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Bonde, Mari
Publications (10 of 20) Show all publications
Tükenmez, H., Singh, P., Sarkar, S., Çakır, M., Oliveira, A. H., Lindgren, C., . . . Johansson, J. (2023). A highly substituted ring-fused 2-pyridone compound targeting PrfA and the efflux regulator BrtA in listeria monocytogenes [Letter to the editor]. mBio, 14(3), Article ID e0044923.
Open this publication in new window or tab >>A highly substituted ring-fused 2-pyridone compound targeting PrfA and the efflux regulator BrtA in listeria monocytogenes
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2023 (English)In: mBio, ISSN 2161-2129, E-ISSN 2150-7511, Vol. 14, no 3, article id e0044923Article in journal, Letter (Refereed) Published
Abstract [en]

Listeria monocytogenes is a facultative Gram-positive bacterium that causes listeriosis, a severe foodborne disease. We previously discovered that ring-fused 2-pyridone compounds can decrease virulence factor expression in Listeria by binding and inactivating the PrfA virulence activator. In this study, we tested PS900, a highly substituted 2-pyridone that was recently discovered to be bactericidal to other Gram-positive pathogenic bacteria, such as Staphylococcus aureus and Enterococcus faecalis. We show that PS900 can interact with PrfA and reduce the expression of virulence factors. Unlike previous ring-fused 2-pyridones shown to inactivate PrfA, PS900 had an additional antibacterial activity and was found to potentiate sensitivity toward cholic acid. Two PS900-tolerant mutants able to grow in the presence of PS900 carried mutations in the brtA gene, encoding the BrtA repressor. In wild-type (WT) bacteria, cholic acid binds and inactivates BrtA, thereby alleviating the expression of the multidrug transporter MdrT. Interestingly, we found that PS900 also binds to BrtA and that this interaction causes BrtA to dissociate from its binding site in front of the mdrT gene. In addition, we observed that PS900 potentiated the effect of different osmolytes. We suggest that the increased potency of cholic acid and osmolytes to kill bacteria in the presence of PS900 is due to the ability of the latter to inhibit general efflux, through a yet-unknown mechanism. Our data indicate that thiazolino 2-pyridones constitute an attractive scaffold when designing new types of antibacterial agents.

IMPORTANCE: Bacteria resistant to one or several antibiotics are a very large problem, threatening not only treatment of infections but also surgery and cancer treatments. Thus, new types of antibacterial drugs are desperately needed. In this work, we show that a new generation of substituted ring-fused 2-pyridones not only inhibit Listeria monocytogenes virulence gene expression, presumably by inactivating the PrfA virulence regulator, but also potentiate the bactericidal effects of cholic acid and different osmolytes. We identified a multidrug repressor as a second target of 2-pyridones. The repressor–2-pyridone interaction displaces the repressor from DNA, thus increasing the expression of a multidrug transporter. In addition, our data suggest that the new class of ring-fused 2-pyridones are efficient efflux inhibitors, possibly explaining why the simultaneous addition of 2-pyridones together with cholic acid or osmolytes is detrimental for the bacterium. This work proves conclusively that 2-pyridones constitute a promising scaffold to build on for future antibacterial drug design.

Place, publisher, year, edition, pages
American Society for Microbiology, 2023
Keywords
2-pyridones, BrtA, Listeria monocytogenes, PrfA, antibacterial, antibiotic
National Category
Biochemistry and Molecular Biology Microbiology in the medical area Organic Chemistry
Research subject
molecular cell biology
Identifiers
urn:nbn:se:umu:diva-214132 (URN)10.1128/mbio.00449-23 (DOI)000975886700001 ()37120759 (PubMedID)2-s2.0-85172894238 (Scopus ID)
Funder
Familjen Erling-Perssons StiftelseNIH (National Institutes of Health), RO1AI134847-01A1NIH (National Institutes of Health), 1IU19AI157797-01Olle Engkvists stiftelseVinnova, 2019-05491Swedish Research Council, 2020-02005Swedish Research Council, 2018-04589Swedish Research Council, 202105040J
Available from: 2023-09-05 Created: 2023-09-05 Last updated: 2023-10-13Bibliographically approved
Hainzl, T., Bonde, M., Almqvist, F., Johansson, J. & Sauer-Eriksson, A. E. (2023). Structural insights into CodY activation and DNA recognition [Letter to the editor]. Nucleic Acids Research, 51(14), 7631-7648
Open this publication in new window or tab >>Structural insights into CodY activation and DNA recognition
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2023 (English)In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 51, no 14, p. 7631-7648Article in journal, Letter (Refereed) Published
Abstract [en]

Virulence factors enable pathogenic bacteria to infect host cells, establish infection, and contribute to disease progressions. In Gram-positive pathogens such as Staphylococcus aureus (Sa) and Enterococcus faecalis (Ef), the pleiotropic transcription factor CodY plays a key role in integrating metabolism and virulence factor expression. However, to date, the structural mechanisms of CodY activation and DNA recognition are not understood. Here, we report the crystal structures of CodY from Sa and Ef in their ligand-free form and their ligand-bound form complexed with DNA. Binding of the ligands - branched chain amino acids and GTP - induces conformational changes in the form of helical shifts that propagate to the homodimer interface and reorient the linker helices and DNA binding domains. DNA binding is mediated by a non-canonical recognition mechanism dictated by DNA shape readout. Furthermore, two CodY dimers bind to two overlapping binding sites in a highly cooperative manner facilitated by cross-dimer interactions and minor groove deformation. Our structural and biochemical data explain how CodY can bind a wide range of substrates, a hallmark of many pleiotropic transcription factors. These data contribute to a better understanding of the mechanisms underlying virulence activation in important human pathogens.

Place, publisher, year, edition, pages
Oxford University Press, 2023
Keywords
CodY, virulence, protein-DNA complex structure
National Category
Biochemistry and Molecular Biology Bioinformatics and Systems Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-214131 (URN)10.1093/nar/gkad512 (DOI)001008706900001 ()2-s2.0-85168963845 (Scopus ID)
Projects
CodY
Funder
Swedish Research Council, ID 2019-03771Swedish Research Council, 2020-02005_3 toSwedish Research Council, 2018-04589Swedish Research Council, 2021-05040J
Available from: 2023-09-05 Created: 2023-09-05 Last updated: 2023-09-05Bibliographically approved
Tükenmez, H., Nye, T. M., Bonde, M., Caparon, M. G., Almqvist, F., Hultgren, S. J. & Johansson, J. (2022). Complete Genome Sequence of the Uropathogenic Methicillin-Resistant Staphylococcus aureus Strain MRSA-1369. Microbiology Resource Announcements, 11(10)
Open this publication in new window or tab >>Complete Genome Sequence of the Uropathogenic Methicillin-Resistant Staphylococcus aureus Strain MRSA-1369
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2022 (English)In: Microbiology Resource Announcements, E-ISSN 2576-098X, Vol. 11, no 10Article in journal (Refereed) Published
Abstract [en]

MRSA-1369 is a uropathogenic methicillin-resistant Staphylococcus aureus (MRSA) strain. Here, we present the complete genome sequence of MRSA-1369, which consists of one chromosome (2.87 Mb) and two plasmids (16.68 kb and 3.13 kb). This will serve as a reference genome for future Staphylococcus aureus pathogenesis and multiomic studies.

Place, publisher, year, edition, pages
American Society for Microbiology, 2022
National Category
Microbiology in the medical area Infectious Medicine
Identifiers
urn:nbn:se:umu:diva-200828 (URN)10.1128/mra.00981-22 (DOI)000868643800002 ()36173194 (PubMedID)2-s2.0-85140455359 (Scopus ID)
Available from: 2022-11-14 Created: 2022-11-14 Last updated: 2023-03-24Bibliographically approved
Curtis, M. W., Fierros, C. H., Hahn, B. L., Surdel, M. C., Kessler, J., Anderson, P. N., . . . Coburn, J. (2022). Identification of amino acid domains of Borrelia burgdorferi P66 that are surface exposed and important for localization, oligomerization, and porin function of the protein. Frontiers in Cellular and Infection Microbiology, 12, Article ID 991689.
Open this publication in new window or tab >>Identification of amino acid domains of Borrelia burgdorferi P66 that are surface exposed and important for localization, oligomerization, and porin function of the protein
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2022 (English)In: Frontiers in Cellular and Infection Microbiology, E-ISSN 2235-2988, Vol. 12, article id 991689Article in journal (Refereed) Published
Abstract [en]

P66, a bifunctional integral outer membrane protein, is necessary for Borrelia burgdorferi to establish initial infection and to disseminate in mice. The integrin binding function of P66 facilitates extravasation and dissemination, but the role of its porin function during murine infection has not been investigated. A limitation to studying P66 porin function during mammalian infection has been the lack of structural information for P66. In this study, we experimentally characterized specific domains of P66 with regard to structure and function. First, we aligned the amino acid sequences of P66 from Lyme disease-causing Borrelia and relapsing fever-causing Borrelia to identify conserved and unique domains between these disease-causing clades. Then, we examined whether specific domains of P66 are exposed on the surface of the bacteria by introducing c-Myc epitope tags into each domain of interest. The c-Myc epitope tag inserted C-terminally to E33 (highly conserved domain), to T187 (integrin binding region domain and a non-conserved domain), and to E334 (non-conserved domain) were all detected on the surface of Borrelia burgdorferi. The c-Myc epitope tag inserted C-terminally to E33 and D303 in conserved domains disrupted P66 oligomerization and porin function. In a murine model of infection, the E33 and D303 mutants exhibited decreased infectivity and dissemination. Taken together, these results suggest the importance of these conserved domains, and potentially P66 porin function, in vivo.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2022
Keywords
bacterial pathogenesis, Borrelia burgdorferi, c-Myc epitope tag, infectious disease, Lyme disease, P66
National Category
Cell and Molecular Biology Immunology in the medical area
Identifiers
urn:nbn:se:umu:diva-200397 (URN)10.3389/fcimb.2022.991689 (DOI)000871857500001 ()36211976 (PubMedID)2-s2.0-85139437187 (Scopus ID)
Available from: 2022-10-25 Created: 2022-10-25 Last updated: 2023-09-05Bibliographically approved
Nye, T. M., Tükenmez, H., Singh, P., Flores-Mireles, A. L., Obernuefemann, C. L. .., Pinkner, J. S., . . . Hultgren, S. J. (2022). Ring-fused 2-pyridones effective against multidrug-resistant Gram-positive pathogens and synergistic with standard-of-care antibiotics. Proceedings of the National Academy of Sciences of the United States of America, 119(43), Article ID e2210912119.
Open this publication in new window or tab >>Ring-fused 2-pyridones effective against multidrug-resistant Gram-positive pathogens and synergistic with standard-of-care antibiotics
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2022 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 119, no 43, article id e2210912119Article in journal (Refereed) Published
Abstract [en]

The alarming rise of multidrug-resistant Gram-positive bacteria has precipitated a healthcare crisis, necessitating the development of new antimicrobial therapies. Here we describe a new class of antibiotics based on a ring-fused 2-pyridone backbone, which are active against vancomycin-resistant enterococci (VRE), a serious threat as classified by the Centers for Disease Control and Prevention, and other multidrug-resistant Gram-positive bacteria. Ring-fused 2-pyridone antibiotics have bacteriostatic activity against actively dividing exponential phase enterococcal cells and bactericidal activity against nondividing stationary phase enterococcal cells. The molecular mechanism of drug-induced killing of stationary phase cells mimics aspects of fratricide observed in enterococcal biofilms, where both are mediated by the Atn autolysin and the GelE protease. In addition, combinations of sublethal concentrations of ring-fused 2-pyridones and standard-of-care antibiotics, such as vancomycin, were found to synergize to kill clinical strains of VRE. Furthermore, a broad range of antibiotic resistant Gram-positive pathogens, including those responsible for the increasing incidence of antibiotic resistant healthcare-associated infections, are susceptible to this new class of 2-pyridone antibiotics. Given the broad antibacterial activities of ring-fused 2-pyridone compounds against Gram-positive (GmP) bacteria we term these compounds GmPcides, which hold promise in combating the rising tide of antibiotic resistant Gram-positive pathogens.

Place, publisher, year, edition, pages
PNAS, 2022
Keywords
antibiotic resistance, antibiotic synergy, multidrug-resistant pathogens, VRE
National Category
Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-201191 (URN)10.1073/pnas.2210912119 (DOI)36252016 (PubMedID)2-s2.0-85141283133 (Scopus ID)
Funder
NIH (National Institutes of Health), 1U19AI157797-01NIH (National Institutes of Health), R01AI134847-01A1NIH (National Institutes of Health), R01DK128805NIH (National Institutes of Health), RO1DK51406NIH (National Institutes of Health), T32AI007172Swedish Research Council, 2018-04589Swedish Research Council, 2021-05040JThe Kempe Foundations, SMK-1755
Available from: 2023-01-05 Created: 2023-01-05 Last updated: 2023-08-25Bibliographically approved
Bharate, J. B., Ådén, J., Gharibyan, A., Adolfsson, D. E., Jayaweera, S. W., Singh, P., . . . Almqvist, F. (2021). K2S2O8-mediated coupling of 6-amino-7-aminomethyl-thiazolino-pyridones with aldehydes to construct amyloid affecting pyrimidine-fused thiazolino-2-pyridones. Organic and biomolecular chemistry, 19(44), 9758-9772
Open this publication in new window or tab >>K2S2O8-mediated coupling of 6-amino-7-aminomethyl-thiazolino-pyridones with aldehydes to construct amyloid affecting pyrimidine-fused thiazolino-2-pyridones
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2021 (English)In: Organic and biomolecular chemistry, ISSN 1477-0520, E-ISSN 1477-0539, Vol. 19, no 44, p. 9758-9772Article in journal (Refereed) Published
Abstract [en]

We herein present the synthesis of diversely functionalized pyrimidine fused thiazolino-2-pyridones via K2S2O8-mediated oxidative coupling of 6-amino-7-(aminomethyl)-thiazolino-2-pyridones with aldehydes. The developed protocol is mild, has wide substrate scope, and does not require transition metal catalyst or base. Some of the synthesized compounds have an ability to inhibit the formation of Amyloid-β fibrils associated with Alzheimer's disease, while others bind to mature amyloid-β and α-synuclein fibrils.

Place, publisher, year, edition, pages
The Royal Society of Chemistry, 2021
National Category
Organic Chemistry
Identifiers
urn:nbn:se:umu:diva-189516 (URN)10.1039/D1OB01580J (DOI)000714122800001 ()34730163 (PubMedID)2-s2.0-85120001225 (Scopus ID)
Funder
Swedish Research Council, 2017-02339; 2017-00695; 2018-04589Knut and Alice Wallenberg Foundation, 2013.0031Göran Gustafsson Foundation for Research in Natural Sciences and MedicineSwedish Foundation for Strategic Research, SB12-0070NIH (National Institutes of Health), (R01AI134847-01A1
Available from: 2021-11-15 Created: 2021-11-15 Last updated: 2023-08-09Bibliographically approved
Orikiiriza, J., Surowiec, I., Lindquist, E., Bonde, M., Magambo, J., Muhinda, C., . . . Normark, J. (2017). Lipid response patterns in acute phase paediatric Plasmodium falciparum malaria. Metabolomics, 13(4), Article ID 41.
Open this publication in new window or tab >>Lipid response patterns in acute phase paediatric Plasmodium falciparum malaria
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2017 (English)In: Metabolomics, ISSN 1573-3882, E-ISSN 1573-3890, Vol. 13, no 4, article id 41Article in journal (Refereed) Published
Abstract [en]

Introduction: Several studies have observed serum lipid changes during malaria infection in humans. All of them were focused at analysis of lipoproteins, not specific lipid molecules. The aim of our study was to identify novel patterns of lipid species in malaria infected patients using lipidomics profiling, to enhance diagnosis of malaria and to evaluate biochemical pathways activated during parasite infection.

Methods: Using a multivariate characterization approach, 60 samples were representatively selected, 20 from each category (mild, severe and controls) of the 690 study participants between age of 0.5–6 years. Lipids from patient’s plasma were extracted with chloroform/methanol mixture and subjected to lipid profiling with application of the LCMS-QTOF method.

Results: We observed a structured plasma lipid response among the malaria-infected patients as compared to healthy controls, demonstrated by higher levels of a majority of plasma lipids with the exception of even-chain length lysophosphatidylcholines and triglycerides with lower mass and higher saturation of the fatty acid chains. An inverse lipid profile relationship was observed when plasma lipids were correlated to parasitaemia.

Conclusions: This study demonstrates how mapping the full physiological lipid response in plasma from malaria-infected individuals can be used to understand biochemical processes during infection. It also gives insights to how the levels of these molecules relate to acute immune responses.

Keywords
Lipidomics profiling, Malaria, Plasmodium falciparum, Triacylglycerides, Lysophosphatidylcholines
National Category
Infectious Medicine
Identifiers
urn:nbn:se:umu:diva-133729 (URN)10.1007/s11306-017-1174-2 (DOI)000394544900010 ()28286460 (PubMedID)2-s2.0-85013783540 (Scopus ID)
Available from: 2017-05-05 Created: 2017-05-05 Last updated: 2023-03-24Bibliographically approved
Surowiec, I., Gouveia-Figueira, S., Orikiiriza, J., Lindquist, E., Bonde, M., Magambo, J., . . . Trygg, J. (2017). The oxylipin and endocannabidome responses in acute phase Plasmodium falciparum malaria in children. Malaria Journal, 16, Article ID 358.
Open this publication in new window or tab >>The oxylipin and endocannabidome responses in acute phase Plasmodium falciparum malaria in children
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2017 (English)In: Malaria Journal, E-ISSN 1475-2875, Vol. 16, article id 358Article in journal (Refereed) Published
Abstract [en]

Background: Oxylipins and endocannabinoids are low molecular weight bioactive lipids that are crucial for initiation and resolution of inflammation during microbial infections. Metabolic complications in malaria are recognized contributors to severe and fatal malaria, but the impact of malaria infection on the production of small lipid derived signalling molecules is unknown. Knowledge of immunoregulatory patterns of these molecules in malaria is of great value for better understanding of the disease and improvement of treatment regimes, since the action of these classes of molecules is directly connected to the inflammatory response of the organism.

Methods: Detection of oxylipins and endocannabinoids from plasma samples from forty children with uncomplicated and severe malaria as well as twenty controls was done after solid phase extraction followed by chromatography mass spectrometry analysis. The stable isotope dilution method was used for compound quantification. Data analysis was done with multivariate (principal component analysis (PCA), orthogonal partial least squares discriminant analysis (OPLS-DA (R)) and univariate approaches (receiver operating characteristic (ROC) curves, t tests, correlation analysis).

Results: Forty different oxylipin and thirteen endocannabinoid metabolites were detected in the studied samples, with one oxylipin (thromboxane B2, TXB2) in significantly lower levels and four endocannabinoids (OEA, PEA, DEA and EPEA) at significantly higher levels in infected individuals as compared to controls according to t test analysis with Bonferroni correction. Three oxylipins (13-HODE, 9-HODE and 13-oxo-ODE) were higher in severe compared to uncomplicated malaria cases according to the results from multivariate analysis. Observed changes in oxylipin levels can be connected to activation of cytochrome P450 (CYP) and 5-lipoxygenase (5-LOX) metabolic pathways in malaria infected individuals compared to controls, and related to increased levels of all linoleic acid oxylipins in severe patients compared to uncomplicated ones. The endocannabinoids were extremely responsive to malaria infection with majority of this class of molecules found at higher levels in infected individuals compared to controls.

Conclusions: It was possible to detect oxylipin and endocannabinoid molecules that can be potential biomarkers for differentiation between malaria infected individuals and controls and between different classes of malaria. Metabolic pathways that could be targeted towards an adjunctive therapy in the treatment of malaria were also pinpointed.

Place, publisher, year, edition, pages
BIOMED CENTRAL LTD, 2017
Keywords
Oxylipins, Endocannabinoids, Malaria infection, Plasmodium falciparum
National Category
Infectious Medicine Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-140041 (URN)10.1186/s12936-017-2001-y (DOI)000410218400001 ()28886714 (PubMedID)2-s2.0-85029086701 (Scopus ID)
Funder
Swedish Research CouncilSwedish Society of Medicine
Note

Ytterligare finansiär: Jeansson Foundation

Available from: 2017-10-05 Created: 2017-10-05 Last updated: 2024-07-04Bibliographically approved
Ristow, L., Bonde, M., Lin, Y.-P., Sato, H., Curtis, M., Wesley, E., . . . Coburn, J. (2015). Integrin binding by Borrelia burgdorferi P66 facilitates dissemination but is not required for infectivity. Cellular Microbiology, 17(7), 1021-1036
Open this publication in new window or tab >>Integrin binding by Borrelia burgdorferi P66 facilitates dissemination but is not required for infectivity
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2015 (English)In: Cellular Microbiology, ISSN 1462-5814, E-ISSN 1462-5822, Vol. 17, no 7, p. 1021-1036Article in journal (Refereed) Published
Abstract [en]

P66, a Borrelia burgdorferi surface protein with porin and integrin-binding activities, is essential for murine infection. The role of P66 integrin-binding activity in B. burgdorferi infection was investigated and found to affect transendothelial migration. The role of integrin binding, specifically, was tested by mutation of two amino acids (D205A,D207A) or deletion of seven amino acids (Del202–208). Neither change affected surface localization or channel-forming activity of P66, but both significantly reduced binding to αvβ3. Integrin-binding deficient B. burgdorferi strains caused disseminated infection in mice at 4 weeks post-subcutaneous inoculation, but bacterial burdens were significantly reduced in some tissues. Following intravenous inoculation, the Del202–208 bacteria were below the limit of detection in all tissues assessed at 2 weeks post-inoculation, but bacterial burdens recovered to wild-type levels at 4 weeks post-inoculation. The delay in tissue colonization correlated with reduced migration of the Del202–208 strains across microvascular endothelial cells, similar to Δp66bacteria. These results indicate that integrin binding by P66 is important to efficient dissemination of B. burgdorferi, which is critical to its ability to cause disease manifestations in incidental hosts and to its maintenance in the enzootic cycle.

National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-101796 (URN)10.1111/cmi.12418 (DOI)000356605900008 ()2-s2.0-84931571353 (Scopus ID)
Available from: 2015-04-13 Created: 2015-04-13 Last updated: 2023-03-24Bibliographically approved
Surowiec, I., Orikiiriza, J., Karlsson, E., Nelson, M., Bonde, M., Kyamanwa, P., . . . Normark, J. (2015). Metabolic signature profiling as a diagnostic and prognostic tool in paediatric Plasmodium falciparum malaria. Open Forum Infectious Diseases, 2(2)
Open this publication in new window or tab >>Metabolic signature profiling as a diagnostic and prognostic tool in paediatric Plasmodium falciparum malaria
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2015 (English)In: Open Forum Infectious Diseases, ISSN 2328-8957, Vol. 2, no 2Article in journal (Refereed) Published
Abstract [en]

Background: Accuracy in malaria diagnosis and staging is vital in order to reduce mortality and post infectious sequelae. Herein we present a metabolomics approach to diagnostic staging of malaria infection, specifically Plasmodium falciparum infection in children. Methods: A group of 421 patients between six months and six years of age with mild and severe states of malaria with age-matched controls were included in the study, 107, 192 and 122 individuals respectively. A multivariate design was used as basis for representative selection of twenty patients in each category. Patient plasma was subjected to Gas Chromatography-Mass Spectrometry analysis and a full metabolite profile was produced from each patient. In addition, a proof-of-concept model was tested in a Plasmodium berghei in-vivo model where metabolic profiles were discernible over time of infection. Results: A two-component principal component analysis (PCA) revealed that the patients could be separated into disease categories according to metabolite profiles, independently of any clinical information. Furthermore, two sub-groups could be identified in the mild malaria cohort who we believe represent patients with divergent prognoses. Conclusion: Metabolite signature profiling could be used both for decision support in disease staging and prognostication.

Place, publisher, year, edition, pages
Oxford University Press, 2015
Keywords
disease staging, malaria, metabolomics
National Category
Bioinformatics (Computational Biology) Infectious Medicine
Identifiers
urn:nbn:se:umu:diva-102800 (URN)10.1093/ofid/ofv062 (DOI)000365786200047 ()2-s2.0-84978328046 (Scopus ID)
Available from: 2015-05-05 Created: 2015-05-05 Last updated: 2023-03-24Bibliographically approved
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