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Book ; Online: PSNV für Kinder und Jugendliche in komplexen Schadenslagen

Karutz, Harald / Fegert, Ann-Katrin / Blank-Gorki, Verena / Bonsch, Claudia

(Forschung im Bevölkerungsschutz ; Band 30)

2021

Institution	Deutschland / Bundesamt für Bevölkerungsschutz und Katastrophenhilfe
Author's details	Autor und Autorinnen: Prof. Dr. phil. Harald Karutz, Ann-Katrin Fegert, Verena Blank-Gorki ; unter Mitwirkung von Claudia Bonsch [und 12 weiteren] ; Herausgeber: Bundesamt für Bevölkerungsschutz und Katastrophenhilfe
Series title	Forschung im Bevölkerungsschutz ; Band 30
Collection
Subject code	610
Language	German
Size	1 Online-Ressource (315 Seiten), Illustrationen, Diagramme
Publisher	Bundesamt für Bevölkerungsschutz und Katastrophenhilfe
Publishing place	Bonn
Publishing country	Germany
Document type	Book ; Online
Note	Open Access
HBZ-ID	HT021367691
ISBN	9783949117060 ; 3949117067
DOI	10.4126/FRL01-006433856
Database	Repository for Life Sciences

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Book: PSNV für Kinder und Jugendliche in komplexen Schadenslagen

Karutz, Harald / Fegert, Ann-Katrin / Blank-Gorki, Verena / Bonsch, Claudia

(Forschung im Bevölkerungsschutz ; Band 30)

2021

Title variant	Psychosoziale Notfallversorgnung für Kinder und Jugendliche in komplexen Schadenslagen
Author's details	Autor und Autorinnen: Prof. Dr. phil. Harald Karutz, Ann-Katrin Fegert, Verena Blank-Gorki ; unter Mitwirkung von Claudia Bonsch [und 12 weiteren]
Series title	Forschung im Bevölkerungsschutz ; Band 30
Collection
Keywords	Kind ; Jugend ; Zivilschutz ; Notfall ; Krisenintervention ; Psychosoziale Versorgung
Subject	Notfallpsychotherapie ; Ärztlicher Notfall ; Bevölkerungsschutz ; Ziviler Bevölkerungsschutz ; Jugend ; Jugendalter ; Jugendlicher ; Teenager ; Kindheit ; Kindesalter ; Kindschaft ; Kinder
Language	German
Size	315 Seiten, Illustrationen, Diagramme
Publisher	Bundesamt für Bevölkerungsschutz und Katastrophenhilfe
Publishing place	Bonn
Publishing country	Germany
Document type	Book
HBZ-ID	HT021210469
ISBN	978-3-949117-06-0 ; 3-949117-06-7
Database	Catalogue ZB MED Medicine, Health

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2022 A 166	available for loan (reading room)	Lesesaal EG

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Article: Leitlinien des European Resuscitation Council 2021

Schiewe, Robert / Bönsch, Claudia / Wnent, Jan / Gräsner, Jan-Thorsten / Scholz, Jens / Bein, Berthold

Notfallmedizin up2date

2022 Volume 17, Issue 01, Page(s) 21–47

Keywords	Herz-Kreislauf-Stillstand ; Wiederbelebung ; Advanced Life Support ; Leitlinie ; Epidemiologie ; Systems Saving Lives ; Out of Hospital Cardiac Arrest ; In Hospital Cardiac Arrest ; Reanimationsschulung
Language	German
Publishing date	2022-02-01
Publisher	Georg Thieme Verlag KG
Publishing place	Stuttgart ; New York
Document type	Article
ZDB-ID	2255461-0
ISSN	1862-6955 ; 1611-6550
ISSN (online)	1862-6955
ISSN	1611-6550
DOI	10.1055/a-1645-8677
Database	Thieme publisher's database

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Article ; Online: Potent Anti-HIV Chemokine Analogs Direct Post-Endocytic Sorting of CCR5.

Bönsch, Claudia / Munteanu, Mihaela / Rossitto-Borlat, Irène / Fürstenberg, Alexandre / Hartley, Oliver

PloS one

2015 Volume 10, Issue 4, Page(s) e0125396

Abstract: G protein-coupled receptors (GPCRs) are desensitized and internalized following activation. They are then subjected to post-endocytic sorting (degradation, slow recycling or fast recycling). The majority of research on post-endocytic sorting has focused ... ...

Abstract	G protein-coupled receptors (GPCRs) are desensitized and internalized following activation. They are then subjected to post-endocytic sorting (degradation, slow recycling or fast recycling). The majority of research on post-endocytic sorting has focused on the role of sequence-encoded address structures on receptors. This study focuses on trafficking of CCR5, a GPCR chemokine receptor and the principal entry coreceptor for HIV. Using Chinese Hamster Ovary cells stably expressing CCR5 we show that two different anti-HIV chemokine analogs, PSC-RANTES and 5P14-RANTES, direct receptor trafficking into two distinct subcellular compartments: the trans-Golgi network and the endosome recycling compartment, respectively. Our results indicate that a likely mechanism for ligand-directed sorting of CCR5 involves capacity of the chemokine analogs to elicit the formation of durable complexes of CCR5 and arrestin2 (beta-arrestin-1), with PSC-RANTES eliciting durable association in contrast to 5P14-RANTES, which elicits only transient association.
MeSH term(s)	Animals ; Arrestins/genetics ; Arrestins/metabolism ; CHO Cells ; Chemokine CCL5/administration & dosage ; Chemokines/genetics ; Chemokines/metabolism ; Cricetinae ; Cricetulus ; Endosomes/genetics ; Endosomes/metabolism ; HIV Infections/genetics ; HIV Infections/metabolism ; HIV Infections/pathology ; Humans ; Ligands ; Receptors, CCR5/biosynthesis ; Receptors, CCR5/genetics ; beta-Arrestin 1 ; beta-Arrestins ; trans-Golgi Network/genetics ; trans-Golgi Network/metabolism
Chemical Substances	ARRB1 protein, human ; Arrestins ; Chemokine CCL5 ; Chemokines ; Ligands ; Receptors, CCR5 ; beta-Arrestin 1 ; beta-Arrestins
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0125396
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Interaction of parvovirus B19 with human erythrocytes alters virus structure and cell membrane integrity.

Bönsch, Claudia / Kempf, Christoph / Ros, Carlos

Journal of virology

2008 Volume 82, Issue 23, Page(s) 11784–11791

Abstract: The unique region of the capsid protein VP1 (VP1u) of B19 virus (B19V) elicits a dominant immune response and has a phospholipase A(2) (PLA(2)) activity required for the infection. Despite these properties, we have observed that the VP1u-PLA(2) motif ... ...

Abstract	The unique region of the capsid protein VP1 (VP1u) of B19 virus (B19V) elicits a dominant immune response and has a phospholipase A(2) (PLA(2)) activity required for the infection. Despite these properties, we have observed that the VP1u-PLA(2) motif occupies an internal position in the capsid. However, brief exposure to increasing temperatures induced a progressive accessibility of the PLA(2) motif as well as a proportional increase of the PLA(2) activity. Similarly, upon binding on human red blood cells (RBCs), a proportion of the capsids externalized the VP1u-PLA(2) motif. Incubation of B19V with RBCs from 17 healthy donors resulted in extensive virus attachment ranging between 3,000 and 30,000 virions per cell. B19V empty capsids represent an important fraction of the viral particles circulating in the blood (30 to 40%) and bind to RBCs in the same way as full capsids. The extensive B19V binding to RBCs did not cause direct hemolysis but an increased osmotic fragility of the cells by a mechanism involving the PLA(2) activity of the exposed VP1u. Analysis of a blood sample from an individual with a recent B19V infection revealed that, at this particular moment of the infection, the virions circulating in the blood were mostly associated to the RBC fraction. However, the RBC-bound B19V was not able to infect susceptible cells. These observations indicate that RBCs play a significant role during B19V infection by triggering the exposure of the immunodominant VP1u including its PLA(2) constituent. On the other hand, the early exposure of VP1u might facilitate viral internalization and/or uncoating in target cells.
MeSH term(s)	Amino Acid Motifs ; Blood Donors ; Capsid/enzymology ; Capsid/physiology ; Cells, Cultured ; Erythrocytes/virology ; Hemolysis ; Hot Temperature ; Humans ; Osmotic Fragility ; Parvovirus B19, Human/physiology ; Parvovirus B19, Human/ultrastructure ; Phospholipase A2 Inhibitors ; Phospholipases A2/chemistry ; Phospholipases A2/physiology
Chemical Substances	Phospholipase A2 Inhibitors ; Phospholipases A2 (EC 3.1.1.4)
Language	English
Publishing date	2008-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01399-08
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Potent Anti-HIV Chemokine Analogs Direct Post-Endocytic Sorting of CCR5.

Claudia Bönsch / Mihaela Munteanu / Irène Rossitto-Borlat / Alexandre Fürstenberg / Oliver Hartley

PLoS ONE, Vol 10, Iss 4, p e

2015 Volume 0125396

Abstract	G protein-coupled receptors (GPCRs) are desensitized and internalized following activation. They are then subjected to post-endocytic sorting (degradation, slow recycling or fast recycling). The majority of research on post-endocytic sorting has focused on the role of sequence-encoded address structures on receptors. This study focuses on trafficking of CCR5, a GPCR chemokine receptor and the principal entry coreceptor for HIV. Using Chinese Hamster Ovary cells stably expressing CCR5 we show that two different anti-HIV chemokine analogs, PSC-RANTES and 5P14-RANTES, direct receptor trafficking into two distinct subcellular compartments: the trans-Golgi network and the endosome recycling compartment, respectively. Our results indicate that a likely mechanism for ligand-directed sorting of CCR5 involves capacity of the chemokine analogs to elicit the formation of durable complexes of CCR5 and arrestin2 (beta-arrestin-1), with PSC-RANTES eliciting durable association in contrast to 5P14-RANTES, which elicits only transient association.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2015-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: The globoside receptor triggers structural changes in the B19 virus capsid that facilitate virus internalization.

Bönsch, Claudia / Zuercher, Christoph / Lieby, Patricia / Kempf, Christoph / Ros, Carlos

Journal of virology

2010 Volume 84, Issue 22, Page(s) 11737–11746

Abstract: Globoside (Gb4Cer), Ku80 autoantigen, and α5β1 integrin have been identified as cell receptors/coreceptors for human parvovirus B19 (B19V), but their role and mechanism of interaction with the virus are largely unknown. In UT7/Epo cells, expression of ... ...

Abstract	Globoside (Gb4Cer), Ku80 autoantigen, and α5β1 integrin have been identified as cell receptors/coreceptors for human parvovirus B19 (B19V), but their role and mechanism of interaction with the virus are largely unknown. In UT7/Epo cells, expression of Gb4Cer and CD49e (integrin alpha-5) was high, but expression of Ku80 was insignificant. B19V colocalized with Gb4Cer and, to a lesser extent, with CD49e. However, only anti-Gb4Cer antibodies could disturb virus attachment. Only a small proportion of cell-bound viruses were internalized, while the majority became detached from the receptor. When added to uninfected cells, the receptor-detached virus showed superior cell binding capacity and infectivity. Attachment of B19V to cells triggered conformational changes in the capsid leading to the accessibility of the N terminus of VP1 (VP1u) to antibodies, which was maintained in the receptor-detached virus. VP1u became similarly accessible to antibodies following incubation of B19V particles with increasing concentrations of purified Gb4Cer. The receptor-mediated exposure of VP1u is critical for virus internalization, since capsids lacking VP1 could bind to cells but were not internalized. Moreover, an antibody against the N terminus of VP1u disturbed virus internalization, but only when present during and not after virus attachment, indicating the involvement of this region in binding events required for internalization. These results suggest that Gb4Cer is not only the primary receptor for B19V attachment but also the mediator of capsid rearrangements required for subsequent interactions leading to virus internalization. The capacity of the virus to detach and reattach again would enhance the probability of productive infections.
MeSH term(s)	Capsid/chemistry ; Capsid/metabolism ; Capsid Proteins/chemistry ; Capsid Proteins/metabolism ; Cell Line ; Globosides/genetics ; Globosides/metabolism ; Humans ; Parvoviridae Infections/metabolism ; Parvoviridae Infections/virology ; Parvovirus B19, Human/chemistry ; Parvovirus B19, Human/genetics ; Parvovirus B19, Human/physiology ; Receptors, Virus/genetics ; Receptors, Virus/metabolism ; Virus Internalization
Chemical Substances	Capsid Proteins ; Globosides ; Receptors, Virus ; globotetraosylceramide (11034-93-8)
Language	English
Publishing date	2010-09-08
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.01143-10
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Coordinate-based co-localization-mediated analysis of arrestin clustering upon stimulation of the C-C chemokine receptor 5 with RANTES/CCL5 analogues.

Tarancón Díez, Laura / Bönsch, Claudia / Malkusch, Sebastian / Truan, Zinnia / Munteanu, Mihaela / Heilemann, Mike / Hartley, Oliver / Endesfelder, Ulrike / Fürstenberg, Alexandre

Histochemistry and cell biology

2014 Volume 142, Issue 1, Page(s) 69–77

Abstract: G protein-coupled receptor activation and desensitization leads to recruitment of arrestin proteins from cytosolic pools to the cell membrane where they form clusters difficult to characterize due to their small size and further mediate receptor ... ...

Abstract	G protein-coupled receptor activation and desensitization leads to recruitment of arrestin proteins from cytosolic pools to the cell membrane where they form clusters difficult to characterize due to their small size and further mediate receptor internalization. We quantitatively investigated clustering of arrestin 3 induced by potent anti-HIV analogues of the chemokine RANTES after stimulation of the C-C chemokine receptor 5 using single-molecule localization-based super-resolution microscopy. We determined arrestin 3 cluster sizes and relative fractions of arrestin 3 molecules in each cluster through image-based analysis of the localization data by adapting a method originally developed for co-localization analysis from molecular coordinates. We found that only classical agonists in the set of tested ligands were able to efficiently recruit arrestin 3 to clusters mostly larger than 150 nm in size and compare our results with existing data on arrestin 2 clustering induced by the same chemokine analogues.
MeSH term(s)	Animals ; Arrestins/analysis ; Arrestins/metabolism ; CHO Cells ; Cattle ; Cells, Cultured ; Chemokine CCL5/chemistry ; Chemokine CCL5/pharmacology ; Cricetulus ; Microscopy, Confocal ; Microscopy, Fluorescence ; Protein Transport/drug effects ; Receptors, CCR5/agonists
Chemical Substances	Arrestins ; Chemokine CCL5 ; Receptors, CCR5 ; arrestin3
Language	English
Publishing date	2014-03-13
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1222930-1
ISSN	1432-119X ; 0301-5564 ; 0948-6143
ISSN (online)	1432-119X
ISSN	0301-5564 ; 0948-6143
DOI	10.1007/s00418-014-1206-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Quantitative morphological analysis of arrestin2 clustering upon G protein-coupled receptor stimulation by super-resolution microscopy.

Truan, Zinnia / Tarancón Díez, Laura / Bönsch, Claudia / Malkusch, Sebastian / Endesfelder, Ulrike / Munteanu, Mihaela / Hartley, Oliver / Heilemann, Mike / Fürstenberg, Alexandre

Journal of structural biology

2013 Volume 184, Issue 2, Page(s) 329–334

Abstract: Clustering of arrestins upon G protein-coupled receptor stimulation is a phenomenon that is well-known but difficult to describe quantitatively due to the size of the clusters close to the diffraction limit of visible light. We introduce a general method ...

Abstract	Clustering of arrestins upon G protein-coupled receptor stimulation is a phenomenon that is well-known but difficult to describe quantitatively due to the size of the clusters close to the diffraction limit of visible light. We introduce a general method to quantitatively investigate the clustering of arrestin following stimulation of the C-C chemokine receptor 5 (CCR5) using single-molecule super-resolution imaging and coordinate and image-based cluster analysis. We investigated the effect of potent anti-HIV ligands of CCR5 with different pharmacological profiles on arrestin2 cluster formation and found that only the ligands capable of inducing CCR5 internalization induced arrestin2 recruitment and clustering. We further demonstrate that the fraction of arrestin2 molecules found in clusters larger than 100nm correlates with the magnitude of ligand-induced CCR5 internalization, but not with G protein activation, indicating that recruitment of arrestin2 to CCR5 is independent of G protein activation. Pre-treatment of the cells with the drug cytochalasin D, which blocks actin polymerization, led to the formation of larger clusters, whereas the inhibitor of microtubule polymerization nocodazole had little effect on arrestin2 recruitment, suggesting an active role of actin in the organization and dynamics of these aggregates.
MeSH term(s)	Actin Cytoskeleton/drug effects ; Actin Cytoskeleton/metabolism ; Animals ; Arrestins/metabolism ; CHO Cells ; Cattle ; Chemokine CCL5/pharmacology ; Chemokine CCL5/physiology ; Chemokines, CC/pharmacology ; Cricetinae ; Cricetulus ; Cytochalasin D/pharmacology ; Green Fluorescent Proteins/metabolism ; Microscopy, Fluorescence ; Nocodazole/pharmacology ; Protein Transport ; Receptors, CCR5/metabolism ; Recombinant Fusion Proteins/metabolism ; Single-Domain Antibodies/chemistry ; Tubulin Modulators/pharmacology
Chemical Substances	5P12-RANTES ; Arrestins ; Chemokine CCL5 ; Chemokines, CC ; Receptors, CCR5 ; Recombinant Fusion Proteins ; Single-Domain Antibodies ; Tubulin Modulators ; Green Fluorescent Proteins (147336-22-9) ; Cytochalasin D (22144-77-0) ; Nocodazole (SH1WY3R615)
Language	English
Publishing date	2013-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1032718-6
ISSN	1095-8657 ; 1047-8477
ISSN (online)	1095-8657
ISSN	1047-8477
DOI	10.1016/j.jsb.2013.09.019
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Characterization of the early steps of human parvovirus B19 infection.

Quattrocchi, Silva / Ruprecht, Nico / Bönsch, Claudia / Bieli, Sven / Zürcher, Christoph / Boller, Klaus / Kempf, Christoph / Ros, Carlos

Journal of virology

2012 Volume 86, Issue 17, Page(s) 9274–9284

Abstract: The early steps of human parvovirus B19 (B19V) infection were investigated in UT7/Epo cells. B19V and its receptor globoside (Gb4Cer) associate with lipid rafts, predominantly of the noncaveolar type. Pharmacological disruption of the lipid rafts ... ...

Abstract	The early steps of human parvovirus B19 (B19V) infection were investigated in UT7/Epo cells. B19V and its receptor globoside (Gb4Cer) associate with lipid rafts, predominantly of the noncaveolar type. Pharmacological disruption of the lipid rafts inhibited infection when the drug was added prior to virus attachment but not after virus uptake. B19V is internalized by clathrin-dependent endocytosis and spreads rapidly throughout the endocytic pathway, reaching the lysosomal compartment within minutes, where a substantial proportion is degraded. B19V did not permeabilize the endocytic vesicles, indicating a mechanism of endosomal escape without apparent membrane damage. Bafilomycin A(1) (BafA1) and NH(4)Cl, which raise endosomal pH, blocked the infection by preventing endosomal escape, resulting in a massive accumulation of capsids in the lysosomes. In contrast, in the presence of chloroquine (CQ), the transfer of incoming viruses from late endosomes to lysosomes was prevented; the viral DNA was not degraded; and the infection was boosted. In contrast to the findings for untreated or BafA1-treated cells, the viral DNA was progressively associated with the nucleus in CQ-treated cells, reaching a plateau by 3 h postinternalization, a time coinciding with the initiation of viral transcription. At this time, more than half of the total intracellular viral DNA was associated with the nucleus; however, the capsids remained extranuclear. Our studies provide the first insight into the early steps of B19V infection and reveal mechanisms involved in virus uptake, endocytic trafficking, and nuclear penetration.
MeSH term(s)	Cell Line ; Cell Nucleus/virology ; Endocytosis ; Endosomes/virology ; Erythema Infectiosum/metabolism ; Erythema Infectiosum/virology ; Globosides/metabolism ; Humans ; Lysosomes/virology ; Parvovirus B19, Human/physiology ; Receptors, Virus/metabolism
Chemical Substances	Globosides ; Receptors, Virus
Language	English
Publishing date	2012-06-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01004-12
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