Herpes simplex virus infection causes the accumulation of a heat-shock protein.

Abstract

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.

Abnormal Forms of the Herpes Simplex Virus Immediate Early Polypeptide Vmw175 Induce the Cellular Stress Response

“…Other published examples of cellular gene activation by HSV were observed after infection with wt virus (LaThangue et al, 1984;Everett, 1985;Kennedy et al, 1985;Patel et aL, 1986), suggesting that they represent a different phenomenon from that reported here. The induction of the stress response by viruses other than HSV also appears to involve a different mechanism, since wt viruses mediate the effect.…”

“…The stimuli include infection with bacteriophage or other viruses (Hightower & Smith, 1978;Peluso et al, 1978;Collins & Hightower, 1982;Drahos & Hendrix, 1982;Nevins, 1982;Notarianni & Preston, 1982;Garry et al, 1983;Khandjian & Turler, 1983;LaThangue et al, 1984). Although the precise function of the stress response or the stress proteins themselves is unclear, it is thought that the stress response has a protective role, since stressed cells can more readily withstand a subsequent exposure to the agents which induced the response (Li & Werb, 1982;Schlesinger, 1986).…”

“…Of the mutants used, only tsK, tsD and tsT, which have mutations in the gene encoding the IE polypeptide Vmw175 (Preston, 1981), induced the response, and this was the first demonstration that HSV can activate cellular gene expression. Subsequent studies have shown that infection with wild-type (wt) HSV type 2 (HSV-2) infection induces the synthesis of minor cellular stress proteins (LaThangue et al, 1984;Kennedy et al, 1985;Patel et al, 1986), and that the synthesis 0000-7735 © 1987 SGM of these proteins is stably increased in cells transformed by HSV (Macnab et al, 1985).…”

The GGTCA palindrome and cognate cellular factors in trans-regulation of human immunodeficiency virus long terminal repeat by herpes simplex virus

“…We believe that the 120K protein is a distinct species rather than a multimer consisting of the lower Mr proteins, since (i) it did not complex with NRE(H) which binds the lower M r proteins, and (ii) it was detected in NRE(P) complexes with HSV-1-infected cell extracts in which p59 and p64 are down-regulated. The HSV-l-induced p50 protein may be a member of the heat-shock protein family that is induced by HSV-1 infection even in the absence of DNA synthesis (LaThangue et al, 1984). We assume that down-regulation of the p37 and p59/p64 species is mediated by HSV virion host shutoff proteins (Read & Frenkel, 1983) whereas induction of the p50 species involves the trans-activating immediate early (IE) genes, directly or through interaction with other cellular factors (Feldman et al, 1982;LaThangue & Latchman, 1987).…”

Expression of the SmB′ splicing protein in rodent cells capable of following an alternative RNA splicing pathway

“…Equal amounts of protein from each sample were then electrophoresed on 12.5070 polyacrylamide SDS gels, transferred to nitrocellulose and reacted with antibody as described [14]. Monoclonal antibody KSm5 [12], which detects the StuB and B' proteins was used as the first layer and peroxidase conjugated rabbit anti-mouse immunoglobulin as the second layer.…”