Abstract
The La antigen is known to associate, at least transiently, with a series of small nuclear and cytoplasmic ribonucleoprotein particles (snRNPs and scRNPs), e.g. U1 and U6 snRNPs. In CV-1 cells a monoclonal antibody (MAb), directed against the La protein (La1B5), immunostained intranuclear speckles. These speckles were found to co-localize with speckles that were stained by MAbs directed against either all U snRNPs or only against U1 snRNPs. Two h after infection of CV-1 cells with herpes simplex virus type 1 (HSV-1) (strain HFEM) the staining of nuclear speckles with the anti-La MAb disappeared and the La protein was found quantitatively in the cytoplasm. In contrast nuclear speckles remained stained with the MAbs against the U snRNPs. Similar results were obtained using HSV-1 strains Lenette or 17 syn+ or temperature-sensitive (ts) mutants defective either in DNA synthesis (tsS) or in the immediate early protein (Mr 175 K) (tsK). Later in infection the La protein returned to the nucleus. Six h after infection most of the nuclear La protein was found to localize within patchy regions. These areas seem to be related to heterogeneous nuclear RNA transcription and/or processing sites, but not to DNA replication sites.
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