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Comparative Analysis of the Nuclear Egress Complex in Human Herpesvirus 6A and 6B

Microbiology and Immunology
ABSTRACTHerpesvirus nucleocapsids are transported from the nucleus to the cytoplasm via a conserved process known as nuclear egress, which is mediated by the nuclear egress complex (NEC) consisting of two core viral proteins. Although the NEC structure is conserved among herpesviruses, functional divergence may exist.
Aila Gulijiahani   +3 more
openaire   +1 more source

A cell free protein fragment complementation assay for monitoring the core interaction of the human cytomegalovirus nuclear egress complex

Antiviral Research, 2012
Certain viral protein-protein interactions provide attractive targets for antiviral drug development. Recently, we described a β-lactamase based protein fragment complementation assay (PCA) to study the core interaction of the nuclear egress complex (NEC) of different herpesviruses in cells.
Margit, Schnee   +3 more
openaire   +2 more sources

The conserved core nuclear egress complex (NEC) as an antiherpesviral drug target: Pharmacophore-based identification of NEC-specific inhibitors

Antiviral Research
The nucleocytoplasmic capsid egress of herpesviruses is a uniquely regulated process. As well-established for the human cytomegalovirus (HCMV) core nuclear egress complex (NEC), the pUL50-pUL53 NEC heterodimer oligomerizes and builds hexameric lattices for the regulated nucleocytoplasmic release of viral capsids.
Julia Tillmanns   +12 more
openaire   +2 more sources

The cytomegalovirus nuclear egress complex: compositional and functional characterization leading to an antiviral targeting

2023
The nuclear egress is an essential stage during lytic replication of human cytomegalovirus (HCMV) that regulates the nucleocytoplasmic translocation of viral capsids. The core nuclear egress complex (NEC) consists of two conserved viral proteins, pUL50 and pUL53, and acts as a mediator in the recruitment of a number of NEC-associated viral and cellular
openaire   +1 more source

Functional analysis of herpesviral nuclear egress complexes - determinants of replication efficiency and targets of novel antiviral strategies

2023
Der herpesvirale nukleäre Egress ist ein hoch konservierter Prozess, welcher die nukleocyto-plasmatische Freisetzung von Kapsiden reguliert. Der nukleäre Egress-Komplex (NEC) des humanen Cytomegalovirus (HCMV) ist durch die Hauptproteine (Core) pUL50 und pUL53 definiert, welche oligomerisieren und ein Grundgerüst für die Kapsidbindung und die ...
openaire   +1 more source

Herpesviruses remodel host membranes for virus egress

Nature Reviews Microbiology, 2011
David Johnson, Joel D Baines
exaly  

Studies on two essential viral proteins forming the core nuclear egress complex of human cytomegalovirus

2014
Human cytomegalovirus (HCMV) is characterized by nuclear replication including synthesis of viral DNA and intranuclear formation of capsids. The nucleocytoplasmic export of cytomegaloviral capsids is regulated by formation of a multicomponent nuclear egress complex (NEC) consisting of viral and cellular proteins and essentially based on the viral NEC ...
openaire   +1 more source

Computational Analysis of Herpesviral Nuclear Egress Complexes and the Hapten Binding Antibody B1-8

2019
Proteins have a large impact on how pathogens interact with their host and vice versa. On the pathogen side, this work investigates the nuclear egress complex (NEC) of her pesviruses, which can reshape the inner nuclear membrane (INM) of the host cells and is vital for viral proliferation.
openaire   +1 more source

Characterization of a viral-cellular protein complex which controls the nuclear egress of human cytomegalovirus

2010
Human cytomegalovirus (HCMV) has developed a replication strategy that is well adapted to conditions of the host cell. Notably, after nuclear capsid assembly, HCMV capsids traverse the nuclear envelope for nuclear egress. In this regard, the phosphorylation-mediated disassembly of the nuclear lamina is believed to be a prerequisite for the budding of ...
openaire   +1 more source

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