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Analysis of mRNA Nuclear Export Kinetics in Mammalian Cells by Microinjection
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Multiple vesiculoviral matrix proteins inhibit both nuclear export and import

J M Petersen1, L S Her, J E Dahlberg

  • 1Department of Biomolecular Chemistry, University of Wisconsin, Madison, WI 53706-1532, USA.

Proceedings of the National Academy of Sciences of the United States of America
|July 12, 2001
PubMed

Insights

Vesicular stomatitis virus matrix (M) proteins inhibit nuclear transport. This function is conserved across related viruses, affecting RNA and protein movement by targeting the nuclear pore complex.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • The matrix (M) protein of vesicular stomatitis virus (VSV) is known to interfere with nuclear transport.
  • Understanding the broader role of M proteins in vesiculovirus infection is crucial for comprehending viral pathogenesis.

Purpose of the Study:

  • To investigate the conservation of nuclear transport inhibitory properties among matrix (M) proteins of different vesiculoviruses.
  • To elucidate the mechanism by which M proteins affect nuclear transport.

Main Methods:

  • Comparative analysis of M proteins from VSV, chandipura virus, and spring viremia carp virus.
  • Expression of M proteins in transfected HeLa cells and assessment of their impact on nuclear transport of various cargoes (mRNA, snRNAs, snRNPs).
  • Site-directed mutagenesis to identify key residues involved in M protein function and localization.

Main Results:

  • M proteins from all three tested vesiculoviruses inhibit nuclear import and export, particularly blocking transport of spliced mRNA, small nuclear RNAs, and small nuclear ribonucleoproteins.
  • Chandipura virus M protein exhibited the strongest inhibitory activity among those that only slowed transport.
  • Active M proteins localized to the nuclear rim, and mutation of a conserved methionine residue abolished both inhibitory activity and nuclear rim targeting.

Conclusions:

  • The nuclear transport inhibitory function of the matrix (M) protein is conserved across vesiculoviruses.
  • Vesiculoviral M proteins likely interact with a common nuclear target, potentially a component of the nuclear pore complex, to exert their inhibitory effects.
  • The nuclear rim localization and conserved methionine residue are critical for M protein-mediated inhibition of nuclear transport.

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