Quantification of the Host Response Proteome after Herpes Simplex Virus Type 1 Infection

Viruses employ numerous host cell
metabolic functions to propagate and manage to evade the host immune
system. For herpes simplex virus type 1 (HSV1), a virus that has evolved
to efficiently infect humans without seriously harming the host in
most cases, the virus–host interaction is specifically interesting.
This interaction can be best characterized by studying the proteomic
changes that occur in the host during infection. Previous studies
have been successful at identifying numerous host proteins that play
important roles in HSV infection; however, there is still much that
we do not know. This study identifies host metabolic functions and
proteins that play roles in HSV infection, using global quantitative
stable isotope labeling by amino acids in cell culture (SILAC) proteomic
profiling of the host cell combined with LC–MS/MS. We showed
differential proteins during early, mid and late infection, using
both cytosolic and nuclear fractions. We identified hundreds of differentially
regulated proteins involved in fundamental cellular functions, including
gene expression, DNA replication, inflammatory response, cell movement,
cell death, and RNA post-transcriptional modification. Novel differentially
regulated proteins in HSV infections include some previously identified
in other virus systems, as well as fusion protein, involved in malignant
liposarcoma (FUS) and hypoxia up-regulated 1 protein precursor (HYOU1),
which have not been identified previously in any virus infection.