Isolation and Characterization of Temperature-Sensitive Mutants of Vesicular Stomatitis Virus, New Jersey Serotype

113

Vesicular stomatitis virus contains a phosphorylated NS protein which is necessary along with L protein and RNP template for transcription of mRNA. To further define the structure of the NS protein and its function in transcription and replication, virion NS was purified and separated into two different phosphorylated forms (NSI and NSII) on DEAE-cellulose columns. Cytoplasmic preparations of NS contained one phosphorylated species which eluted from the column in the same place as the virion NSI. When electrophoresed in sodium dodecyl sulfate-polyacrylamide gels containing urea, NSI and NSII each resolved into two components, whereas cell NS migrated as a single band. NSI and cell NS exhibited little activity in a reconstituted transcription assay, whereas the more highly phosphorylated NSII was very active in the same system. Addition of NSI or cell NS to a transcription system containing NSII resulted in even higher levels of activity, indicating that the various NS species might have different enzymatic functions.

Section: /~~~~~~~~Ns 11 Nsimentioning

confidence: 99%

Transcriptional activities of different phosphorylated species of NS protein purified from vesicular stomatitis virions and cytoplasm of infected cells

Kingsford¹,

Emerson²

1980

113

“…We have been studying the process of replication, using VSV as a model system. Our approach is based on analyses of temperature-sensitive (ts) mutants of the New Jersey serotype of VSV (20). It has been demonstrated that representatives of two of the six nonoverlapping complementation groups (Al and El) can transcribe but are unable to replicate their RNA at the restrictive temperature in vivo (13).…”

mentioning

confidence: 99%

Proposed replicative role of the NS polypeptide of vesicular stomatitis virus: structural analysis of an electrophoretic variant

Lesnaw¹,

Dickson²,

Curry³

1979

RI, the El revertant RI; R2, the El revertant R2; +, the New Jersey wild type; R5, the El revertant R5; R6, the El revertant R6; +, the New Jersey wild type; El, the ts mutant El. The identification of the structural proteins is given on the right. The designations are from top to bottom: L, the large protein required for transcription (molecular weight, 190,000); G, the surface glycoprotein (molecular weight, 70,000); NS, the phosphorylated protein required for transcription; N, the structural protein of the ribonucleoprotein core (molecular weight, 50,000); X, a minor phosphorylated component; and M, the matrix protein (molecular weight, 30,000).

“…However, VSNJ strains Ogden and Missouri showed RNA base sequence homology of only 25% compared to >90% homology between RNAs of the Ogden and Concan strains (17). Most investigators appear to use Ogden and Concan VSNJ wildtype virus, although all current temperature-sensitive (ts) mutants of VSNJ virus are derived from the Glasgow passage of the Missouri strain (14). To minimize confusion in comparing data emanating from different laboratories, it seemed essential to determine the degree of relatedness among standard isolates of the New Jersey serotype of VS virus.…”

mentioning

confidence: 99%

Classification of the New Jersey serotype of vesicular stomatitis virus into two subtypes

Reichmann¹,

Schnitzlein²,

Bishop³

et al. 1978

We propose a reclasification of five strains of the New Jersey serotype of vesicular stomatitis virus into two subtypes designated Concan and Hazelhurst. This subclassification into two subtypes is based on reciprocal differences in antibody neutralization of virion infectivity, nucleotide base sequence homology, oligonucleotide maps of virion RNA, and interference by defective-interfering particles.