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Article ; Online: Effect of proteins isolated from Brazilian snakes on enterovirus A71 replication cycle: An approach against hand, foot and mouth disease

Shimizu, Jacqueline Farinha / Leite, Shiraz Feferbaum / Santos, Igor Andrade / Martins, Daniel Oliveira Silva / Kingston, Natalie J. / Shegdar, Mona / Zothner, Carsten / Sampaio, Suely Vilela / Harris, Mark / Stonehouse, Nicola J. / Jardim, Ana Carolina Gomes

International Journal of Biological Macromolecules. 2023 Apr. 19, p.124519-

2023 , Page(s) 124519–

Abstract: Enterovirus A71 (EVA71) belongs to the Picornaviridae family and is the main etiological agent of hand, foot, and mouth disease (HFMD). There is no approved antiviral against EVA71, and therefore the search for novel anti-EVA71 therapeutics is essential. ...

Abstract	Enterovirus A71 (EVA71) belongs to the Picornaviridae family and is the main etiological agent of hand, foot, and mouth disease (HFMD). There is no approved antiviral against EVA71, and therefore the search for novel anti-EVA71 therapeutics is essential. In this context, the antiviral activity of proteins isolated from snake venoms has been reported against a range of viruses. Here, the proteins CM10 and CM14 isolated from Bothrops moojeni, and Crotamin and PLA2CB isolated from Crotalus durissus terrificus were investigated for their antiviral activity against EVA71 infection. CM14 and Crotamin possessed a selective index (SI) of 170.8 and 120.4, respectively, while CM10 and PLA2CB had an SI of 67.4 and 12.5, respectively. CM14 inhibited all steps of viral replication (protective effect: 76 %; virucidal: 99 %; and post-entry: 99 %). Similarly, Crotamin inhibited up to 99 % of three steps. In contrast, CM10 and PLA2CB impaired one or two steps of EVA71 replication, respectively. Further dose-response assays using increasing titres of EVA71 were performed and CM14 and Crotamin retained functionality with high concentrations of EVA71 (up to 1000 TCID₅₀). These data demonstrate that proteins isolated from snake venom are potent inhibitors of EVA71 and could be used as scaffolds for future development of novel antivirals.
Keywords	Bothrops ; Crotalus durissus terrificus ; Enterovirus A ; antiviral agents ; antiviral properties ; dose response ; etiological agents ; foot-and-mouth disease ; mouth ; protective effect ; snake venoms ; snakes ; therapeutics ; virus replication ; Enterovirus A71 ; Antiviral ; Brazilian snakes ; Toxins ; EVA71
Language	English
Dates of publication	2023-0419
Publishing place	Elsevier B.V.
Document type	Article ; Online
Note	Pre-press version
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2023.124519
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Article ; Online: Effect of proteins isolated from Brazilian snakes on enterovirus A71 replication cycle: An approach against hand, foot and mouth disease.

Shimizu, Jacqueline Farinha / Feferbaum-Leite, Shiraz / Santos, Igor Andrade / Martins, Daniel Oliveira Silva / Kingston, Natalie J / Shegdar, Mona / Zothner, Carsten / Sampaio, Suely Vilela / Harris, Mark / Stonehouse, Nicola J / Jardim, Ana Carolina Gomes

International journal of biological macromolecules

2023 Volume 241, Page(s) 124519

Abstract	Enterovirus A71 (EVA71) belongs to the Picornaviridae family and is the main etiological agent of hand, foot, and mouth disease (HFMD). There is no approved antiviral against EVA71, and therefore the search for novel anti-EVA71 therapeutics is essential. In this context, the antiviral activity of proteins isolated from snake venoms has been reported against a range of viruses. Here, the proteins CM10 and CM14 isolated from Bothrops moojeni, and Crotamin and PLA2
MeSH term(s)	Animals ; Enterovirus ; Hand, Foot and Mouth Disease ; Brazil ; Enterovirus Infections ; Proteins ; Antiviral Agents/pharmacology ; Antigens, Viral ; Crotalid Venoms ; Snakes ; Phospholipases A2
Chemical Substances	Proteins ; Antiviral Agents ; Antigens, Viral ; Crotalid Venoms ; Phospholipases A2 (EC 3.1.1.4)
Language	English
Publishing date	2023-04-19
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2023.124519
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Article ; Online: SNAP-tagged Chikungunya Virus Replicons Improve Visualisation of Non-Structural Protein 3 by Fluorescence Microscopy.

Remenyi, Roland / Roberts, Grace C / Zothner, Carsten / Merits, Andres / Harris, Mark

Scientific reports

2017 Volume 7, Issue 1, Page(s) 5682

Abstract: Chikungunya virus (CHIKV), a mosquito-borne alphavirus, causes febrile disease, muscle and joint pain, which can become chronic in some individuals. The non-structural protein 3 (nsP3) plays essential roles during infection, but a complete understanding ... ...

Abstract	Chikungunya virus (CHIKV), a mosquito-borne alphavirus, causes febrile disease, muscle and joint pain, which can become chronic in some individuals. The non-structural protein 3 (nsP3) plays essential roles during infection, but a complete understanding of its function is lacking. Here we used a microscopy-based approach to image CHIKV nsP3 inside human cells. The SNAP system consists of a self-labelling enzyme tag, which catalyses the covalent linking of exogenously supplemented synthetic ligands. Genetic insertion of this tag resulted in viable replicons and specific labelling while preserving the effect of nsP3 on stress granule responses and co-localisation with GTPase Activating Protein (SH3 domain) Binding Proteins (G3BPs). With sub-diffraction, three-dimensional, optical imaging, we visualised nsP3-positive structures with variable density and morphology, including high-density rod-like structures, large spherical granules, and small, low-density structures. Next, we confirmed the utility of the SNAP-tag for studying protein turnover by pulse-chase labelling. We also revealed an association of nsP3 with cellular lipid droplets and examined the spatial relationships between nsP3 and the non-structural protein 1 (nsP1). Together, our study provides a sensitive, specific, and versatile system for fundamental research into the individual functions of a viral non-structural protein during infection with a medically important arthropod-borne virus (arbovirus).
MeSH term(s)	Carrier Proteins ; Cell Line, Tumor ; Chikungunya Fever/virology ; Chikungunya virus/physiology ; Cytoplasmic Granules ; Humans ; Microscopy, Fluorescence/methods ; Replicon ; Viral Nonstructural Proteins/metabolism ; src Homology Domains
Chemical Substances	Carrier Proteins ; Viral Nonstructural Proteins
Language	English
Publishing date	2017-07-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-05820-0
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Article ; Online: Evaluation of a range of mammalian and mosquito cell lines for use in Chikungunya virus research.

Roberts, Grace C / Zothner, Carsten / Remenyi, Roland / Merits, Andres / Stonehouse, Nicola J / Harris, Mark

Scientific reports

2017 Volume 7, Issue 1, Page(s) 14641

Abstract: Chikungunya virus (CHIKV) is becoming an increasing global health issue which has spread across the globe and as far north as southern Europe. There is currently no vaccine or anti-viral treatment available. Although there has been a recent increase in ... ...

Abstract	Chikungunya virus (CHIKV) is becoming an increasing global health issue which has spread across the globe and as far north as southern Europe. There is currently no vaccine or anti-viral treatment available. Although there has been a recent increase in CHIKV research, many of these in vitro studies have used a wide range of cell lines which are not physiologically relevant to CHIKV infection in vivo. In this study, we aimed to evaluate a panel of cell lines to identify a subset that would be both representative of the infectious cycle of CHIKV in vivo, and amenable to in vitro applications such as transfection, luciferase assays, immunofluorescence, western blotting and virus infection. Based on these parameters we selected four mammalian and two mosquito cell lines, and further characterised these as potential tools in CHIKV research.
MeSH term(s)	A549 Cells ; Aedes/virology ; Animals ; Cells, Cultured ; Cercopithecus aethiops ; Chikungunya Fever/virology ; Chikungunya virus/pathogenicity ; HeLa Cells ; Hep G2 Cells ; Humans ; In Vitro Techniques ; Luciferases/metabolism ; Vero Cells ; Viral Plaque Assay/methods ; Virus Replication
Chemical Substances	Luciferases (EC 1.13.12.-)
Language	English
Publishing date	2017-11-07
Publishing country	England
Document type	Evaluation Studies ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-15269-w
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Article ; Online: Persistent Replication of a Chikungunya Virus Replicon in Human Cells Is Associated with Presence of Stable Cytoplasmic Granules Containing Nonstructural Protein 3.

Remenyi, Roland / Gao, Yanni / Hughes, Ruth E / Curd, Alistair / Zothner, Carsten / Peckham, Michelle / Merits, Andres / Harris, Mark

Journal of virology

2018 Volume 92, Issue 16

Abstract: Chikungunya virus (CHIKV), a mosquito-borne human pathogen, causes a disabling disease characterized by severe joint pain that can persist for weeks, months, or even years in patients. The nonstructural protein 3 (nsP3) plays essential roles during acute ...

Abstract	Chikungunya virus (CHIKV), a mosquito-borne human pathogen, causes a disabling disease characterized by severe joint pain that can persist for weeks, months, or even years in patients. The nonstructural protein 3 (nsP3) plays essential roles during acute infection, but little is known about the function of nsP3 during chronic disease. Here, we used subdiffraction multicolor microscopy for spatial and temporal analysis of CHIKV nsP3 within human cells that persistently replicate replicon RNA. Round cytoplasmic granules of various sizes (i) contained nsP3 and stress granule assembly factors 1 and 2 (G3BP1/2), (ii) were next to double-stranded RNA foci and nsP1-positive structures, and (iii) were close to the nuclear membrane and the nuclear pore complex protein Nup98. Analysis of protein turnover and mobility by live-cell microscopy revealed that the granules could persist for hours to days, accumulated newly synthesized protein, and moved through the cytoplasm at various speeds. The granules also had a static internal architecture and were stable in cell lysates. Refractory cells that had cleared the noncytotoxic replicon regained the ability to respond to arsenite-induced stress. In summary, nsP3 can form uniquely stable granular structures that persist long-term within the host cell. This continued presence of viral and cellular protein complexes has implications for the study of the pathogenic consequences of lingering CHIKV infection and the development of strategies to mitigate the burden of chronic musculoskeletal disease brought about by a medically important arthropod-borne virus (arbovirus).
MeSH term(s)	Chikungunya virus/physiology ; Cytoplasmic Granules/chemistry ; Humans ; Spatio-Temporal Analysis ; Viral Nonstructural Proteins/analysis ; Virus Replication
Chemical Substances	Viral Nonstructural Proteins ; nsp3 protein, alphavirus
Language	English
Publishing date	2018-07-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00477-18
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Article ; Online: Is the ADP ribose site of the Chikungunya virus NSP3 Macro domain a target for antiviral approaches?

Shimizu, Jacqueline Farinha / Martins, Daniel Oliveira Silva / McPhillie, Martin J / Roberts, Grace C / Zothner, Carsten / Merits, Andres / Harris, Mark / Jardim, Ana Carolina Gomes

Acta tropica

2020 Volume 207, Page(s) 105490

Abstract: Chikungunya virus (CHIKV) is a mosquito-transmitted virus of special concern as it causes Chikungunya fever, characterized by an acute febrile illness, rash, and arthralgia that can progress to chronic and debilitating arthritic symptoms. The effects of ... ...

Abstract	Chikungunya virus (CHIKV) is a mosquito-transmitted virus of special concern as it causes Chikungunya fever, characterized by an acute febrile illness, rash, and arthralgia that can progress to chronic and debilitating arthritic symptoms. The effects of climate change on the geographic distribution of the mosquito vector has the potential to expose more of the globe to this virus. No antiviral agents or vaccines are currently available against CHIKV infection and the development of novel therapies that may lead to a future treatment is therefore necessary. In this context, the ADP-ribose binding site of the CHIKV nsP3 macro domain has been reported as a potential target for the development of antivirals. Mutations in the ADP-ribose binding site demonstrated decreased viral replication in cell culture and reduced virulence. In this study, 48,750 small molecules were screened in silico for their ability to bind to the ADP-ribose binding site of the CHIKV nsP3 macro domain. From this in silico analysis, 12 molecules were selected for in vitro analysis using a CHIKV subgenomic replicon in Huh-7 cells. Cell viability and CHIKV replication were evaluated and molecules C5 and C13 demonstrated 53 and 66% inhibition of CHIKV replication, respectively. By using a CHIKV-Dual luciferase replicon contain two reporter genes, we also demonstrated that the treatment with either compounds are probably interfering in the early replication rather than after RNA replication has occurred.
MeSH term(s)	Adenosine Diphosphate Ribose/metabolism ; Animals ; Antiviral Agents/pharmacology ; Binding Sites ; Cell Line, Tumor ; Chikungunya virus/drug effects ; Humans ; Mice ; Molecular Docking Simulation ; Protein Domains ; Viral Nonstructural Proteins/antagonists & inhibitors ; Viral Nonstructural Proteins/chemistry ; Virus Replication/drug effects
Chemical Substances	Antiviral Agents ; Viral Nonstructural Proteins ; nsp3 protein, alphavirus ; Adenosine Diphosphate Ribose (20762-30-5)
Language	English
Publishing date	2020-04-23
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	210415-5
ISSN	1873-6254 ; 0001-706X
ISSN (online)	1873-6254
ISSN	0001-706X
DOI	10.1016/j.actatropica.2020.105490
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Article ; Online: Flavonoids from Pterogyne nitens Inhibit Hepatitis C Virus Entry.

Shimizu, Jacqueline Farinha / Lima, Caroline Sprengel / Pereira, Carina Machado / Bittar, Cintia / Batista, Mariana Nogueira / Nazaré, Ana Carolina / Polaquini, Carlos Roberto / Zothner, Carsten / Harris, Mark / Rahal, Paula / Regasini, Luis Octávio / Jardim, Ana Carolina Gomes

Scientific reports

2017 Volume 7, Issue 1, Page(s) 16127

Abstract: Hepatitis C virus (HCV) is one of the leading causes of liver diseases and transplantation worldwide. The current available therapy for HCV infection is based on interferon-α, ribavirin and the new direct-acting antivirals (DAAs), such as NS3 protease ... ...

Abstract	Hepatitis C virus (HCV) is one of the leading causes of liver diseases and transplantation worldwide. The current available therapy for HCV infection is based on interferon-α, ribavirin and the new direct-acting antivirals (DAAs), such as NS3 protease and NS5B polymerase inhibitors. However, the high costs of drug design, severe side effects and HCV resistance presented by the existing treatments demonstrate the need for developing more efficient anti-HCV agents. This study aimed to evaluate the antiviral effects of sorbifolin (1) and pedalitin (2), two flavonoids from Pterogyne nitens on the HCV replication cycle. These compounds were investigated for their anti-HCV activities using genotype 2a JFH-1 subgenomic replicons and infectious virus systems. Flavonoids 1 and 2 inhibited virus entry up to 45.0% and 78.7% respectively at non-cytotoxic concentrations. The mechanism of the flavonoid 2 block to virus entry was demonstrated to be by both the direct action on virus particles and the interference on the host cells. Alternatively, the flavonoid 1 activity was restricted to its virucidal effect. Additionally, no inhibitory effects on HCV replication and release were observed by treating cells with these flavonoids. These data are the first description of 1 and 2 possessing in vitro anti-HCV activity.
MeSH term(s)	Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Fabaceae/chemistry ; Flavones/chemistry ; Flavones/pharmacology ; Flavonoids/chemistry ; Flavonoids/pharmacology ; Hepacivirus/drug effects ; Interferon-alpha/pharmacology ; Virus Replication/drug effects
Chemical Substances	Antiviral Agents ; Flavones ; Flavonoids ; Interferon-alpha ; pedalitin
Language	English
Publishing date	2017-11-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-16336-y
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Article ; Online: Multiple effects of toxins isolated from Crotalus durissus terrificus on the hepatitis C virus life cycle.

Shimizu, Jacqueline Farinha / Pereira, Carina Machado / Bittar, Cintia / Batista, Mariana Nogueira / Campos, Guilherme Rodrigues Fernandes / da Silva, Suely / Cintra, Adélia Cristina Oliveira / Zothner, Carsten / Harris, Mark / Sampaio, Suely Vilela / Aquino, Victor Hugo / Rahal, Paula / Jardim, Ana Carolina Gomes

PloS one

2017 Volume 12, Issue 11, Page(s) e0187857

Abstract: Hepatitis C virus (HCV) is one of the main causes of liver disease and transplantation worldwide. Current therapy is expensive, presents additional side effects and viral resistance has been described. Therefore, studies for developing more efficient ... ...

Abstract	Hepatitis C virus (HCV) is one of the main causes of liver disease and transplantation worldwide. Current therapy is expensive, presents additional side effects and viral resistance has been described. Therefore, studies for developing more efficient antivirals against HCV are needed. Compounds isolated from animal venoms have shown antiviral activity against some viruses such as Dengue virus, Yellow fever virus and Measles virus. In this study, we evaluated the effect of the complex crotoxin (CX) and its subunits crotapotin (CP) and phospholipase A2 (PLA2-CB) isolated from the venom of Crotalus durissus terrificus on HCV life cycle. Huh 7.5 cells were infected with HCVcc JFH-1 strain in the presence or absence of these toxins and virus was titrated by focus formation units assay or by qPCR. Toxins were added to the cells at different time points depending on the stage of virus life cycle to be evaluated. The results showed that treatment with PLA2-CB inhibited HCV entry and replication but no effect on HCV release was observed. CX reduced virus entry and release but not replication. By treating cells with CP, an antiviral effect was observed on HCV release, the only stage inhibited by this compound. Our data demonstrated the multiple antiviral effects of toxins from animal venoms on HCV life cycle.
MeSH term(s)	Animals ; Antiviral Agents/chemistry ; Antiviral Agents/isolation & purification ; Antiviral Agents/pharmacology ; Cell Line ; Crotalid Venoms/chemistry ; Crotalus ; Crotoxin/chemistry ; Crotoxin/pharmacology ; Crystallography, X-Ray ; Hepacivirus/drug effects ; Hepacivirus/physiology ; Humans ; Membrane Fusion/drug effects ; Molecular Structure ; Phospholipases A2/chemistry ; Phospholipases A2/pharmacology ; Virus Replication/drug effects
Chemical Substances	Antiviral Agents ; Crotalid Venoms ; Crotoxin (9007-40-3) ; Phospholipases A2 (EC 3.1.1.4)
Language	English
Publishing date	2017-11-15
Publishing country	United States
Document type	Journal Article
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0187857
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Article: Basic research confirms coexistence of acquired Blaschkolinear Vitiligo and acrofacial Vitiligo.

Schallreuter, Karin U / Krüger, Christian / Rokos, Hartmut / Hasse, Sybille / Zothner, Carsten / Panske, Angela

Archives of dermatological research

2007 Volume 299, Issue 5-6, Page(s) 225–230

Abstract: We report about a female patient with bilateral and unilateral blaschkolinear depigmentation on the extremities and coexistence of acrofacial vitiligo, who initially presented her first signs of depigmentation at the age of 32 years. The patient was ... ...

Abstract	We report about a female patient with bilateral and unilateral blaschkolinear depigmentation on the extremities and coexistence of acrofacial vitiligo, who initially presented her first signs of depigmentation at the age of 32 years. The patient was otherwise healthy. The correct diagnosis was based on the latest up to date technology utilizing in vivo FT-Raman and Fluorescence spectroscopy, Wood's light examination of the depigmented skin and immunoreactivity of epidermal catalase expression in 3 mm punch biopsies from the linear depigmented area. The results yielded decreased catalase protein expression compared to healthy controls as well as complete absence of melanocytes. FT-Raman spectroscopy identified the presence of hydrogen peroxide (H(2)O(2)) in the mM range and Fluorescence spectroscopy demonstrated H(2)O(2)-mediated oxidation of tryptophan residues in the depigmented area. The results were in agreement with vitiligo. Repigmentation of the linear lesion was initiated after reduction/removal of epidermal H(2)O(2) with pseudocatalase PC-KUS further supporting the correct diagnosis. To the best of our knowledge this is the first case documented with vitiligo following Blaschko lines in coexistence with classical acrofacial vitiligo. This observation raises the question whether besides H(2)O(2)-mediated stress in association with genomic mosaicism could play a role in some cases with vitiligo.
MeSH term(s)	Abnormalities, Multiple/diagnosis ; Abnormalities, Multiple/metabolism ; Abnormalities, Multiple/pathology ; Adult ; Antioxidants/metabolism ; Biopsy, Needle ; Catalase/metabolism ; Epidermis/pathology ; Extremities/pathology ; Face/pathology ; Female ; Humans ; Hydrogen Peroxide/metabolism ; Oxidants/metabolism ; Vitiligo/diagnosis
Chemical Substances	Antioxidants ; Oxidants ; Hydrogen Peroxide (BBX060AN9V) ; Catalase (EC 1.11.1.6)
Language	English
Publishing date	2007-08
Publishing country	Germany
Document type	Case Reports ; Journal Article
ZDB-ID	130131-7
ISSN	1432-069X ; 0340-3696
ISSN (online)	1432-069X
ISSN	0340-3696
DOI	10.1007/s00403-007-0748-7
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Article ; Online: Recombinant human L-ficolin directly neutralizes hepatitis C virus entry.

Hamed, Mohamed R / Brown, Richard J P / Zothner, Carsten / Urbanowicz, Richard A / Mason, Christopher P / Krarup, Anders / McClure, C Patrick / Irving, William L / Ball, Jonathan K / Harris, Mark / Hickling, Timothy P / Tarr, Alexander W

Journal of innate immunity

2014 Volume 6, Issue 5, Page(s) 676–684

Abstract: L-ficolin is a soluble pattern recognition molecule expressed by the liver that contributes to innate immune defense against microorganisms. It is well described that binding of L-ficolin to specific pathogen-associated molecular patterns activates the ... ...

Abstract	L-ficolin is a soluble pattern recognition molecule expressed by the liver that contributes to innate immune defense against microorganisms. It is well described that binding of L-ficolin to specific pathogen-associated molecular patterns activates the lectin complement pathway, resulting in opsonization and lysis of pathogens. In this study, we demonstrated that in addition to this indirect effect, L-ficolin has a direct neutralizing effect against hepatitis C virus (HCV) entry. Specific, dose-dependent binding of recombinant L-ficolin to HCV glycoproteins E1 and E2 was observed. This interaction was inhibited by soluble L-ficolin ligands. Interaction of L-ficolin with E1 and E2 potently inhibited entry of retroviral pseudoparticles bearing these glycoproteins. L-ficolin also inhibited entry of cell-cultured HCV in a calcium-dependent manner. Neutralizing concentrations of L-ficolin were found to be circulating in the serum of HCV-infected individuals. This is the first description of direct neutralization of HCV entry by a ficolin and highlights a novel role for L-ficolin as a virus entry inhibitor.
MeSH term(s)	Complement Pathway, Mannose-Binding Lectin ; HEK293 Cells ; Hepacivirus/pathogenicity ; Hepacivirus/physiology ; Hepatitis C/immunology ; Hepatitis C/transmission ; Humans ; Lectins/metabolism ; Liver/drug effects ; Liver/physiology ; Liver/virology ; Protein Binding/drug effects ; Receptors, Pattern Recognition/metabolism ; Recombinant Proteins/metabolism ; Viral Envelope Proteins/metabolism ; Virulence ; Virus Internalization/drug effects ; Ficolins
Chemical Substances	E1 protein, Hepatitis C virus ; Lectins ; Receptors, Pattern Recognition ; Recombinant Proteins ; Viral Envelope Proteins ; glycoprotein E2, Hepatitis C virus (157184-61-7)
Language	English
Publishing date	2014-05-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454158-8
ISSN	1662-8128 ; 1662-811X
ISSN (online)	1662-8128
ISSN	1662-811X
DOI	10.1159/000362209
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