Proteomics

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Rabbit haemorrhagic disease virus (RHDV) infected rabbit liver proteome


ABSTRACT: Rabbit haemorrhagic disease virus (RHDV) belongs to the family Caliciviridae, genus Lagovirus and is used in Australia as a biocontrol tool to keep the population of european rabbits low. This virus has a positive-sense single-stranded RNA genome that encodes structural (capsid) and non-structural proteins. Due to the lack of an established cell culture system for this virus, some of the non-structural proteins are yet awaiting characterisation and their function is unknown. This work attempted to characterise the process of RHDV infection and identify pathways that alterate in RHDV-infected rabbit liver at the proteome level. Young rabbits were infected with RHDV2 (genotype GI.1bP-GI.2) and humanely killed 24 hours post-infection. 25% liver homogenates were prepared in RNAlater buffer and stored at -20C. Uninfected rabbit liver samples served as a control. Samples from three RHDV2-infected animals (K375, K376, K378) and three uninfected animals (K3, K14, K12) were used in this study.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Oryctolagus Cuniculus Cuniculus

TISSUE(S): Hepatocyte, Liver, Epithelial Cell

SUBMITTER: Elena Smertina  

LAB HEAD: Tanja Strive

PROVIDER: PXD031027 | Pride | 2022-10-14

REPOSITORIES: Pride

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Publications

Lagovirus Non-structural Protein p23: A Putative Viroporin That Interacts With Heat Shock Proteins and Uses a Disulfide Bond for Dimerization.

Smertina Elena E   Carroll Adam J AJ   Boileau Joseph J   Emmott Edward E   Jenckel Maria M   Vohra Harpreet H   Rolland Vivien V   Hands Philip P   Hayashi Junna J   Neave Matthew J MJ   Liu Jian-Wei JW   Hall Robyn N RN   Strive Tanja T   Frese Michael M  

Frontiers in microbiology 20220707


The exact function(s) of the lagovirus non-structural protein p23 is unknown as robust cell culture systems for the <i>Rabbit haemorrhagic disease virus</i> (RHDV) and other lagoviruses have not been established. Instead, a range of <i>in vitro</i> and <i>in silico</i> models have been used to study p23, revealing that p23 oligomerizes, accumulates in the cytoplasm, and possesses a conserved C-terminal region with two amphipathic helices. Furthermore, the positional homologs of p23 in other cali  ...[more]

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