Abstract
As a large double-stranded DNA virus, herpes simplex virus type 1 (HSV-1) assembles capsids in the nucleus where the viral particles exit by budding through the inner nuclear membrane. Although a number of viral and host proteins are involved, the machinery of viral egress is not well understood. In a search for host interacting proteins of ICP34.5, which is a virulence factor of HSV-1, we identified a cellular protein, p32 (gC1qR/HABP1), by mass spectrophotometer analysis. When expressed, ICP34.5 associated with p32 in mammalian cells. Upon HSV-1 infection, p32 was recruited to the inner nuclear membrane by ICP34.5, which paralleled the phosphorylation and rearrangement of nuclear lamina. Knockdown of p32 in HSV-1-infected cells significantly reduced the production of cell-free viruses, suggesting that p32 is a mediator of HSV-1 nuclear egress. These observations suggest that the interaction between HSV-1 ICP34.5 and p32 leads to the disintegration of nuclear lamina and facilitates the nuclear egress of HSV-1 particles.
Highlights
HSV disrupts nuclear lamina for release from nucleus during productive infection
We report that ICP34.5 targets a cellular protein, p32, known as component 1q receptor (C1qR) or hyaluronic acid-binding protein (HABP1). p32 is an abundant protein primarily located in mitochondrial matrix and associates with a number of cellular proteins including lamin B receptor (LBR) [34]
These results demonstrate a specific interaction between viral protein ICP34.5 and host protein p32 in vitro and in the virus-infected cells
Summary
HSV disrupts nuclear lamina for release from nucleus during productive infection. UL31 is thought to form a complex with UL34 and interact with lamin A/C at the nuclear rim [15, 16], which disrupts the nuclear lamina by interference with lamin-lamin interactions [5] This process involves protein kinase C (PKC), lamin B [12], lamin B receptor (LBR), and emerin [6, 17, 18]. The interaction between ICP34.5 and p32 leads to the redistribution of nuclear lamina and facilitates the nuclear egress of HSV-1 These results suggest that p32 is a novel target for ICP34.5 and plays a significant role in the productive infection of HSV-1
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