Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • foamy virus  (3)
Keywords
  • 1
    Keywords: CELLS ; CELL ; Germany ; human ; SITE ; SITES ; DISTINCT ; GENE ; GENES ; GENOME ; transcription ; cell line ; FAMILY ; SEQUENCE ; SEQUENCES ; TARGET ; virus ; VECTOR ; PROMOTER ; NUMBER ; CELL-LINE ; leukemia ; LINE ; PCR ; HUMAN GENOME ; REGION ; REGIONS ; ONCOGENE ; SELECTION ; foamy virus ; GENE-THERAPY ; HEMATOPOIETIC STEM-CELLS ; RETROVIRAL VECTORS ; DNA INTEGRATION ; HUMAN-IMMUNODEFICIENCY-VIRUS ; CPG-ISLANDS ; INTEGRATION ; FAMILIES ; CPG ISLANDS ; HIV ; SEVERE COMBINED IMMUNODEFICIENCY ; HIGH-THROUGHPUT ; PROMOTER REGION ; IMMUNODEFICIENCY VIRUS ; LEUKEMIA-VIRUS ; HUMAN-GENOME ; TRANSCRIPTION START REGIONS ; HIV INTEGRASE ; RETROTRANSPOSITION ; RETROVIRAL INTEGRATION ; SITE SELECTION
    Abstract: Integration-site selection by retroviruses and retroviral vectors has gained increased scientific interest. Foamy viruses (FVs) constitute a unique subfamily (Spumavirinae) of the family Retroviridae, for which the integration pattern into the human genome has not yet been determined. To accomplish this, 293 cells were transduced with FV vectors and the integration sites into the cellular genome were determined by a high-throughput method based on inverse PCR. For comparison, a limited number of murine leukemia virus (MLV) and human immunodeficiency virus (HIV) integration sites were analysed in parallel. Altogether, 628 FV, 87 HIV and 141 MLV distinct integration sites were mapped to the human genome. The sequences were analysed for RefSeq genes, promoter regions, CpG islands and insertions into cellular oncogenes. Compared with the integration-site preferences of HIV, which strongly favours active genes, and MLV, which favours integration near transcription-start regions, our results indicate that FV integration has neither of these preferences. However, once integration has occurred into a transcribed region of the genome, FVs tend to target promoter-close regions, albeit with less preference than MLV. Furthermore, our study revealed a palindromic consensus sequence for integration, which was centred on the virus-specific, four-base-duplicated target site. In summary, it is shown that the integration pattern of FVs appears to be unique compared with those of other retroviral genera
    Type of Publication: Journal article published
    PubMed ID: 16603537
    Signatur Availability
    BibTip Others were also interested in ...
  • 2
    Keywords: INHIBITOR ; Germany ; ENZYMES ; GENE ; EFFICIENCY ; DNA ; MECHANISM ; CONTRAST ; BIOLOGY ; MOLECULAR-BIOLOGY ; ACID ; virus ; MUTANT ; NO ; REVERSE-TRANSCRIPTASE ; DIFFERENCE ; ESCHERICHIA-COLI ; resistance ; MUTATION ; MUTATIONS ; REPLICATION ; sensitivity ; foamy virus ; INHIBITORS ; HIV-1 ; molecular biology ; molecular ; RECOMBINANT ; RE ; SUBSTRATE ; ENZYME ; MUTANTS ; ENGLAND ; Escherichia coli ; POLYMERIZATION ; MEDIATED EXCISION ; PRIMER-UNBLOCKING ; RNASE-H ; SELECTIVE EXCISION ; ZIDOVUDINE
    Abstract: Azidothymidine (AZT, zidovudine) is one of the few nucleoside inhibitors known to inhibit foamy virus replication. We have shown previously that up to four mutations in the reverse transcriptase gene of simian foamy virus from macaque (SFVmac) are necessary to confer high resistance against AZT. To characterize the mechanism of AZT resistance we expressed two recombinant reverse transcriptases of highly AZT-resistant SFVmac in Escherichia coli harboring three (K211I, S345T, E350K) or four mutations (K211I, I224T, S345T, E350K) in the reverse transcriptase gene. Our analyses show that the polymerization activity of these mutants is impaired. In contrast to the AZT-resistant reverse transcriptase of HIV-1, the AZT resistant enzymes of SFVmac reveal differences in their kinetic properties. The SFVmac enzymes exhibit lower specific activities on poly(rA)/oligo(dT) and higher K-M-values for polymerization but no change in K-D-values for DNA/DNA or RNA/DNA substrates. The AZT resistance of the mutant enzymes is based on the excision of the incorporated inhibitor in the presence of ATP. The additional amino acid change of the quadruple mutant appears to be important for regaining polymerization efficiency
    Type of Publication: Journal article published
    PubMed ID: 18096624
    Signatur Availability
    BibTip Others were also interested in ...
  • 3
    Keywords: INHIBITOR ; CELL ; Germany ; SITE ; SITES ; GENE ; GENOME ; MECHANISM ; SEQUENCE ; culture ; virus ; ACQUISITION ; REVERSE-TRANSCRIPTASE ; resistance ; MUTATION ; MUTATIONS ; PURIFICATION ; PHENOTYPE ; REPLICATION ; SELECTION ; foamy virus ; POL ; ORDER ; molecular ; ENZYME ; POL PROTEINS ; REPLICATION STRATEGY ; USA ; NOR ; viral ; block ; reverse transcriptase ; NUCLEOTIDE ; viruses ; AZT resistance ; RIBONUCLEASE-H DOMAINS ; TYPE-1 RESISTANT ; ZIDOVUDINE AZT
    Abstract: Azidothymidine (AZT) is a reverse transcriptase (RT) inhibitor that efficiently blocks the replication of spumaretroviruses or foamy viruses (FVs). To more precisely elucidate the mechanism of action of the FV RT enzyme, we generated an AZT-resistant FV in cell culture. Biologically resistant virus was obtained for simian foamy virus from macaque (SFVmac), which was insensitive to AZT concentrations of 1 mM, but not for FVs derived from chimpanzees. Nucleotide sequencing revealed four non-silent mutations in the pol gene. Introduction of these mutations into an infectious molecular clone identified all changes to be required for the fully AZT-resistant phenotype of SFVmac. The alteration of individual sites showed that AZT resistance in SFVmac was likely acquired by consecutive acquisition of pol mutations in a defined order, because some alterations on their own did not result in an efficiently replicating virus, neither in the presence nor in the absence of AZT. The introduction of the mutations into the RT of the closely related prototypic FV (PFV) did not yield an AZT-resistant virus, instead they significantly impaired the viral fitness. (c) 2007 Elsevier Inc. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 17904181
    Signatur Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...