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The effect of monensin on virion production and protein secretion in pseudorabies virus-infected cells
Abstract:
The effects of monensin on cells infected with pseudorabies virus have been studied. Treatment with monensin (1 microM) prevented the secretion of the 89K pseudorabies virus-induced sulphated glycoprotein. A polypeptide with a mol. wt. of 78K was secreted into the medium from monensin-treated BSC-1 cells. Mannose labelling showed that initial glycosylation proceeded normally in the presence of monensin, although the absence of fucose label revealed that the later stages in processing were blocked. No intracellular accumulation of virus-induced proteins was found in monensin-treated cells. Infectivity assays, measurement of thymidine-labelled particles and electron microscopy showed that monensin blocked the release of virus particles from cells, although viral morphogenesis was unaffected.
Insights
Monensin treatment blocks pseudorabies virus release from cells by inhibiting glycoprotein processing. Viral morphogenesis remains unaffected, but infectious particle secretion is halted.
Area of Science:
- Virology
- Cell Biology
- Biochemistry
Background:
- Pseudorabies virus (PRV) infection impacts cellular processes.
- Viral glycoproteins are crucial for PRV pathogenesis.
- Understanding viral protein processing is key to developing antivirals.
Purpose of the Study:
- To investigate the effects of monensin on PRV-infected cells.
- To determine how monensin affects viral glycoprotein secretion and processing.
- To assess monensin's impact on PRV particle release and infectivity.
Main Methods:
- Treatment of BSC-1 cells with monensin (1 microM) during PRV infection.
- Analysis of secreted and intracellular viral proteins using molecular weight markers.
- Glycosylation analysis using mannose and fucose labeling.
- Viral infectivity assays, measurement of thymidine-labeled particles, and electron microscopy.
Main Results:
- Monensin prevented secretion of the 89K PRV-induced glycoprotein.
- A 78K polypeptide was secreted from monensin-treated cells.
- Initial glycosylation was normal, but later processing stages were blocked (fucose label absent).
- No intracellular accumulation of viral proteins was observed.
- Monensin blocked virus particle release without affecting viral morphogenesis.
Conclusions:
- Monensin inhibits PRV glycoprotein processing and blocks virus particle release.
- The drug affects later stages of glycoprotein maturation.
- Monensin is a potential agent for controlling PRV spread by preventing infectious virion secretion.