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VSV disrupts the Rae1/mrnp41 mRNA nuclear export pathway
Paula A Faria1, Papia Chakraborty, Agata Levay
1Department of Molecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, FL 33136, USA.
Molecular Cell
|January 5, 2005
Summary
Vesicular stomatitis virus (VSV) matrix (M) protein blocks host mRNA export by binding Rae1. Upregulating Rae1 reverses this inhibition, revealing a viral strategy and potential therapeutic target.
Area of Science:
- Molecular Biology
- Virology
- Cell Biology
Background:
- Viruses can disrupt host cell functions by interfering with nucleocytoplasmic transport.
- The matrix (M) protein of vesicular stomatitis virus (VSV) is known to inhibit host mRNA nuclear export, but the mechanism is unclear.
Purpose of the Study:
- To elucidate the mechanism by which VSV M protein inhibits host mRNA nuclear export.
- To investigate the role of the mRNA export factor Rae1 in this process.
Main Methods:
- Binding assays to determine interaction between VSV M protein and Rae1.
- Analysis of mRNA export in cells expressing wild-type or mutant M protein.
- Assessment of Rae1 expression levels and its effect on M protein-induced inhibition.
Main Results:
- VSV M protein directly binds to the mRNA export factor Rae1.
- A mutant M protein unable to bind Rae1 does not inhibit mRNA nuclear export.
- Increased Rae1 expression fully rescues mRNA export inhibition caused by M protein or VSV infection.
- Rae1 expression is induced by interferon-gamma, a key antiviral cytokine.
Conclusions:
- VSV M protein inhibits host mRNA nuclear export by disrupting Rae1 function.
- Induction of Rae1 expression, such as by interferon-gamma, can overcome VSV-mediated inhibition of mRNA export.