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Differential stability of host mRNAs in Friend erythroleukemia cells infected with herpes simplex virus type 1
Abstract:
The consequences of herpes simplex virus type 1 infection on cellular macromolecules were investigated in Friend erythroleukemia cells. The patterns of protein synthesis, examined by polyacrylamide gel electrophoresis, demonstrated that by 4 h postinfection the synthesis of many host proteins, with the exception of histones, was inhibited. Examination of the steady-state level of histone H3 mRNA by molecular hybridization of total RNA to a cloned mouse histone H3 complementary DNA probe demonstrated that the ratio of histone H3 mRNA to total RNA remained unchanged for the first 4 h postinfection. In contrast, the steady-state levels of globin and actin mRNAs decreased progressively at early intervals postinfection. Studies on RNA synthesis in isolated nuclei demonstrated that the transcription of the histone H3 gene was inhibited to approximately the same extent as that of actin gene. We concluded that the stabilization of preexisting histone H3 mRNA was responsible for the persistence of H3 mRNA and histone protein synthesis in herpes simplex virus type 1-infected Friend erythroleukemia cells. The possible mechanisms influencing the differential stability of host mRNAs during the course of productive infection with herpes simplex virus type 1 are discussed.
Insights
Herpes simplex virus type 1 (HSV-1) infection inhibits host protein synthesis but not histone production. This is due to the stabilization of histone H3 mRNA, preventing its degradation during infection.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Herpes simplex virus type 1 (HSV-1) infection significantly impacts host cell functions.
- Understanding how viral infections alter cellular macromolecule synthesis is crucial for comprehending viral pathogenesis.
Purpose of the Study:
- To investigate the effects of HSV-1 infection on cellular macromolecules in Friend erythroleukemia cells.
- To elucidate the mechanisms behind the differential regulation of host protein and mRNA synthesis during HSV-1 infection.
Main Methods:
- Polyacrylamide gel electrophoresis was used to analyze protein synthesis patterns.
- Molecular hybridization with a cloned mouse histone H3 complementary DNA probe assessed histone H3 mRNA levels.
- RNA synthesis was studied in isolated nuclei to examine gene transcription.
Main Results:
- HSV-1 infection inhibited the synthesis of most host proteins, excluding histones, within 4 hours postinfection.
- While globin and actin mRNA levels decreased, histone H3 mRNA levels remained stable for the initial 4 hours.
- Transcription of both histone H3 and actin genes was similarly inhibited by HSV-1.
Conclusions:
- The persistence of histone H3 mRNA and subsequent histone protein synthesis in HSV-1-infected cells is attributed to mRNA stabilization.
- Differential mRNA stability plays a key role in regulating host macromolecule synthesis during productive HSV-1 infection.