Multiple Vesiculoviral Matrix Proteins Inhibit Both Nuclear Export and Import

The matrix (M) protein of vesicular stomatitis virus inhibits both nuclear import and export. Here, we demonstrate that this inhibitory property is conserved between the M proteins from two other vesiculoviruses, chandipura virus and spring viremia carp virus. All three M proteins completely block n...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2001-07, Vol.98 (15), p.8590-8595
Main Authors: Petersen, J M, Her, L S, Dahlberg, J E
Format: Article
Language:English
Subjects:
Active Transport, Cell Nucleus
AM protein
Amino Acid Sequence
Animals
Biological Sciences
Cell Nucleus - metabolism
Chandipura virus
Cytoplasm
Freight
Freight transport
HeLa Cells
Humans
Imports
matrix protein
Messenger RNA
Methionine - metabolism
Molecular Sequence Data
Oocytes
Receptors
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
RNA
Sequence Homology, Amino Acid
Small nuclear ribonucleoproteins
Small nuclear RNA
Spring viremia of carp virus
Vesicular stomatitis Indiana virus - genetics
Vesicular stomatitis Indiana virus - metabolism
Vesicular stomatitis virus
Vesiculovirus - genetics
Vesiculovirus - metabolism
Viral Matrix Proteins - genetics
Viral Matrix Proteins - metabolism
Xenopus laevis
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Summary:The matrix (M) protein of vesicular stomatitis virus inhibits both nuclear import and export. Here, we demonstrate that this inhibitory property is conserved between the M proteins from two other vesiculoviruses, chandipura virus and spring viremia carp virus. All three M proteins completely block nuclear transport of spliced mRNA, small nuclear RNAs, and small nuclear ribonucleoproteins and slow the nuclear transport of many other cargoes. In all cases where transport was merely slowed by the M proteins, the chandipura virus M protein had the strongest inhibitory activity. When expressed in transfected HeLa cells, active M proteins displayed prominent association with the nuclear rim. Moreover, mutation of a conserved methionine abolished both the inhibitory activity and efficient targeting of the M proteins to the nuclear rim. We propose that all of the vesiculoviral M proteins associate with the same nuclear target, which is likely to be a component of the nuclear pore complex.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.151240998