Sciences
Research subject
Biotechnology
Identifiers
urn:nbn:se:kth:diva-236474 (URN)10.1021/acs.jproteome.8b00406 (DOI)000452930000010 ()30272454 (PubMedID)2-s2.0-85055105364 (Scopus ID)
Note

QC 20181018

Available from: 2018-10-17 Created: 2018-10-17 Last updated: 2019-01-11Bibliographically approved
Reuterswärd, P., Bergström, S., Orikiiriza, J., Lindquist, E., Bergström, S., Svahn Andersson, H., . . . Nilsson, P. (2018). Levels of human proteins in plasma associated with acute paediatric malaria. Malaria Journal, 17, Article ID 426.
Open this publication in new window or tab >>Levels of human proteins in plasma associated with acute paediatric malaria
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2018 (English)In: Malaria Journal, ISSN 1475-2875, E-ISSN 1475-2875, Vol. 17, article id 426Article in journal (Refereed) Published
Abstract [en]

Background: The intimate interaction between the pathophysiology of the human host and the biology of the Plasmodium falciparum parasite results in a wide spectrum of disease outcomes in malaria. Development of severe disease is associated with a progressively augmented imbalance in pro- and anti-inflammatory responses to high parasite loads and sequestration of parasitized erythrocytes. Although these phenomena collectively constitute common denominators for the wide variety of discrete severe malaria manifestations, the mechanistic rationales behind discrepancies in outcome are poorly understood. Exploration of the human pathophysiological response by variations in protein profiles in plasma presents an excellent opportunity to increase the understanding. This is ultimately required for better prediction, prevention and treatment of malaria, which is essential for ongoing elimination and eradication efforts. Results: An affinity proteomics approach was used to analyse 541 paediatric plasma samples collected from community controls and patients with mild or severe malaria in Rwanda. Protein profiles were generated with an antibody-based suspension bead array containing 255 antibodies targetting 115 human proteins. Here, 57 proteins were identified with significantly altered levels (adjusted p-values<0.001) in patients with malaria compared to controls. From these, the 27 most significant proteins (adjusted p-values<10(-14)) were selected for a stringent analysis approach. Here, 24 proteins showed elevated levels in malaria patients and included proteins involved in acute inflammatory response as well as cell adhesion. The remaining three proteins, also implicated in immune regulation and cellular adhesivity, displayed lower abundance in malaria patients. In addition, 37 proteins (adjusted p-values<0.05) were identified with increased levels in patients with severe compared to mild malaria. This set includes, proteins involved in tissue remodelling and erythrocyte membrane proteins. Collectively, this approach has been successfully used to identify proteins both with known and unknown association with different stages of malaria. Conclusion: In this study, a high-throughput affinity proteomics approach was used to find protein profiles in plasma linked to P. falciparum infection and malaria disease progression. The proteins presented herein are mainly involved in inflammatory response, cellular adhesion and as constituents of erythrocyte membrane. These findings have a great potential to provide increased conceptual understanding of host-parasite interaction and malaria pathogenesis.

Place, publisher, year, edition, pages
BMC, 2018
Keywords
Affinity proteomics, Human plasma profiling, Malaria, Plasmodium falciparum, suspension bead arrays, Sequestration, Cytoadhesion
National Category
Medical Biotechnology
Identifiers
urn:nbn:se:kth:diva-239769 (URN)10.1186/s12936-018-2576-y (DOI)000450509700002 ()30442134 (PubMedID)2-s2.0-85056636195 (Scopus ID)
Note

QC 20190109

Available from: 2019-01-09 Created: 2019-01-09 Last updated: 2019-01-09Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0001-8993-048X

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