Abstract
The UL15, UL28 and UL33 proteins of herpes simplex virus type 1 (HSV-1) are thought to comprise a terminase complex responsible for cleavage and packaging of the viral genome into pre-assembled capsids. Immunofluorescence studies confirmed that shortly after infection with wild-type HSV-1 these three proteins localize to viral DNA replication compartments within the nucleus, identified by the presence of the single-stranded DNA-binding protein, ICP8. In cells infected with either UL28- or UL33-null mutants, the other two terminase proteins also co-localized with ICP8. In contrast, neither UL28 nor UL33 was detectable in replication compartments following infection with a UL15-null mutant, although Western blot analysis showed they were present in normal amounts in the infected cells. Provision of UL15 in a complementing cell line restored the ability of all three proteins to localize to replication compartments. These data indicate that UL15 plays a key role in localizing the terminase complex to DNA replication compartments, and that it can interact independently with UL28 and UL33.
Highlights
Replication of herpes simplex virus type 1 (HSV-1) DNA in infected cells leads to the accumulation of high molecular mass concatemers consisting of genomes arranged in a tandem head-to-tail fashion
The results indicate that the UL15 component is likely to play an important role in localizing the terminase complex to the replication compartments
UL15 (Fig. 1d), UL28 (Fig. 1j) and UL33 (Fig. 1p) were all detectable in discrete areas within infected cell nuclei where they colocalized with ICP8 (Fig. 1f, l, r)
Summary
Replication of herpes simplex virus type 1 (HSV-1) DNA in infected cells leads to the accumulation of high molecular mass concatemers consisting of genomes arranged in a tandem head-to-tail fashion. The mock-infected cells exhibited no signal from channels specific to either ICP8 or the three putative terminase proteins (Fig. 1a–c, g–i, m–o). In HSV-1-infected cell nuclei, discrete foci of ICP8 were evident, consistent with replication compartment formation (Fig. 1e, k, q).
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