A cellular protein related to heat-shock protein 90 accumulates during herpes simplex virus infection and is overexpressed in transformed cells.

A monoclonal antibody produced from mice immunized with HSV-infected cell DNA binding proteins reacts with two cell-encoded polypeptides, p90 and p40, synthesized constitutively by many different cell types and expressed at high levels in transformed cells. In uninfected cells heat shock induces a cytoplasmic accumulation of p90 and in agreement with this we show that p90 is related to hsp90. During HSV-2 lytic productive infection, p90 accumulates to very high levels, such accumulation being detectable by 2 h p.i. In infected cells p90 is distributed throughout the cell, and in contrast to uninfected cells, is also located on the cell surface. Infection with HSV-1 strains causes an accumulation of p40, which has an intracellular location and is absent from the cell surface. These results show that HSV lytic infection results in an accumulation of at least two cell-encoded polypeptides, one of which is related to hsp90.