Survival of UV-irradiated vaccinia virus in normal and xeroderma pigmentosum fibroblasts; evidence for repair of UV-damaged viral DNA

Klein, B.; Filon, A.R.; Zeeland, A.A. van; Eb, A. J. Van Der

doi:10.1016/0027-5107(94)90274-7

Cited by 10 publications

(2 citation statements)

References 14 publications

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“…It is well known that poxviruses undergo rapid recombination and mutation events or are inactivated by UV light: e.g. UV light of 254 nm inactivates VACV in drinking water within 20 s (von Brodorotti and Mahnel, 1982;Klein et al., 1994; Tsung et al., 1996; Humlova et al., 2002). Inactivation will differ depending on pH, virus concentration and properties of the water (natural water turbidity, depth, surface, ionic concentration).…”

Section: Discussionmentioning

confidence: 99%

Long‐Lasting Stability of Vaccinia Virus (Orthopoxvirus) in Food and Environmental Samples

Eßbauer

Meyer

Porsch-Özçürümez

et al. 2007

Zoonoses and Public Health

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Poxviruses are known to remain infectious in the scabs of patients for months to years. The aim of this study was to investigate viral stability in storm water, food or gauze spiked with vaccinia virus strain Munich 1 (VACV M1). Storm water, storm water supplemented with either fetal calf serum (FCS) or potting soil was stored at two different temperatures (refrigerator, room temperature; 4 degrees C/25 degrees C). In addition, we analysed the viability of VACV M1 on the surface of bread, salad, sausages and gauze bandages stored at 4 degrees C. Samples were titrated in MA 104 cells and the presence of viral DNA was demonstrated by orthopoxvirus-specific PCRs. After 2 weeks, reisolation of VACV M1 from all kinds of food, bandage and water samples except for storm water supplemented with potting soil was possible. Viral DNA was detected in almost all samples by PCR. Prolonged experiments with VACV M1-spiked storm water and storm water supplemented with FCS revealed that samples kept at 4.5 degrees C are infectious for up to 166 days. Our data demonstrate that VACV M1 has a longlasting stability in water and food. The results obtained during this study should be taken into account for risk assessment calculations for poxvirus transmission. Implying that variola virus and vaccinia virus behave in a similar way, our data call for sophisticated countermeasures in cases of a variola release in biological warfare.

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Section: Discussionmentioning

confidence: 99%

Long‐Lasting Stability of Vaccinia Virus (Orthopoxvirus) in Food and Environmental Samples

Eßbauer

Meyer

Porsch-Özçürümez

et al. 2007

Zoonoses and Public Health

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“…In the case of the TFIIH factor, the core complex of five polypeptides is modified with different proteins for activity in transcription or DNA repair (56). Although the evidence for a vaccinia virus DNA repair system is limited, vaccinia virus can repair its DNA during infection of cells deficient in DNA repair (27), and vaccinia virus-encoded proteins have been identified that could function in a vaccinia virus DNA NER pathway, including a uracil N-glycosylase (55), DNA ligase (26), and DNases that could serve as an apyrimidinic-apurinic endonuclease (58). During NER, a short oligonucleotide containing the DNA damage is excised (12 to 13 nt in prokaryotes, 27 to 29 nt in eukaryotes), the oligonucleotide is removed by a helicase, and the resulting gap is filled in and ligated to complete the repair process (46).…”

Section: Discussionmentioning

confidence: 99%

Vaccinia virus gene A18R encodes an essential DNA helicase

Simpson

Condit

1995

J Virol

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The vaccinia virus A18R protein is a DNA-dependent ATPase that contains the canonical sequence motifs associated with the DEXH group of DNA and RNA helicases. Investigation of A18R protein function during infection indicated it functions in the early and late phases of vaccinia virus transcription. The A18R protein shares sequence similarity with the mammalian DNA helicase ERCC3. The ERCC3 protein has a dual function: it is a component of the transcription factor TFIIH and is an essential participant in the cellular nucleotide excision repair pathway. Here we present evidence that the A18R protein is a DNA helicase that unwinds duplex DNA in a 3-to-5 direction. The A18R helicase was inactive on RNA-DNA and RNA-RNA hybrids. The A18R unwinding activity was most efficient on DNA substrates with lengths of 20 nucleotides or less, and its unwinding activity was not stimulated by the addition of Escherichia coli single-strand-binding protein (SSB), the bacteriophage T4 gene 32 SSB, or the vaccinia virus I3L protein, a putative SSB. We have used an electrophoretic gel mobility shift assay to show that the A18R protein forms a stable complex with single-stranded DNA, and to a lesser extent RNA, in a reaction that does not require ATP.

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