The vaccinia virus 14-kilodalton fusion protein forms a stable complex with the processed protein encoded by the vaccinia virus A17L gene

Rodrı́guez, Dolores; Rodriguez, Juan-Ramon; Esteban, Mariano

doi:10.1128/jvi.67.6.3435-3440.1993

Cited by 74 publications

(60 citation statements)

References 34 publications

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“…3B). A27 (sometimes called the 14kDa fusion protein), is a membrane-associated protein that interacts with the membrane protein A17 (Rodriguez et al, 1993), although A27 is not itself an integral membrane protein. We detected A27 in the both soluble and insoluble fractions following detergent treatment of wt or Cts9 virions grown at 40°C, but A27 was almost entirely soluble following detergent and DTT treatment (Fig.…”

Section: Purified Mature Virions Of Cts6 Produced At Both Permissive mentioning

confidence: 99%

Vaccinia virus temperature-sensitive mutants in the A28 gene produce non-infectious virions that bind to cells but are defective in entry

et al. 2007

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The vaccinia virus temperature-sensitive mutations Cts6 and Cts9 were mapped by marker rescue and DNA sequencing to the A28 gene. Cts6 and Cts9 contain an identical 2-bp deletion truncating the A28 protein and removing the fourth conserved cysteine near the C-terminus. Cts9 mutant virions produced at 40 degrees C were non-infectious and unable to cause cytopathic effect. However, the mutant A28 protein localized to purified mature virions (MV) at 31 degrees C and 40 degrees C. MV of Cts9 produced at 40 degrees C bound to cells but did not enter cells. Low pH treatment of Cts9-infected cells at 18 h p.i. failed to produce fusion from within at 40 degrees C, but gave fusion at 31 degrees C. Adsorption of Cts9 mutant virions to cells followed by low pH treatment showed a defect in fusion from without. The Cts9 phenotype suggests that the A28 protein is involved in both virus entry and cell-cell fusion, and supports the linkage between the two processes.

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Section: Purified Mature Virions Of Cts6 Produced At Both Permissive mentioning

confidence: 99%

Vaccinia virus temperature-sensitive mutants in the A28 gene produce non-infectious virions that bind to cells but are defective in entry

et al. 2007

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“…The localization of the p14 and p32 proteins to wild-type VV has recently been described (42). The peripheral membrane protein p14 (gene A27L) is probably involved in the infection process (31)(32)(33) as well as in the wrapping of IMV by a Golgiderived cisterna to produce the intracellular and extracellular enveloped viruses (34). We have shown by immunoelectron microscopy that in cells infected with wild-type VV, a monoclonal antibody against p14 labels the outer membrane of the IMV and an assembly intermediate between the IV and the IMV (see the introduction), whereas the IV particles are devoid of labelling (42).…”

Section: Vol 69 1995mentioning

confidence: 99%

Characterization of ts 16, a temperature-sensitive mutant of vaccinia virus

Ericsson

Cudmore

Shuman

et al. 1995

J Virol

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We have characterized a temperature-sensitive mutant of vaccinia virus, ts16, originally isolated by Condit et al. (Virology 128:429-443, 1983), at the permissive and nonpermissive temperatures. In a previous study by Kane and Shuman (J. Virol 67:2689-2698, 1993), the mutation of ts16 was mapped to the I7 gene, encoding a 47-kDa protein that shows partial homology to the type II topoisomerase of Saccharomyces cerevisiae. The present study extends previous electron microscopy analysis, showing that in BSC40 cells infected with ts16 at the restrictive temperature (40؇C), the assembly was arrested at a stage between the spherical immature virus and the intracellular mature virus (IMV). In thawed cryosections, a number of the major proteins normally found in the IMV were subsequently localized to these mutant particles. By using sucrose density gradients, the ts16 particles were purified from cells infected at the permissive and nonpermissive temperatures. These were analyzed by immunogold labelling and negative-staining electron microscopy, and their protein composition was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. While the ts16 virus particles made at the permissive temperature appeared to have a protein pattern identical to that of wild-type IMV, in the mutant particles the three core proteins, p4a, p4b, and 28K, were not proteolytically processed. Consistent with previous data the sucrose-purified particles could be labelled with [ 3 H]thymidine. In addition, anti-DNA labelling on thawed cryosections suggested that most of the mutant particles had taken up DNA. On thawed cryosections of cells infected at the permissive temperature, antibodies to I7 labelled the virus factories, the immature viruses, and the IMVs, while under restrictive conditions these structures were labelled much less, if at all. Surprisingly, however, by Western blotting (immunoblotting) the I7 protein was present in similar amounts in the defective particles and in the IMVs isolated at the permissive temperature. Finally, our data suggest that at the nonpermissive temperature the assembly of ts16 is irreversibly arrested in a stage at which the DNA is in the process of entering but before the particle has completely sealed, as monitored by protease experiments.

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“…The A27L protein is multifunctional ( Figure 3A) and is attached to the IMV surface via interactions with proteins A17L and A14L (92,122). It is involved in IMV attachment (19), virus-cell fusion (23), cell-cell fusion (34,44,94), and wrapping of IMV to form IEV.…”

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confidence: 99%

Vaccinia Virus Motility

Smith

Murphy

Law

2003

Annu. Rev. Microbiol.

105

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Vaccinia virus (VV), the virus smallpox vaccine, replicates in the cytoplasm of infected cells. The intracellular movement of this large virus would be inefficient without specific transport mechanisms; therefore, VV uses microtubules for movement during both entry and egress. In addition, the dissemination of virus from infected cells to adjacent cells is promoted by the polymerization of actin beneath cell surface virions to drive virus particles away from the cell. Last, the roles of different VV particles in virus movement within and between hosts are discussed.

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The vaccinia virus 14-kilodalton fusion protein forms a stable complex with the processed protein encoded by the vaccinia virus A17L gene

Cited by 74 publications

References 34 publications

Vaccinia virus temperature-sensitive mutants in the A28 gene produce non-infectious virions that bind to cells but are defective in entry

Vaccinia virus temperature-sensitive mutants in the A28 gene produce non-infectious virions that bind to cells but are defective in entry

Characterization of ts 16, a temperature-sensitive mutant of vaccinia virus

Vaccinia Virus Motility

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