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Article ; Online: Experimental Model of Pulmonary Inflammation Induced by SARS-CoV-2 Spike Protein and Endotoxin.

Puthia, Manoj / Tanner, Lloyd / Petruk, Ganna / Schmidtchen, Artur

ACS pharmacology & translational science

2022 Volume 5, Issue 3, Page(s) 141–148

Abstract: COVID-19 is characterized by a dysregulated and excessive inflammatory response and, in severe cases, acute respiratory distress syndrome. We have recently demonstrated a previously unknown high-affinity interaction between the SARS-CoV-2 spike (S) ... ...

Abstract	COVID-19 is characterized by a dysregulated and excessive inflammatory response and, in severe cases, acute respiratory distress syndrome. We have recently demonstrated a previously unknown high-affinity interaction between the SARS-CoV-2 spike (S) protein and bacterial lipopolysaccharide (LPS), leading to the boosting of inflammation. Here we present a mouse inflammation model employing the coadministration of aerosolized S protein together with LPS to the lungs. Using NF-κB-RE-Luc reporter and C57BL/6 mice followed by combinations of bioimaging, cytokine, chemokine, fluorescence-activated cell sorting, and histochemistry analyses, we show that the model yields severe pulmonary inflammation and a cytokine profile similar to that observed in COVID-19. Therefore, the model offers utility for analyses of the pathophysiological features of COVID-19 and the development of new treatments.
Language	English
Publishing date	2022-01-25
Publishing country	United States
Document type	Journal Article
ISSN	2575-9108
ISSN (online)	2575-9108
DOI	10.1021/acsptsci.1c00219
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Antibacterial and Anti-Inflammatory Effects of Apolipoprotein E.

Puthia, Manoj / Marzinek, Jan K / Petruk, Ganna / Ertürk Bergdahl, Gizem / Bond, Peter J / Petrlova, Jitka

Biomedicines

2022 Volume 10, Issue 6

Abstract: Apolipoprotein E (APOE) is a lipid-transport protein that functions as a key mediator of lipid transport and cholesterol metabolism. Recent studies have shown that peptides derived from human APOE display anti-inflammatory and antimicrobial effects. Here, ...

Abstract	Apolipoprotein E (APOE) is a lipid-transport protein that functions as a key mediator of lipid transport and cholesterol metabolism. Recent studies have shown that peptides derived from human APOE display anti-inflammatory and antimicrobial effects. Here, we applied in vitro assays and fluorescent microscopy to investigate the anti-bacterial effects of full-length APOE. The interaction of APOE with endotoxins from
Language	English
Publishing date	2022-06-17
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2720867-9
ISSN	2227-9059
ISSN	2227-9059
DOI	10.3390/biomedicines10061430
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Article ; Online: Selective protein aggregation confines and inhibits endotoxins in wounds: Linking host defense to amyloid formation.

Petrlova, Jitka / Hartman, Erik / Petruk, Ganna / Lim, Jeremy Chun Hwee / Adav, Sunil Shankar / Kjellström, Sven / Puthia, Manoj / Schmidtchen, Artur

iScience

2023 Volume 26, Issue 10, Page(s) 107951

Abstract: Bacterial lipopolysaccharide (LPS) induces rapid protein aggregation in human wound fluid. We aimed to characterize these LPS-induced aggregates and their functional implications using a combination of mass spectrometry analyses, biochemical assays, ... ...

Abstract	Bacterial lipopolysaccharide (LPS) induces rapid protein aggregation in human wound fluid. We aimed to characterize these LPS-induced aggregates and their functional implications using a combination of mass spectrometry analyses, biochemical assays, biological imaging, cell experiments, and animal models. The wound-fluid aggregates encompass diverse protein classes, including sequences from coagulation factors, annexins, histones, antimicrobial proteins/peptides, and apolipoproteins. We identified proteins and peptides with a high aggregation propensity and verified selected components through Western blot analysis. Thioflavin T and Amytracker staining revealed amyloid-like aggregates formed after exposure to LPS
Language	English
Publishing date	2023-09-19
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2023.107951
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Article ; Online: Thrombin-Derived C-Terminal Peptide Reduces

Dahlman, Anna / Puthia, Manoj / Petrlova, Jitka / Schmidtchen, Artur / Petruk, Ganna

Antimicrobial agents and chemotherapy

2021 Volume 65, Issue 11, Page(s) e0103221

Abstract: Infections due to the opportunistic fungus Candida have been on the rise in the last decades, especially in immunocompromised individuals and hospital settings. Unfortunately, the treatments available today are limited. Thrombin-derived C-terminal ... ...

Abstract	Infections due to the opportunistic fungus Candida have been on the rise in the last decades, especially in immunocompromised individuals and hospital settings. Unfortunately, the treatments available today are limited. Thrombin-derived C-terminal peptide (TCP-25) is an antimicrobial peptide (AMP) with antibacterial and immunomodulatory effects. In this work, we, for the first time, demonstrate the ability of TCP-25 ability to counteract Candida
MeSH term(s)	Animals ; Antifungal Agents/pharmacology ; Candida ; Candida albicans ; Inflammation/drug therapy ; Mice ; Mice, Inbred C57BL ; Peptides ; Thrombin
Chemical Substances	Antifungal Agents ; Peptides ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	2021-08-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/AAC.01032-21
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Zs.A 809: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Selective protein aggregation confines and inhibits endotoxins in wounds

Jitka Petrlova / Erik Hartman / Ganna Petruk / Jeremy Chun Hwee Lim / Sunil Shankar Adav / Sven Kjellström / Manoj Puthia / Artur Schmidtchen

iScience, Vol 26, Iss 10, Pp 107951- (2023)

Linking host defense to amyloid formation

2023

Abstract: Summary: Bacterial lipopolysaccharide (LPS) induces rapid protein aggregation in human wound fluid. We aimed to characterize these LPS-induced aggregates and their functional implications using a combination of mass spectrometry analyses, biochemical ... ...

Abstract	Summary: Bacterial lipopolysaccharide (LPS) induces rapid protein aggregation in human wound fluid. We aimed to characterize these LPS-induced aggregates and their functional implications using a combination of mass spectrometry analyses, biochemical assays, biological imaging, cell experiments, and animal models. The wound-fluid aggregates encompass diverse protein classes, including sequences from coagulation factors, annexins, histones, antimicrobial proteins/peptides, and apolipoproteins. We identified proteins and peptides with a high aggregation propensity and verified selected components through Western blot analysis. Thioflavin T and Amytracker staining revealed amyloid-like aggregates formed after exposure to LPS in vitro in human wound fluid and in vivo in porcine wound models. Using NF-κB-reporter mice and IVIS bioimaging, we demonstrate that such wound-fluid LPS aggregates induce a significant reduction in local inflammation compared with LPS in plasma. The results show that protein/peptide aggregation is a mechanism for confining LPS and reducing inflammation, further emphasizing the connection between host defense and amyloidogenesis.
Keywords	Immunology ; Bacteriology ; cell biology ; Science ; Q
Subject code	630
Language	English
Publishing date	2023-10-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: The role of full-length apoE in clearance of Gram-negative bacteria and their endotoxins.

Petruk, Ganna / Elvén, Malin / Hartman, Erik / Davoudi, Mina / Schmidtchen, Artur / Puthia, Manoj / Petrlova, Jitka

Journal of lipid research

2021 Volume 62, Page(s) 100086

Abstract: ApoE is a well-known lipid-binding protein that plays a main role in the metabolism and transport of lipids. More recently, apoE-derived peptides have been shown to exert antimicrobial effects. Here, we investigated the antibacterial activity of apoE ... ...

Abstract	ApoE is a well-known lipid-binding protein that plays a main role in the metabolism and transport of lipids. More recently, apoE-derived peptides have been shown to exert antimicrobial effects. Here, we investigated the antibacterial activity of apoE using in vitro assays, advanced imaging techniques, and in vivo mouse models. The formation of macromolecular complexes of apoE and endotoxins from Gram-negative bacteria was explored using gel shift assays, transmission electron microscopy, and CD spectroscopy followed by calculation of the α-helical content. The binding affinity of apoE to endotoxins was also confirmed by fluorescent spectroscopy detecting the quenching and shifting of tryptophan intrinsic fluorescence. We showed that apoE exhibits antibacterial activity particularly against Gram-negative bacteria such as Pseudomonas aeruginosa and Escherichia coli. ApoE protein folding was affected by binding of bacterial endotoxin components such as lipopolysaccharide (LPS) and lipid A, yielding similar increases in the apoE α-helical content. Moreover, high-molecular-weight complexes of apoE were formed in the presence of LPS, but not to the same extent as with lipid A. Together, our results demonstrate the ability of apoE to kill Gram-negative bacteria, interact with their endotoxins, which leads to the structural changes in apoE and the formation of aggregate-like complexes.
MeSH term(s)	Endotoxins
Chemical Substances	Endotoxins
Language	English
Publishing date	2021-05-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1016/j.jlr.2021.100086
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Zs.A 175: Show issues

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Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Publisher Correction: Targeting Toll-like receptor-driven systemic inflammation by engineering an innate structural fold into drugs.

Petruk, Ganna / Puthia, Manoj / Samsudin, Firdaus / Petrlova, Jitka / Olm, Franziska / Mittendorfer, Margareta / Hyllén, Snejana / Edström, Dag / Strömdahl, Ann-Charlotte / Diehl, Carl / Ekström, Simon / Walse, Björn / Kjellström, Sven / Bond, Peter J / Lindstedt, Sandra / Schmidtchen, Artur

Nature communications

2023 Volume 14, Issue 1, Page(s) 6436

Language	English
Publishing date	2023-10-13
Publishing country	England
Document type	Published Erratum
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-42294-3
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Article ; Online: SARS-CoV-2 spike protein as a bacterial lipopolysaccharide delivery system in an overzealous inflammatory cascade.

Samsudin, Firdaus / Raghuvamsi, Palur / Petruk, Ganna / Puthia, Manoj / Petrlova, Jitka / MacAry, Paul / Anand, Ganesh S / Bond, Peter J / Schmidtchen, Artur

Journal of molecular cell biology

2022 Volume 14, Issue 9

Abstract: Accumulating evidence indicates a potential role for bacterial lipopolysaccharide (LPS) in the overactivation of the immune response during SARS-CoV-2 infection. LPS is recognized by Toll-like receptor 4, mediating proinflammatory effects. We previously ... ...

Abstract	Accumulating evidence indicates a potential role for bacterial lipopolysaccharide (LPS) in the overactivation of the immune response during SARS-CoV-2 infection. LPS is recognized by Toll-like receptor 4, mediating proinflammatory effects. We previously reported that LPS directly interacts with SARS-CoV-2 spike (S) protein and enhances proinflammatory activities. Using native gel electrophoresis and hydrogen-deuterium exchange mass spectrometry, we showed that LPS binds to multiple hydrophobic pockets spanning both the S1 and S2 subunits of the S protein. Molecular simulations validated by a microscale thermophoresis binding assay revealed that LPS binds to the S2 pocket with a lower affinity compared to S1, suggesting a role as an intermediate in LPS transfer. Congruently, nuclear factor-kappa B (NF-κB) activation in monocytic THP-1 cells is strongly boosted by S2. Using NF-κB reporter mice followed by bioimaging, a boosting effect was observed for both S1 and S2, with the former potentially facilitated by proteolysis. The Omicron S variant binds to LPS, but with reduced affinity and LPS boosting in vitro and in vivo. Taken together, the data provide a molecular mechanism by which S protein augments LPS-mediated hyperinflammation.
MeSH term(s)	Humans ; Mice ; Animals ; NF-kappa B/metabolism ; Signal Transduction ; Spike Glycoprotein, Coronavirus ; Lipopolysaccharides ; COVID-19 ; SARS-CoV-2/metabolism
Chemical Substances	NF-kappa B ; spike protein, SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Lipopolysaccharides
Language	English
Publishing date	2022-10-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2500949-7
ISSN	1759-4685 ; 1759-4685
ISSN (online)	1759-4685
ISSN	1759-4685
DOI	10.1093/jmcb/mjac058
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Article ; Online: Antibacterial and Anti-Inflammatory Effects of Apolipoprotein E

Manoj Puthia / Jan K. Marzinek / Ganna Petruk / Gizem Ertürk Bergdahl / Peter J. Bond / Jitka Petrlova

Biomedicines, Vol 10, Iss 1430, p

2022 Volume 1430

Abstract	Apolipoprotein E (APOE) is a lipid-transport protein that functions as a key mediator of lipid transport and cholesterol metabolism. Recent studies have shown that peptides derived from human APOE display anti-inflammatory and antimicrobial effects. Here, we applied in vitro assays and fluorescent microscopy to investigate the anti-bacterial effects of full-length APOE. The interaction of APOE with endotoxins from Escherichia coli was explored using surface plasmon resonance, binding assays, transmission electron microscopy and all-atom molecular dynamics (MD) simulations. We also studied the immunomodulatory activity of APOE using in vitro cell assays and an in vivo mouse model in combination with advanced imaging techniques. We observed that APOE exhibits anti-bacterial activity against several Gram-negative bacterial strains of Pseudomonas aeruginosa and Escherichia coli . In addition, we showed that APOE exhibits a significant binding affinity for lipopolysaccharide (LPS) and lipid A as well as heparin. MD simulations identified the low-density lipoprotein receptor (LDLR) binding region in helix 4 of APOE as a primary binding site for these molecules via electrostatic interactions. Together, our data suggest that APOE may have an important role in controlling inflammation during Gram-negative bacterial infection.
Keywords	apolipoprotein E ; antimicrobial peptides ; Gram-negative bacteria ; host defense ; innate immunity ; aggregation ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2022-06-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Publisher Correction

Ganna Petruk / Manoj Puthia / Firdaus Samsudin / Jitka Petrlova / Franziska Olm / Margareta Mittendorfer / Snejana Hyllén / Dag Edström / Ann-Charlotte Strömdahl / Carl Diehl / Simon Ekström / Björn Walse / Sven Kjellström / Peter J. Bond / Sandra Lindstedt / Artur Schmidtchen

Nature Communications, Vol 14, Iss 1, Pp 1-

Targeting Toll-like receptor-driven systemic inflammation by engineering an innate structural fold into drugs

2023 Volume 1

Keywords	Science ; Q
Language	English
Publishing date	2023-10-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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