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

Lesnaw, Judith A.; Dickson, Lesley R.; Curry, Ruth

doi:10.1128/jvi.31.1.8-15.1979

Cited by 33 publications

(11 citation statements)

References 26 publications

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“…Similar complexes of the N and NS proteins in the soluble cytoplasmic fraction of VSV-infected cells are also detected by immunoprecipitation with monospecific anti-NS antisera (21). These observed roles of NS protein in VSV replication are consistent with the previous studies on VSV mutants which established clearly a replicative role of NS protein in the life cycle of VSV (130). It is interesting to note that when the highly conserved C-terminal portion (Fig.…”

Section: In Vitro Systems For Study Of Rhabdoviral Genome Replicationsupporting

confidence: 89%

Transcription and replication of rhabdoviruses.

Banerjee¹

1987

Microbiological Reviews

187

110

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Section: In Vitro Systems For Study Of Rhabdoviral Genome Replicationsupporting

confidence: 89%

Transcription and replication of rhabdoviruses.

Banerjee¹

1987

Microbiological Reviews

187

110

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“…P2, however, is resistant to this unfolding. An analogous situation can be found in the case of the NS polypeptide of vesicular stomatitis virus, where conformational changes have been suggested to explain gel migration differences in the NS phosphoprotein of the class E temperature-sensitive mutants (3,15).…”

Section: Fig 4 Peptide Map Of Some Of the Measles Virusmentioning

confidence: 63%

Measles virus polypeptides in infected cells studied by immune precipitation and one-dimensional peptide mapping

Graves¹

1981

J Virol

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Measles virus does not turn off host cell polypeptide synthesis, making it difficult to precisely identify the polypeptides specified by the virus during the infectious cycle. By using the technique of imnmune precipitation with measlesspecific antisera, the host cell background has been eliminated, and new observations have been made concerning measles virus polypeptides H, P, NP, F, and M. The H polypeptide is first synthesized as a monomer which is processed by further glycosylation and by the formation of disulfide-bonded dimers. Polypeptide P (70,000 daltons) has been found to occur also as a 65,000-dalton molecule, P2, and both forms of the molecule are equally phosphorylated. Polypeptide NP is processed from a cleavage-sensitive form (which undergoes cleavage during the process of isolation to form polypeptide 6 [41,000 daltons]) to a form which is resistant to this cleavage. The fusion and hemolysin polypeptide is first found in the cells as a 55,000-dalton precursor, Fo, which is clearly resolved from the NP polypeptide on gel electrophoresis. The measles virus Fo protein identified in previous reports had not been resolved from the 60,000-dalton NP polypeptide. The M protein occurs in the infected cells as two distinct bands, and, as in the case of Sendai virus, one of these two M protein bands represents a phosphorylated form of the other.

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“…Available evidence suggests that this is true. The ts E-1 mutant has been shown to have a lesion in the NS gene (12, 24,28). NS is present in virions in small amounts (5) suggesting that there is only a single mutation responsible for the temperature-sensitive phenotype.…”

Section: Discussionmentioning

confidence: 99%

Assembly of vesicular stomatitis virus: distribution of the glycoprotein on the surface of infected cells

Jacobs¹,

Penhoet²

1982

J Virol

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This study demonstrates that the glycoprotein of vesicular stomatitis virus clusters in the plasma membrane of infected Chinese hamster lung cells during morphogenesis and suggests that viral nucleocapsids are required for this clustering. A mutant virus (ts E-1) which is temperature sensitive for the synthesis of viral nucleocapsids but not viral membrane proteins was used. The surface distribution of the viral glycoprotein in cells infected by this virus was determined by a specific indirect immunoferritin stain. Early in infection at permissive temperatures, the glycoprotein was randomly distributed on membrane ghosts. Later, clusters of ferritin the size and shape of virus particles were seen. In contrast, ghosts prepared from virus-infected cells maintained at a restrictive temperature always had a random distribution of viral glycoprotein.Integral membrane proteins span the membranes with which they are associated and may participate in significant molecular interactions on both sides of the membrane. In many cases, these proteins are freely diffusible in the plane of the membrane (37). An increasing number of membrane proteins, however, are found to be distributed over the surface of the cell in a nonrandom fashion. For example, Ash et al. (1) have shown that several antibody-patched integral membrane proteins are arranged in linear arrays on the surface of cultured fibroblasts, specific receptor molecules are frequently localized in defined regions of the membrane, and viral glycoproteins of lipid-containing viruses are localized in regions of the membrane active in virus assembly (8). The molecular interactions which lead to the nonrandom distribution of integral proteins are currently under active study in a number of laboratories. Evidence is accumulating which indicates that the linear arrays of membrane proteins visible on the surface of fibroblasts result from interactions of domains of these proteins present on the cytoplasmic surface with elements of the cytoskeleton (1, 14,22). In the case of the best-studied receptor system, that of the low-density lipoproteins, the molecules appear to be inserted into the membrane at random sites and then to migrate laterally in the plane of the membrane until they reach a "coated pit." A domain of the receptor presumed to be on the cytoplasmic side t Present address:

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

Cited by 33 publications

References 26 publications

Transcription and replication of rhabdoviruses.

Transcription and replication of rhabdoviruses.

Measles virus polypeptides in infected cells studied by immune precipitation and one-dimensional peptide mapping

Assembly of vesicular stomatitis virus: distribution of the glycoprotein on the surface of infected cells

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