Immediate protection of mice from lethal wild-type Sendai virus (HVJ) infections by a temperature-sensitive mutant, HVJpi, possessing homologous interfering capacity

Kiyotani, Katsuhiro; Takao, Shinichi; Sakaguchi, Takemasa; Yoshida, Takemi

doi:10.1016/0042-6822(90)90460-9

Cited by 46 publications

(45 citation statements)

References 16 publications

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“…LLC-MK 2 and CV1 cells were grown in Eagle's minimal essential medium supplemented with 10% fetal calf serum. Wild-type SeV derived from a cDNA of the Z strain (16) and its 4C(Ϫ) mutant virus, in which all four C proteins were knocked out (20), were propagated in embryonated chicken eggs, and infectivity was measured using an immunofluorescent infectious focus assay (19) and expressed as cell infectious units (CIU)/milliliter.…”

Section: Methodsmentioning

confidence: 99%

AIP1/Alix Is a Binding Partner of Sendai Virus C Protein and Facilitates Virus Budding

Sakaguchi

Kato

Sugahara

et al. 2005

J Virol

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Section: Methodsmentioning

confidence: 99%

AIP1/Alix Is a Binding Partner of Sendai Virus C Protein and Facilitates Virus Budding

Sakaguchi

Kato

Sugahara

et al. 2005

J Virol

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“…Recombinant SeV derived from the genomic cDNA of the Z strain (7) was propagated in embryonated chicken eggs, and infectivity was measured by an immunofluorescent infectious focus assay (8) and expressed as cell infectious units (CIU)/ml. Vesicular stomatitis virus (VSV) New Jersey serotype was propagated in CV1 cells, and infectivity was determined by a plaque assay using CV1 cells.…”

Section: Methodsmentioning

confidence: 99%

“…MG132 (z-Leu-Leu-Leu-H) was purchased from Calbiochem (La Jolla, Calif., U.S.A.), and lactacystin (N-acetyl-L-cysteine) and zLL (z-Leu-Leu-H) were purchased from Peptide Institute (Osaka, Japan). Anti-SeV rabbit serum is described in (8), and anti-F monoclonal antibody F881 and anti-HN monoclonal antibody HN892 are described in (20). Anti-M rabbit serum was provided by Makoto Inoue (DNAVEC Corporation, 6) and anti-C serum was provided by Atsushi Kato (National Institute of Infectious Diseases, Japan).…”

Section: Methodsmentioning

confidence: 99%

Cell‐Specific Inhibition of Paramyxovirus Maturation by Proteasome Inhibitors

Watanabe

Tanaka²,

Shimazu

et al. 2005

Microbiology and Immunology

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Effects of proteasome inhibitors on the replication of a paramyxovirus in comparison with the effects on replication of an orthomyxovirus and rhabdovirus were investigated. Treatment of Sendai virus (SeV)‐infected LLC‐MK2 cells with 50 μM MG132 reduced virus growth to ca. 1/10,000, and treatment with different concentrations of MG132 reduced virus growth in a dose‐dependent manner. Released amounts of viral proteins were reduced in correspondence with decrease in infectivity. The inhibition of virus maturation was confirmed by an SeV‐like particle formation system. Lactacystin also impaired SeV growth and zLL impaired the growth to a lesser extent, suggesting involvement of proteasomes in the restriction of virus growth. In the presence of MG132, localizations of the M protein and viral F and HN glycoproteins on the cell membrane appeared to be partly dissociated, although the viral glycoproteins were normally transported to the cell surface. These results suggest that an early step of SeV assembly was disturbed by proteasome inhibitors. The relationship of the results with ubiquitin is also discussed. SeV maturation was less susceptible and resistant to MG132 in CV1 cells and A549 cells, respectively, indicating cell specificity of the drug effect. Release of vesicular stomatitis virus also showed high susceptibility to MG132 and release of influenza virus A/WSN/33 was only mildly susceptible to the drug in LLC‐MK2 cells. Effects of proteasome inhibitors on virus maturation are thus highly cell‐specific and partly virus‐specific.

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“…At various hours(h) post-infection (p.i. ), the culture media were assayed for CIU and HAU as described (Kiyotani et al 1990). Plaque assays on CV1 cells were carried out with agar overlay medium containing the same amount of trypsin (Kato et al 1996).…”

Section: Cell Cultures and Virus Infectionmentioning

confidence: 99%

Sendai virus C proteins are categorically nonessential gene products but silencing their expression severely impairs viral replication and pathogenesis

et al. 1998

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Background: The P/C mRNA of Sendai virus (SeV), a prototypic member of the family Paramyxoviridae in the Mononegavirales superfamily comprising a large number of nonsegmented negative strand RNA viruses, encodes a nested set of accessory proteins, C 0 , C, Y1 and Y2, referred to collectively as C proteins, initiating, respectively, at ACG/81 and AUGs/114, 183, 201 in the þ1 frame relative to the ORF of phospho (P) protein, the smaller subunit of RNA polymerase. Among them, C is the major species expressed in infected cells at a molar ratio which is several-fold higher than the other three. However, their function has remained an enigma. It has not even been established whether or not the C proteins are essential for viral replication. Many other viruses in Mononegavirales encode C-like proteins, but their roles also remain to be defined.

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Immediate protection of mice from lethal wild-type Sendai virus (HVJ) infections by a temperature-sensitive mutant, HVJpi, possessing homologous interfering capacity

Cited by 46 publications

References 16 publications

AIP1/Alix Is a Binding Partner of Sendai Virus C Protein and Facilitates Virus Budding

AIP1/Alix Is a Binding Partner of Sendai Virus C Protein and Facilitates Virus Budding

Cell‐Specific Inhibition of Paramyxovirus Maturation by Proteasome Inhibitors

Sendai virus C proteins are categorically nonessential gene products but silencing their expression severely impairs viral replication and pathogenesis

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