Rabies virus protein synthesis in infected BHK-21 cells

Madore, H P; England, James M.

doi:10.1128/jvi.22.1.102-112.1977

Cited by 49 publications

(21 citation statements)

References 50 publications

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“…These numbers are different from values previously determined by biochemical methods (26): molecules per virion-on September 2, 2020 by guest http://mmbr.asm.org/ Downloaded from N = 2,300; NS = 230; L = 60; G = 2,100; and M = 4,700. The polypeptide compositions of fish rhabdoviruses and rabies virus are very similar to that of VSV, except that for rabies virus both Ml (the equivalent of NS) and the nucleocapsid protein (N) appear to be phosphorylated (46,47,59,67,132,225,229,245). The polypeptides of plant rhabdoviruses (58,247), although considerably different in both size and polyacrylamide gel electrophoresis patterns, are similar to animal rhabdoviruses and follow the nomenclature proposed for the latter (Jackson et al, in press).…”

Section: Introductionmentioning

confidence: 65%

Transcription and replication of rhabdoviruses.

Banerjee¹

1987

Microbiological Reviews

187

110

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Section: Introductionmentioning

confidence: 65%

Transcription and replication of rhabdoviruses.

Banerjee¹

1987

Microbiological Reviews

187

110

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“…Slab gel electrophoresis was used to study viral protein synthesis in CER cells infected with the three mutant classes and with the wild type at an MOI of 1 to 2 PFU/cell after 15, 20, and 24 h of incubation at PT and NPT. Cellular protein synthesis was selectively depressed by high-salt treatment (14). Under these conditions, proteins N, Ml, and M2 are clearly visible, whereas proteins L and G are less easily detectable.…”

Section: Resultsmentioning

confidence: 96%

“…Clearly, this numeration gives no indication about the relative amount of mRNA species. It is probable that some are more abundant than the others, since the five viral cistrons may not be transcribed with the same efficiency, depending on their position on the viral genome (9,14).…”

Section: Resultsmentioning

confidence: 99%

Biochemical characterization of temperature-sensitive rabies virus mutants

Saghi¹,

Flamand²

1979

J Virol

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Biochemical characterization of 70 temperature-sensitive (ts) mutants of rabies virus has been done by following the appearance of viral proteins and RNA molecules in infected cells at both permissive and nonpermissive temperature. The presence or absence of the nucleocapsid protein (N) was demonstrated by treating infected cells with anti-N fluorescent antibodies. At 33 degrees C, all the mutants induced a fluorescence comparable to the wild type. At 39.6 degrees C, the mutants can be classified into three groups. Three mutants induced a fluorescence comparable to the wild type (F+ mutants); 54 mutants induced a faint fluorescence which was proportional to the multiplicity of infection and increased with time (F+- mutants). No fluorescence could be detected for the 13 remaining mutants (F- mutants). The synthesis of all viral proteins was shown to be normal for F+ mutants, indicating that transcription and replication of the virus were normal and that the ts lesion was located in a protein which is not directly required for those functions. The synthesis of all viral proteins was similarly decreased for F+- mutants and undetectable for the F- mutants. This suggests that the ts lesion affects the transcription and/or replication of the virus. By annealing techniques it was demonstrated that the F+- mutants were able to perform some amount of secondary transcription at nonpermissive temperature. No secondary transcription occurred with F- mutants. When detectable (i.e., at higher multiplicity of infection), primary transcription of F- mutants was normal.

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“…In contrast to RV neuronal tropism in vivo, laboratorypassaged or fixed strains such as CVS, PV, and ERA bind in vitro to every neuronal or nonneuronal cell line tested so far, regardless of its species of origin (21,31,45,48,50,59), making it impossible to use strategies successfully designed for cloning the receptor(s) for other viruses. These strategies rely on the existence of cell lines nonpermissive for infection and/or virus binding.…”

mentioning

confidence: 99%

Neuronal Cell Surface Molecules Mediate Specific Binding to Rabies Virus Glycoprotein Expressed by a Recombinant Baculovirus on the Surfaces of Lepidopteran Cells

Tuffereau

Benejean

Alfonso

et al. 1998

J Virol

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The existence of specific rabies virus (RV) glycoprotein (G) binding sites on the surfaces of neuroblastoma cells is demonstrated.Spodoptera frugiperda (Sf21) cells expressing G of the RV strain CVS (Gcvs-Sf21 cells) bind specifically to neuroblastoma cells of different species but not to any other cell type (fibroblast, myoblast, epithelial, or glioma). Attachment to mouse neuroblastoma NG108-15 cells is abolished by previous treatment of Gcvs-Sf21 cells with anti-G antibody. Substitutions for lysine at position 330 and for arginine at position 333 in RV G greatly reduce interaction between Gcvs-Sf21 cells and NG108-15 cells. These data are consistent with in vivo results: an avirulent RV mutant bearing the same double mutation is not able to infect sensory neurons or motoneurons (P. Coulon, J.-P. Ternaux, A. Flamand, and C. Tuffereau, J. Virol. 72:273–278, 1998) after intramuscular inoculation into a mouse. Furthermore, infection of NG108-15 cells by RV but not by vesicular stomatitis virus leads to a reduction of the number of binding sites at the neuronal-cell surface. Our data strongly suggest that these specific attachment sites on neuroblastoma cells represent a neuronal receptor(s) used by RV to infect certain types of neurons in vivo.

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Rabies virus protein synthesis in infected BHK-21 cells

Cited by 49 publications

References 50 publications

Transcription and replication of rhabdoviruses.

Transcription and replication of rhabdoviruses.

Biochemical characterization of temperature-sensitive rabies virus mutants

Neuronal Cell Surface Molecules Mediate Specific Binding to Rabies Virus Glycoprotein Expressed by a Recombinant Baculovirus on the Surfaces of Lepidopteran Cells

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