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Book: Forschungsanträge in den Life Sciences

Marschall, Manfred / Lang, Stefan

Drittmittel erfolgreich einwerben

2020

Author's details	Manfred Marschall, Stefan Lang
Keywords	Labor ; Finanzierung ; Ratgeber ; Medizin ; Forschung ; Wissenschaft ; Klinik ; Tipps ; Schreiben ; Biologie ; Förderung ; Anleitung ; Wissenschaftlich ; Life Science ; Scientific Writing ; Medical Writing ; Forschungsprojekt ; Drittmittel ; Forschungsantrag ; Forschungsvorhaben ; Drittmittelförderung ; Projektförderung
Language	German
Size	X, 153 Seiten, Illustrationen, 22 cm x 17 cm, 302 g
Edition	1. Auflage
Publisher	tredition
Publishing place	Hamburg
Publishing country	Germany
Document type	Book
HBZ-ID	HT020805180
ISBN	978-3-347-17077-3 ; 3-347-17077-6 ; 978-3-347-17078-0 ; 9783347170797 ; 3-347-17078-4 ; 3347170792
Database	Catalogue ZB MED Medicine, Health

In stock of ZB MED Cologne/Königswinter

Shelf mark	Loan status	Location
2021 A 173	available for loan (reading room)	Lesesaal EG

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Article ; Online: 'Getting Better'-Is It a Feasible Strategy of Broad Pan-Antiherpesviral Drug Targeting by Using the Nuclear Egress-Directed Mechanism?

Tillmanns, Julia / Kicuntod, Jintawee / Lösing, Josephine / Marschall, Manfred

International journal of molecular sciences

2024 Volume 25, Issue 5

Abstract: The herpesviral nuclear egress represents an essential step of viral replication efficiency in host cells, as it defines the nucleocytoplasmic release of viral capsids. Due to the size limitation of the nuclear pores, viral nuclear capsids are unable to ... ...

Abstract	The herpesviral nuclear egress represents an essential step of viral replication efficiency in host cells, as it defines the nucleocytoplasmic release of viral capsids. Due to the size limitation of the nuclear pores, viral nuclear capsids are unable to traverse the nuclear envelope without a destabilization of this natural host-specific barrier. To this end, herpesviruses evolved the regulatory nuclear egress complex (NEC), composed of a heterodimer unit of two conserved viral NEC proteins (core NEC) and a large-size extension of this complex including various viral and cellular NEC-associated proteins (multicomponent NEC). Notably, the NEC harbors the pronounced ability to oligomerize (core NEC hexamers and lattices), to multimerize into higher-order complexes, and, ultimately, to closely interact with the migrating nuclear capsids. Moreover, most, if not all, of these NEC proteins comprise regulatory modifications by phosphorylation, so that the responsible kinases, and additional enzymatic activities, are part of the multicomponent NEC. This sophisticated basis of NEC-specific structural and functional interactions offers a variety of different modes of antiviral interference by pharmacological or nonconventional inhibitors. Since the multifaceted combination of NEC activities represents a highly conserved key regulatory stage of herpesviral replication, it may provide a unique opportunity towards a broad, pan-antiherpesviral mechanism of drug targeting. This review presents an update on chances, challenges, and current achievements in the development of NEC-directed antiherpesviral strategies.
MeSH term(s)	Cytomegalovirus/metabolism ; Nuclear Envelope/metabolism ; Viral Proteins/metabolism ; Herpesviridae/metabolism ; Phosphorylation ; Simplexvirus/metabolism ; Cell Nucleus/metabolism
Chemical Substances	Viral Proteins
Language	English
Publishing date	2024-02-29
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms25052823
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: 'Come together'-The Regulatory Interaction of Herpesviral Nuclear Egress Proteins Comprises Both Essential and Accessory Functions.

Häge, Sigrun / Marschall, Manfred

Cells

2022 Volume 11, Issue 11

Abstract: Herpesviral nuclear egress is a fine-tuned regulatory process that defines the nucleocytoplasmic release of viral capsids. Nuclear capsids are unable to traverse via nuclear pores due to the fact of their large size; therefore, herpesviruses evolved to ... ...

Abstract	Herpesviral nuclear egress is a fine-tuned regulatory process that defines the nucleocytoplasmic release of viral capsids. Nuclear capsids are unable to traverse via nuclear pores due to the fact of their large size; therefore, herpesviruses evolved to develop a vesicular transport pathway mediating the transition across the two leaflets of the nuclear membrane. The entire process involves a number of regulatory proteins, which support the local distortion of the nuclear envelope. In the case of the prototype species of β-
MeSH term(s)	Antiviral Agents/metabolism ; Cytomegalovirus ; Humans ; Infant, Newborn ; Nuclear Envelope/metabolism ; Simplexvirus/metabolism ; Viral Proteins/metabolism
Chemical Substances	Antiviral Agents ; Viral Proteins
Language	English
Publishing date	2022-06-04
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11111837
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Human cytomegalovirus (CMV) dysregulates neurodevelopmental pathways in cerebral organoids.

Egilmezer, Ece / Hamilton, Stuart T / Foster, Charles S P / Marschall, Manfred / Rawlinson, William D

Communications biology

2024 Volume 7, Issue 1, Page(s) 340

Abstract: Human cytomegalovirus (CMV) infection is the leading non-genetic aetiology of congenital malformation in developed countries, causing significant fetal neurological injury. This study investigated potential CMV pathogenetic mechanisms of fetal neural ... ...

Abstract	Human cytomegalovirus (CMV) infection is the leading non-genetic aetiology of congenital malformation in developed countries, causing significant fetal neurological injury. This study investigated potential CMV pathogenetic mechanisms of fetal neural malformation using in vitro human cerebral organoids. Cerebral organoids were permissive to CMV replication, and infection dysregulated cellular pluripotency and differentiation pathways. Aberrant expression of dual-specificity tyrosine phosphorylation-regulated kinases (DYRK), sonic hedgehog (SHH), pluripotency, neurodegeneration, axon guidance, hippo signalling and dopaminergic synapse pathways were observed in CMV-infected organoids using immunofluorescence and RNA-sequencing. Infection with CMV resulted in dysregulation of 236 Autism Spectrum Disorder (ASD)-related genes (p = 1.57E-05) and pathways. This notable observation suggests potential links between congenital CMV infection and ASD. Using DisGeNET databases, 103 diseases related to neural malformation or mental disorders were enriched in CMV-infected organoids. Cytomegalovirus infection-related dysregulation of key cerebral cellular pathways potentially provides important, modifiable pathogenetic mechanisms for congenital CMV-induced neural malformation and ASD.
MeSH term(s)	Female ; Humans ; Cytomegalovirus/physiology ; Autism Spectrum Disorder/genetics ; Autism Spectrum Disorder/metabolism ; Hedgehog Proteins/metabolism ; Cytomegalovirus Infections/congenital ; Cytomegalovirus Infections/metabolism ; Fetal Diseases ; Organoids/metabolism
Chemical Substances	Hedgehog Proteins
Language	English
Publishing date	2024-03-19
Publishing country	England
Document type	Journal Article
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-024-05923-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: The Cytomegalovirus Protein Kinase pUL97:Host Interactions, Regulatory Mechanisms and Antiviral Drug Targeting.

Steingruber, Mirjam / Marschall, Manfred

Microorganisms

2020 Volume 8, Issue 4

Abstract: Human cytomegalovirus (HCMV) expresses a variety of viral regulatory proteins that undergo close interaction with host factors including viral-cellular multiprotein complexes. The HCMV protein kinase pUL97 represents a viral cyclin-dependent kinase ... ...

Abstract	Human cytomegalovirus (HCMV) expresses a variety of viral regulatory proteins that undergo close interaction with host factors including viral-cellular multiprotein complexes. The HCMV protein kinase pUL97 represents a viral cyclin-dependent kinase ortholog (vCDK) that determines the efficiency of HCMV replication via phosphorylation of viral and cellular substrates. A hierarchy of functional importance of individual pUL97-mediated phosphorylation events has been discussed; however, the most pronounced pUL97-dependent phenotype could be assigned to viral nuclear egress, as illustrated by deletion of the UL97 gene or pharmacological pUL97 inhibition. Despite earlier data pointing to a cyclin-independent functionality, experimental evidence increasingly emphasized the role of pUL97-cyclin complexes. Consequently, the knowledge about pUL97 involvement in host interaction, viral nuclear egress and additional replicative steps led to the postulation of pUL97 as an antiviral target. Indeed, validation experiments in vitro and in vivo confirmed the sustainability of this approach. Consequently, current investigations of pUL97 in antiviral treatment go beyond the known pUL97-mediated ganciclovir prodrug activation and henceforward include pUL97-specific kinase inhibitors. Among a number of interesting small molecules analyzed in experimental and preclinical stages, maribavir is presently investigated in clinical studies and, in the near future, might represent a first kinase inhibitor applied in the field of antiviral therapy.
Language	English
Publishing date	2020-04-04
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2720891-6
ISSN	2076-2607
ISSN	2076-2607
DOI	10.3390/microorganisms8040515
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: The Cytomegalovirus Protein Kinase pUL97: Host Interactions, Regulatory Mechanisms and Antiviral Drug Targeting

Steingruber, Mirjam / Marschall, Manfred

Microorganisms. 2020 Apr. 04, v. 8, no. 4

2020

Abstract	Human cytomegalovirus (HCMV) expresses a variety of viral regulatory proteins that undergo close interaction with host factors including viral-cellular multiprotein complexes. The HCMV protein kinase pUL97 represents a viral cyclin-dependent kinase ortholog (vCDK) that determines the efficiency of HCMV replication via phosphorylation of viral and cellular substrates. A hierarchy of functional importance of individual pUL97-mediated phosphorylation events has been discussed; however, the most pronounced pUL97-dependent phenotype could be assigned to viral nuclear egress, as illustrated by deletion of the UL97 gene or pharmacological pUL97 inhibition. Despite earlier data pointing to a cyclin-independent functionality, experimental evidence increasingly emphasized the role of pUL97-cyclin complexes. Consequently, the knowledge about pUL97 involvement in host interaction, viral nuclear egress and additional replicative steps led to the postulation of pUL97 as an antiviral target. Indeed, validation experiments in vitro and in vivo confirmed the sustainability of this approach. Consequently, current investigations of pUL97 in antiviral treatment go beyond the known pUL97-mediated ganciclovir prodrug activation and henceforward include pUL97-specific kinase inhibitors. Among a number of interesting small molecules analyzed in experimental and preclinical stages, maribavir is presently investigated in clinical studies and, in the near future, might represent a first kinase inhibitor applied in the field of antiviral therapy.
Keywords	Human betaherpesvirus 5 ; antiviral agents ; cyclin-dependent kinase ; genes ; phenotype ; phosphorylation ; therapeutics
Language	English
Dates of publication	2020-0404
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2720891-6
ISSN	2076-2607
ISSN	2076-2607
DOI	10.3390/microorganisms8040515
Database	NAL-Catalogue (AGRICOLA)

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Book ; Online ; Thesis: Etablierung eines qRT-PCR-Verfahrens zum quantitativen Nachweis von lymphatischen Endothelzellen in Zellmischungen

Kölbel, Patrick [Verfasser] / Marschall, Manfred [Akademischer Betreuer] / Naschberger, Elisabeth [Gutachter]

2023

Author's details	Patrick Kölbel ; Gutachter: Elisabeth Naschberger ; Betreuer: Manfred Marschall
Keywords	Medizin, Gesundheit ; Medicine, Health
Subject code	sg610
Language	German
Publisher	Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU)
Publishing place	Erlangen
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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Article ; Online: An antiviral targeting strategy based on the inducible interference with cytomegalovirus nuclear egress complex.

Kicuntod, Jintawee / Häge, Sigrun / Lösing, Josephine / Kopar, Serli / Muller, Yves A / Marschall, Manfred

Antiviral research

2023 Volume 212, Page(s) 105557

Abstract: The nucleocytoplasmic capsid egress of herpesviruses like the human cytomegalovirus (HCMV) is based on a uniquely regulated process. The core nuclear egress complex (NEC) of HCMV, represented by the pUL50-pUL53 heterodimer, is able to oligomerize and ... ...

Abstract	The nucleocytoplasmic capsid egress of herpesviruses like the human cytomegalovirus (HCMV) is based on a uniquely regulated process. The core nuclear egress complex (NEC) of HCMV, represented by the pUL50-pUL53 heterodimer, is able to oligomerize and thus to build hexameric lattices. Recently, we and others validated the NEC as a novel target for antiviral strategies. So far, the experimental targeting approaches included the development of NEC-directed small molecules, cell-penetrating peptides and NEC-directed mutagenesis. Our postulate states that an interference with the hook-into-groove interaction of pUL50-pUL53 prevents NEC formation and strictly limits viral replication efficiency. Here, we provide an experimental proof-of-concept of the antiviral strategy: the inducible intracellular expression of a NLS-Hook-GFP construct exerted a pronounced level of antiviral activity. The data provide evidence for the following points: (i) generation of a primary fibroblast population with inducible NLS-Hook-GFP expression showed nuclear localization of the construct, (ii) interaction between NLS-Hook-GFP and the viral core NEC was found specific for cytomegaloviruses but not for other herpesviruses, (iii) construct overexpression exerted a strong antiviral activity against three strains of HCMV, (iv) confocal imaging demonstrated the interference with NEC nuclear rim formation in HCMV-infected cells, and (v) quantitative nuclear egress assay confirmed the block of viral nucleocytoplasmic transition and, consequently, an inhibitory effect onto viral cytoplasmic virion assembly complex (cVAC). Combined, data confirmed that the specific interference with protein-protein interaction of the HCMV core NEC represents an efficient antiviral targeting strategy.
MeSH term(s)	Humans ; Cytomegalovirus ; Antiviral Agents/pharmacology ; Antiviral Agents/metabolism ; Cell Nucleus ; Virus Assembly ; Virus Replication
Chemical Substances	Antiviral Agents
Language	English
Publishing date	2023-02-14
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	306628-9
ISSN	1872-9096 ; 0166-3542
ISSN (online)	1872-9096
ISSN	0166-3542
DOI	10.1016/j.antiviral.2023.105557
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Article ; Online: The Oligomeric Assemblies of Cytomegalovirus Core Nuclear Egress Proteins Are Associated with Host Kinases and Show Sensitivity to Antiviral Kinase Inhibitors.

Kicuntod, Jintawee / Häge, Sigrun / Hahn, Friedrich / Sticht, Heinrich / Marschall, Manfred

Viruses

2022 Volume 14, Issue 5

Abstract: The nucleo-cytoplasmic capsid egress of herpesviruses is a unique regulated process that ensures the efficiency of viral replication and release. For human cytomegalovirus (HCMV), the core of the nuclear egress complex (NEC) consists of the pUL50-pUL53 ... ...

Abstract	The nucleo-cytoplasmic capsid egress of herpesviruses is a unique regulated process that ensures the efficiency of viral replication and release. For human cytomegalovirus (HCMV), the core of the nuclear egress complex (NEC) consists of the pUL50-pUL53 heterodimer that is able to oligomerize and thus to build hexameric lattices. These structures determine capsid binding and multicomponent protein interaction including NEC-associated host factors. The underlying characteristic of the core NEC formation is based on the N-terminal hook structure of pUL53 that binds into an alpha-helical groove of pUL50, and is thus described as a hook-into-groove interaction. This central regulatory element has recently been validated as a target of antiviral strategies, and first NEC-targeted prototypes of inhibitory small molecules were reported by our previous study. Here, we further analyzed the oligomerization properties of the viral NEC through an approach of chemical protein cross-linking. Findings were as follows: (i) a cross-link approach demonstrated the oligomeric state of the HCMV core NEC using material from HCMV-infected or plasmid-transfected cells, (ii) a Western blot-based identification of NEC-associated kinases using the cross-linked multicomponent NECs was successful, and (iii) we demonstrated the NEC-inhibitory and antiviral activity of specific inhibitors directed to these target kinases. Combined, the results strongly underline the functional importance of the oligomerization of the HCMV-specific NEC that is both phosphorylation-dependent and sensitive to antiviral kinase inhibitors.
MeSH term(s)	Antiviral Agents/metabolism ; Antiviral Agents/pharmacology ; Cytomegalovirus/metabolism ; Humans ; Infant, Newborn ; Viral Proteins/metabolism ; Virus Release ; Virus Replication
Chemical Substances	Antiviral Agents ; Viral Proteins
Language	English
Publishing date	2022-05-11
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v14051021
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Book ; Online ; Thesis: Studies on the human cytomegalovirus kinase−cyclin interaction that determines host regulation and viral replication efficiency

Schuetz, Martin [Verfasser] / Marschall, Manfred [Akademischer Betreuer] / Muller, Yves [Gutachter] / Sticht, Heinrich [Gutachter]

2024

Author's details	Martin Schuetz ; Gutachter: Yves Muller, Heinrich Sticht ; Betreuer: Manfred Marschall
Keywords	Medizin, Gesundheit ; Medicine, Health
Subject code	sg610
Language	English
Publisher	Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU)
Publishing place	Erlangen
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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