Project description:Biomolecular condensates selectively compartmentalise and organise biomolecules within the crowded cellular milieu, and are instrumental in some disease mechanisms, including aiding RNA virus replication. Upon infection, many RNA viruses form biomolecular condensates that are often referred to as viral factories. The assembly mechanism of these viral factories remains poorly defined, but involves transient, non-stoichiometric protein/RNA interactions, posing challenges for their characterisation. Here we present HDX-MS data of NSP2 and NSP5, in a biomolecular condensate to study the mechanism of condensate assembly.
Project description:We report the human intestinal epithelial host transcriptional response to human enteric virus infection using primary human intestinal enteroids cultures as a model system.
Project description:We have employed a single-cell sequencing approach using the 10x Genomics scRNAseq pipeline to study the effect of maternal antibodies on the response to vaccination in the mesenteric lymph node. Given the ability of maternal antibodies to intefere with sero-conversion to rotatvirus vaccination we hypothesized that maternal antibodies would alter the activation and differentiation of lymphocytes. This study presents data on transcriptome dynamics of the mesenteric lymph node following rotavirus vaccination in the absence or presence of maternal antibodies.
Project description:ChIP peaks were identified in both the human and viral genomes (genome assembly GRCh37 (hg19) and Epstein-Barr virus, Human Herpesvirus 4; GenBank accession KF717093.1).
Project description:<p>Tick-borne encephalitis virus is an enveloped, pathogenic, RNA virus in the family Flaviviridae, genus Flavivirus. Viral particles are formed when the nucleocapsid, consisting of an RNA genome and multiple copies of the capsid protein, buds through the endoplasmic reticulum membrane and acquires the viral envelope and the associated proteins. The coordination of the nucleocapsid components to the sites of assembly and budding are poorly understood. Here, we investigate nucleocapsid assembly by characterizing the interactions of the wild-type and truncated capsid proteins with membranes by using biophysical methods and model membrane systems. We show that capsid protein initially binds membranes via electrostatic interactions with negatively-charged lipids which is followed by membrane insertion. Additionally, we show that membrane-bound capsid protein can recruit viral genomic RNA. We confirm the biological relevance of the biophysical findings by using mass spectrometry to show that purified virions contain negatively-charged lipids. Our results suggest that nucleocapsid assembly is coordinated by negatively-charged membrane patches on the endoplasmic reticulum and that the capsid protein mediates direct contacts between the nucleocapsid and the membrane.</p>