Newcastle disease virus stimulates the cellular accumulation of stress (heat shock) mRNAs and proteins

P L Collins, L E Hightower
1982 Journal of Virology  
A biological agent, Newcastle disease virus, stimulated the synthesis of stress proteins in cultured chicken embryo cells. Previously, only physical and chemical agents were known to induce these proteins. The levels of translatable stress mRNAs were elevated in cells infected with avirulent or virulent strains; however, stress protein synthesis was stimulated strongly only in cells infected by avirulent strains. As did several other paramyxoviruses, avirulent strains of Newcastle disease virus
more » ... astle disease virus stimulated the synthesis of glucose-regulated proteins as well as stress proteins. Possible stimuli of the synthesis of these two sets of proteins in paramyxovirus-infected cells are considered. Few known cellular proteins are synthesized at increased rates after infections by negativestrand-RNA viruses. The proteins of the interferon system are the most intensely studied example. In addition, Peluso and co-workers (19) have reported that infection of cultured chicken embryo (CE) cells by the paramyxoviruses Sendai virus and simian virus 5 stimulates the synthesis of several abundant cellular polypeptides. One of these was an 86-kilodalton protein which was not characterized further; the others were identified (20) as glucose-regulated, 99-and 78-kilodalton proteins. Glucose-regulated proteins are cellular proteins synthesized in detectable amounts by uninfected cells under normal culture conditions (14) and at increased rates by mutant cell types (13, 15, 21) , during paramyxovirus infection, and in response to glucose starvation (24, 26, 28) and exposure to inhibitors of glycosylation, such as 2-deoxyglucose (21) and tunicamycin (17) . In this report, we show that the accumulation of a second set of proteins and their functional mRNAs in CE cells was stimulated by avian paramyxovirus Newcastle disease virus (NDV) infection. These proteins were identified as the cellular stress (heat shock) proteins. Previously, we (5, 8) and others (9, 11) have demonstrated that stress proteins and their functional mRNAs rapidly accumulate in avian and mammalian cells in response to a variety of stresses, including heat shock, heavy metals, sulfhydryl reagents, amino acid analogs, and tissue explantation. The functions of the stress and glucoseregulated proteins and the mechanisms whereby t Present address:
doi:10.1128/jvi.44.2.703-707.1982 fatcat:rjs3dgdhuzfi3mha2dsw6227rq