Proteomics

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SFPQ and KSHV protein ORF11 protein interactomes during lytic KSHV replication


ABSTRACT: The nucleus is a highly structured environment containing multiple membrane-less bodies formed through liquid-liquid phase separation. These provide spatial separation and concentration of specific biomolecules enabling efficient and discrete processes to occur which regulate gene expression. One such nuclear body, paraspeckles, are comprised of multiple paraspeckle proteins (PSPs) built around the architectural RNA, NEAT1_2. Paraspeckle function is yet to be fully elucidated but has been implicated in a variety of developmental and disease scenarios. We demonstrate that Kaposi’s sarcoma-associated herpesvirus (KSHV) drives formation of structurally distinct paraspeckles with a dramatically increased size and altered protein composition that are essential for productive lytic replication. We highlight these virus-induced paraspeckle-like structures form adjacent to virus replication centres, functioning as RNA processing hubs for both viral and cellular transcripts during infection. Notably, we reveal that PSP sequestration into virus-induced paraspeckle-like structures results in increased genome instability during both KSHV and Epstein Barr virus (EBV) infection, implicating their formation in virus-mediated tumorigenesis.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human) Human Gammaherpesvirus 8

TISSUE(S): B Cell, Cell Culture

SUBMITTER: Elena Harrington  

LAB HEAD: Professor Adrian Whitehouse

PROVIDER: PXD048834 | Pride | 2024-11-04

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
131221_Exp1_Fraction_1.raw Raw
131221_Exp1_Fraction_2.raw Raw
131221_Exp1_Fraction_3.raw Raw
131221_Exp1_Fraction_4.raw Raw
131221_Exp2_Fraction_1.raw Raw
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