Herpes simplex virus infection causes the accumulation of a heat-shock protein.
A monoclonal antibody, produced from mice immunized with a herpes simplex virus (HSV)-infected cell extract, reacts with a molecule which is present in uninfected cells and which accumulates in large amounts during HSV 2 infection. In uninfected cells this molecule is growth regulated, in that exponentially growing cells have intense nuclear immunofluorescence, whereas confluent quiescent cells have little. It has a mol. wt. of 57 000 (p57) in exponential cells, and one of 61 000 (p61) in quiescent cells. In HSV 2-infected cells, p57 accumulates and nuclear and cytoplasmic immunofluorescence increases. In uninfected cells, p57 also accumulates during heat-shock treatment, and this is associated with a new immunofluorescence throughout the cytoplasm. We suggest that HSV 2 infection induces a cellular stress response which is involved in the shut-off of host cell polypeptide synthesis.
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D002460:Cell Line; D002467:Cell Nucleus / Q000032:analysis; D006224:Cricetinae; D004622:Embryo, Mammalian; D005347:Fibroblasts / Q000032:analysis / Q000502:physiology; D005455:Fluorescent Antibody Technique; D006360:Heat-Shock Proteins / Q000032:analysis*; D006801:Humans; D007668:Kidney; D008647:Mesocricetus; D014176:Protein Biosynthesis; D018139:Simplexvirus / Q000502:physiology*
D000911:Antibodies, Monoclonal; D006360:Heat-Shock Proteins