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Review
- Replicating poxviruses for human cancer therapy
- Manbok Kim
- J. Microbiol. 2015;53(4):209-218. Published online April 8, 2015
- DOI: https://doi.org/10.1007/s12275-015-5041-4
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- 24 Crossref
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Abstract
- Naturally occurring oncolytic viruses are live, replicationproficient viruses that specifically infect human cancer cells while sparing normal cell counterparts. Since the eradication of smallpox in the 1970s with the aid of vaccinia viruses, the vaccinia viruses and other genera of poxviruses have shown various degrees of safety and efficacy in pre-clinical or clinical application for human anti-cancer therapeutics. Furthermore, we have recently discovered that cellular tumor suppressor genes are important in determining poxviral oncolytic tropism. Since carcinogenesis is a multi-step process involving accumulation of both oncogene and tumor suppressor gene abnormalities, it is interesting that poxvirus can exploit abnormal cellular tumor suppressor signaling for its oncolytic specificity and efficacy. Many tumor suppressor genes such as p53, ATM, and RB are known to play important roles in genomic fidelity/maintenance. Thus, tumor suppressor gene abnormality could affect host genomic integrity and likely disrupt intact antiviral networks due to accumulation of genetic defects, which would in turn result in oncolytic virus susceptibility. This review outlines the characteristics of oncolytic poxvirus strains, including vaccinia, myxoma, and squirrelpox virus, recent progress in elucidating the molecular connection between oncogene/tumor suppressor gene abnormalities and poxviral oncolytic tropism, and the associated preclinical/clinical implications. I would also like to propose future directions in the utility of poxviruses for oncolytic virotherapy.
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Citations
Citations to this article as recorded by
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- The invariant region I sequence of the adenovirus serotype 2 DNA polymerase influences template specificity during DNA synthesis
- Houng , In Sil
- J. Microbiol. 1998;36(3):222-230.
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Abstract
- Mutants in highly conserved region I (YGDTDS) of the adenovirus serotyope 2 DNA polymerase (Ad Pol) have been shown previously to be defective in assays for initiation and elongation of adenovirus DNA replication in vitro. A selected subset of these mutants was characterized in a number of assays to determine in more detail the nature of the defect that they cause in Ad Pol. The single amino acid substitution in this sequence motif had no detectable effect on binding either to factors required for viral DNA replication or to Ad DNA origin. However, in the deletion mutant mimicking a similar sequence found in the Klenow fragment and in RNA polymerases, binding to Ad DNA origins was reduced. When the nucleotide and template specificity of partially purified mutant Ad Pol proteins was checked there were no significant differences between mutant and wild-type Ad Pols in RNA polymerase assays both on DNA templates and on RNA templates. In reverse transcription assays, both wild type and mutant Ad Pol were inactive, with the exception of a Gly to Met replacement mutant which mimicked the sequence found in reverse transcriptase; this mutant showed low but reproducible levels of reverse transcriptase activity when compared to wt Ad Pol. Taken together, these results suggest that region I may influence template specificity during DNA synthesis, although the single replacement is not sufficient to convert Ad Pol to a reverse transcriptase or an RNA polymerase. Region I probably acts independently of other regions of Ad Pol that are responsible for DNA binding, since mutations in this sequence did not significantly alter adenovirus DNA origin interactions in gel shift assays.
- Expression of Human Mitochondiral Aldehyde Dehydrogenase 2 in Mammalian Cells using Vaccinia Virus-T7 RNA Polymerase
- Kang, Su Min , Yoo, Seung Ku , Lee, Ki Whan
- J. Microbiol. 1999;37(1):41-44.
- 42 View
- 0 Download
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Abstract
- Human mitochondrial aldehyde dehydrogenase 2 (ALDH2) is mainly responsible for oxidation of acetaldehyde generated during alcohol oxidation in vivo. A full-length cDNA of human liver ALDH2 was successfully expressed using a vaccinia virus-T7 RNA polymerase system. The expressed ALDH2 had an enzymatic activity as high as the native human liver ALDH2 enzyme.
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