Rhabdovirus Biology and Infection

Wagner, Robert R.

doi:10.1007/978-1-4684-7032-1_2

Cited by 66 publications

(66 citation statements)

References 252 publications

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“…PCR products were digested with MfeI and StuI and ligated into the similarly cut vector, pGEX-2T-OM. pGEX-OM (48)(49)(50)(51)(52)(53)(54)(55)(56)(57)(58)(59)(60)(61)(62), encoding amino acids 48 to 62 of M protein fused to the C terminus of GST, was made by ligation of complementary oligonucleotides containing the appropriate ends with pGEX-2T plasmid DNA linearized with the same restriction enzymes.…”

Section: Methodsmentioning

confidence: 99%

“…Infection of cells by VSV, a negative-strand RNA virus that replicates in the cytoplasm, results in rapid shutoff of cellular gene expression (59) and snRNA processing (18). The M protein, a major structural component of the VSV virion, plays a central role both in the inhibition of host cell gene expression (5,42) and in viral assembly (59).…”

mentioning

confidence: 99%

“…The M protein, a major structural component of the VSV virion, plays a central role both in the inhibition of host cell gene expression (5,42) and in viral assembly (59). These two properties are genetically separable from each other (6,8,37) in that methionine 51 (Met-51) of the M protein is required for inhibition of host cell gene expression, but not for viral assembly, whereas amino acids 4 to 21 are needed for viral assembly but not for inhibition of host cell gene expression.…”

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confidence: 99%

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The Matrix Protein of Vesicular Stomatitis Virus Inhibits Nucleocytoplasmic Transport When It Is in the Nucleus and Associated with Nuclear Pore Complexes

Petersen

Her

Varvel

et al. 2000

Molecular and Cellular Biology

166

184

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The matrix (M) protein of vesicular stomatitis virus (VSV) is a potent inhibitor of bidirectional nuclear transport. Here we demonstrate that inhibition occurs when M protein is in the nucleus of Xenopus laevis oocytes and that M activity is readily reversed by a monoclonal antibody (␣M). We identify a region of M protein, amino acids 51 to 59, that is required both for inhibition of transport and for efficient recognition by ␣M. When expressed in transfected HeLa cells, M protein colocalizes with nuclear pore complexes (NPCs) at the nuclear rim. Moreover, mutation of a single amino acid, methionine 51, eliminates both transport inhibition and targeting to NPCs. We propose that M protein inhibits bidirectional transport by interacting with a component of the NPC or an NPC-associated factor that participates in nucleocytoplasmic transport.Trafficking of large macromolecules (more than 50 kDa) between the nucleus and the cytoplasm occurs through nuclear pore complexes (NPCs) via signal-dependent, carrier-mediated processes (reviewed in references 39 and 54). This transport is subject to control in response to a variety of stimuli such as progression through the cell cycle, exposure to stress, and infection by viruses (reviewed in reference 39). Thus, control of nucleocytoplasmic transport is an important element in the regulation of gene expression.Much of the carrier-mediated movement through NPCs requires cargo-specific transport receptors called importins and exportins (or karyopherins), which are members of the importin ␤ superfamily of proteins (16,21,45,61). Transport receptors can bind their cargoes either directly or via specialized adapter proteins. For example, importin ␤ mediates import of proteins containing basic nuclear localization sequences and small nuclear ribonucleoproteins (snRNPs) using the adapter proteins importin ␣ (1) and snurportin (28, 43), respectively. Importin ␤ can also interact directly with import cargoes, such as cyclin B (40, 53) and certain ribosomal proteins (30). CRM1 (Exportin1) mediates the export of proteins containing leucine-rich nuclear export signals (NES) as well as unspliced viral mRNAs and pre-snRNAs that are bound to specific NEScontaining adapter proteins (14,17,51,57). Exportin-t binds directly to its RNA export cargo, tRNA (3, 33).Directionality of nuclear transport appears to be governed largely by Ran, a small GTPase that is a central component of most known nucleocytoplasmic transport pathways (reviewed in references 9 and 41). Owing to the asymmetric localization of the Ran effector proteins RanGAP (the GTPase activating protein in the cytoplasm) and RCC1 (the guanine nucleotide exchange factor in the nucleus), a steep concentration gradient of RanGTP is presumed to exist across the nuclear envelope (29). This gradient plays a pivotal role in nucleocytoplasmic transport by triggering both assembly and disassembly of receptor-cargo complexes in the appropriate subcellular compartment (60). Thus, import complexes assemble in the cytoplasm in the absence of RanG...

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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The Matrix Protein of Vesicular Stomatitis Virus Inhibits Nucleocytoplasmic Transport When It Is in the Nucleus and Associated with Nuclear Pore Complexes

Petersen

Her

Varvel

et al. 2000

Molecular and Cellular Biology

166

184

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“…Vesicular stomatitis virus (VSV) is an enveloped negative strand RNA virus that belongs to the rhabdovirus family (Wagner, 1987). Five proteins are encoded by the viral genome, three of which (N, NS and L) are associated with the RNA to constitute the ribonucleoprotein core (RNP).…”

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confidence: 99%

Genetic evidence for multiple functions of the matrix protein of vesicular stomatitis virus

Coulon

Deutsch

Lafay

et al. 1990

Journal of General Virology

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“…The SNT detects neutralizing antibodies or those directed against the glycoprotein of VS viruses. 10 The ELISA incorporates the nucleoprotein as antigen and thus detects antibodies made against the nucleoprotein. 5 The kappa coefficient indicates how much the observed agreement exceeds that expected by chance alone.…”

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confidence: 99%

Comparison of the Serum Neutralization Test and a Competitive Enzyme-Linked Immunosorbent Assay for the Detection of Antibodies to Vesicular Stomatitis Virus New Jersey and Vesicular Stomatitis Virus Indiana

Alvarado¹,

Dolz²,

Herrero³

et al. 2002

J VET Diagn Invest

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A competitive enzyme-linked immunosorbent assay (C-ELISA) for the detection of antibodies against vesicular stomatitis virus New Jersey (VSV-NJ) and vesicular stomatitis virus Indiana (VSV-IN) was compared with the serum neutralization test (SNT) using 1,106 serum samples obtained from dairy cattle on sentinel study farms in the Poás region of Costa Rica. Kappa coefficients between the C-ELISA and the SNT were 0.8871 (95% confidence interval [CI]: 0.8587–0.9155) and 0.6912 (95% CI: 0.6246–0.7577) for the VSV-NJ and VSV-IN tests, respectively. These results indicate good to excellent agreement between the 2 tests under these conditions.

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Rhabdovirus Biology and Infection

Cited by 66 publications

References 252 publications

The Matrix Protein of Vesicular Stomatitis Virus Inhibits Nucleocytoplasmic Transport When It Is in the Nucleus and Associated with Nuclear Pore Complexes

The Matrix Protein of Vesicular Stomatitis Virus Inhibits Nucleocytoplasmic Transport When It Is in the Nucleus and Associated with Nuclear Pore Complexes

Genetic evidence for multiple functions of the matrix protein of vesicular stomatitis virus

Comparison of the Serum Neutralization Test and a Competitive Enzyme-Linked Immunosorbent Assay for the Detection of Antibodies to Vesicular Stomatitis Virus New Jersey and Vesicular Stomatitis Virus Indiana

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