Genetics of Rhabdoviruses

Pringle, C. R.

doi:10.1007/978-1-4684-2718-9_6

Cited by 30 publications

(31 citation statements)

References 115 publications

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“…This behaviour is due to the fact that alphavirus nucleocapsids interact directly with the transmembranous regions of the homologous glycoproteins El, E2 or both (for reviews, see Brown, 1980;Simons & Garoff, 1980), where VSV nucleocapsids interact specifically with VSV matrix protein lining the cytoplasmic surface of the bilayer. [The interaction of the matrix protein with the outer membrane glycoproteins appears much less specific and VSV particles have been detected with heterologous glycoproteins from alphaviruses, paramyxoviruses and several other groups of enveloped viruses (Pringle, 1977).] Alphavirus glycoproteins and nucleocapsid protein are found in equal molar ratios in the virion, indicating a single interactive site per glycoprotein molecule.…”

Section: Discussionmentioning

confidence: 99%

Mutants of Sindbis Virus. IV. Heterotypic Complementation and Phenotypic Mixing between Temperature-sensitive Mutants and Wild-type Sindbis and Western Equine Encephalitis Viruses

Strauss

Tsukeda

Simizu

1983

Journal of General Virology

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Section: Discussionmentioning

confidence: 99%

Mutants of Sindbis Virus. IV. Heterotypic Complementation and Phenotypic Mixing between Temperature-sensitive Mutants and Wild-type Sindbis and Western Equine Encephalitis Viruses

Strauss

Tsukeda

Simizu

1983

Journal of General Virology

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“…These should probably be less virulent, but we have not yet determined the LDs0 of these mutants in mice. Presumably the rate of generation/amplification of DI particles would be regulated by viral replication/encapsidation genes (Leppert et al, 1977;Huang, 1977) and mutants of viral complementation group I (L protein polymerase gene) are the most abundant mutants of VSV (Pringle, 1970(Pringle, , 1977Szilagyi & Pringle, 1979). Some RNA viruses might generate DI particles extremely rapidly even from common wild-type and mutant strains.…”

Section: Short Communicationmentioning

confidence: 99%

Very Rapid Generation/Amplification of Defective Interfering Particles by Vesicular Stomatitis Virus Variants Isolated from Persistent Infection

DePolo

Holland

1986

Journal of General Virology

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SUMMARYMultiply cloned variants of vesicular stomatitis virus (VSV) were found to generate/amplify defective interfering (DI) particles at a rate greatly exceeding the rates normally observed for wild-type VSV (or for other mutants of VSV). A single undiluted passage of the first clonal pool of this variant virus produced concentrated visible bands of DI particles on sucrose gradients whereas wild-type and other mutant strains of VSV required from three to six or more serial undiluted passages. Since DI particle amplication by wild-type VSV at each undiluted passage can exceed 10000-fold enrichment, these variant virus clones were generating/amplifying DI particles many millions of times more rapidly than were wild-type and other mutant strains of VSV. This rate of generation/amplification is so high that it was not feasible to obtain accurate estimates of the rates of generation (or amplification) of these DI particles. Stampfer et al. (1971) first demonstrated that defective interfering (DI) particles can be eliminated from vesicular stomatitis virus (VSV) stocks by cloning, preferably multiple cloning, of infectious virus. Holland et al. (1976 a) demonstrated that even the first clonal pools prepared from multiply cloned virus are already contaminated with seed quantities of newly generated DI particles, and this was confirmed for both VSV and Sendai virus DI particles

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“…Temperature-sensitive mutants of vesicular stomatitis virus (VSV) serotype New Jersey have been classified into six non-overlapping complementation groups and characterized as replicase-positive or -negative mutants by their ability to synthesize virion RNA in infected cells at the restrictive (39 °C) temperature, and as transcriptase-positive or -negative mutants by their ability to synthesize mRNA species in vitro at 39 °C (Pringle et aI., 1971 ;Pringle, 1977 ;Szil~gyi & Pringle, 1979). Transcriptase-negative mutants have been identified in complementation groups B, E and F (mutants tsB1, tsE1 and tsF1), suggesting the involvement of three viral polypeptides in the transcription process (Szil~gyi & Pringle, 1979).…”

Section: Introductionmentioning

confidence: 99%

Temperature Sensitivity of the Transcriptase of Mutants tsB1 and tsF1 of Vesicular Stomatitis Virus New Jersey Is a Consequence of Mutation Affecting Polypeptide L

Ongrádi

Cunningham

Szilágyi

1985

Journal of General Virology

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SUMMARYTwo condition~il transcriptase-negative mutants of vesicular stomatitis virus (VSV) serotype New Jersey, tsB 1 and tsF 1, their revertants tsB 1/R 1 and tsF 1/R 1 and the wildtype virus were dissociated into pellet, NS and L fractions and, after reconstitution of these in various combinations, the transcriptase activities were assayed in vitro at the permissive (31 °C) and restrictive (39 °C) temperatures. The pellet fractions contained the virion RNA-polypeptide N complexes, while the NS and L fractions were essentially pure preparations of these polypeptides. The synthesis of RNA by the reconstituted pellet and L fractions was inhibited at 39 °C only when the L fractions of tsB1 or tsFl were used. Addition of the NS fractions to the reconstituted pellet and L fractions did not alter the rates of RNA synthesis. These results demonstrate that polypeptide L is the temperature-sensitive polypeptide of both mutants tsB1 and tsFl and support previous observations that polypeptide L is the transcriptase itself. The fact that a second mutant of complementation group F, tsF2, is transcriptase-positive but replicase-negative suggests that polypeptide L is involved both in transcription and replication. Intracistronic complementations may account for the observation that the temperature-sensitive mutations affect polypeptide L in complementation groups B and F.

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Genetics of Rhabdoviruses

Cited by 30 publications

References 115 publications

Mutants of Sindbis Virus. IV. Heterotypic Complementation and Phenotypic Mixing between Temperature-sensitive Mutants and Wild-type Sindbis and Western Equine Encephalitis Viruses

Mutants of Sindbis Virus. IV. Heterotypic Complementation and Phenotypic Mixing between Temperature-sensitive Mutants and Wild-type Sindbis and Western Equine Encephalitis Viruses

Very Rapid Generation/Amplification of Defective Interfering Particles by Vesicular Stomatitis Virus Variants Isolated from Persistent Infection

Temperature Sensitivity of the Transcriptase of Mutants tsB1 and tsF1 of Vesicular Stomatitis Virus New Jersey Is a Consequence of Mutation Affecting Polypeptide L

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