Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
Filter
  • 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: PEPTIDE ; Germany ; MICROSCOPY ; PATHWAY ; PATHWAYS ; PROTEIN ; PROTEINS ; RELEASE ; DOMAIN ; CONTRAST ; SEQUENCE ; PARTICLES ; virus ; MUTATION ; LINE ; inactivation ; OVEREXPRESSION ; MATRIX PROTEIN ; VIRION RELEASE ; electron microscopy ; MORPHOGENESIS ; ELECTRON-MICROSCOPY ; assembly ; AMINO-ACID ; interaction ; MUTANTS ; STRUCTURAL PROTEINS ; ENV ; VIRAL INFECTIVITY ; ENVELOPE GLYCOPROTEIN ; ROUS-SARCOMA VIRUS ; TSG101
    Abstract: Foamy viruses (FV) are unusual among retroviruses since they require both Gag and Env structural proteins for particle egress. Recently significant progress has been made towards the mechanistic understanding of the viral release process, in particular that of retroviruses, and the viral domains and cellular pathways involved. However little is currently known about domains of FV structural proteins and cellular proteins engaged in this process. By mutational analysis of sequence motifs in prototype FV (PFV) Gag, bearing homology to known late assembly (L) domains, a PSAP motif with L domain function that was functionally interchangeable by heterologous L domains was identified. In contrast the inactivation of a PPPI motif had no significant influence on PFV particle release, although mutant viral particles displayed reduced infectivity. Similarly mutation of an evolutionary conserved YXXL motif revealed no classical L-domain function but resulted in release of noninfectious viruslike particles. Biochemical and electron microscopy analysis demonstrated that these mutant particles incorporated all viral structural proteins but contained aberrantly capsid structures, suggesting a role in capsid assembly for this PFV Gag sequence motif. In line with the mutational analysis, overexpression of dominant negative (DN) mutants and wild-type TSG101 but not the DN mutant of AIP-1/ALIX reduced PFV particle release and infectivity. Furthermore, DN mutants of Vps4A, Vps4B, and CHMP3 inhibited PFV egress and infectivity. Taken together these results demonstrate that PFV, like other viruses, requires components of the vacuolar protein sorting (VPS) machinery for egress and enters the VPS pathway through interaction with TSG101
    Type of Publication: Journal article published
    PubMed ID: 15827161
    Signatur Availability
    BibTip Others were also interested in ...
  • 3
    Keywords: Germany ; SITE ; GENE ; PROTEIN ; PROTEINS ; DOMAIN ; SEQUENCE ; ACID ; virus ; DELETION ; REVERSE-TRANSCRIPTASE ; MUTATION ; DELETIONS ; REGION ; MUTATIONS ; point mutation ; MATRIX PROTEIN ; MURINE LEUKEMIA-VIRUS ; RESIDUES ; assembly ; END ; AMINO-ACID ; MUTANTS ; D RETROVIRUSES ; ENV ; ENV LEADER PROTEIN ; ENVELOPE ; ENVELOPE PROTEIN ; POL PROTEINS ; REPLICATION STRATEGY ; VIRAL INFECTIVITY
    Abstract: Among the Retroviridae, foamy viruses (FVs) exhibit an unusual way of particle assembly and a highly specific incorporation of envelope protein into progeny virions. We have analyzed deletions and point mutants of the prototypic FV gag gene for capsid assembly and egress, envelope protein incorporation, infectivity, and ultrastructure. Deletions introduced at the 3' end of gag revealed the first 297 amino acids (aa) to be sufficient for specific Env incorporation and export of particulate material. Deletions introduced at the 5' end showed the region between as 6 and 200 to be dispensable for virus capsid assembly but required for the incorporation of Env and particle egress. Point mutations were introduced in the 5' region of gag to target residues conserved among FVs from different species. Alanine substitutions of residues in a region between as 40 and 60 resulted in severe alterations in particle morphology. Furthermore, at position 50, this region harbors the conserved arginine that is presumably at the center of a signal sequence directing FV Gag proteins to a cytoplasmic assembly site
    Type of Publication: Journal article published
    PubMed ID: 16160174
    Signatur Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1432-1424
    Keywords: Key words: Detergent — Triton X-100 — Nonidet P-40 — n-Octylglucoside — Sodium deoxycholate — Apoptosis — Caspase — Jurkat T lymphoblast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract. Due to their amphiphilic properties, detergents readily disrupt cellular membranes and cause rapid cytolysis. In this study we demonstrate that treatment of cells with sublytic concentrations of detergents such as Triton X-100, Nonidet P-40, n-octylglucoside and the bile salt sodium deoxycholate induce typical signs of apoptosis including DNA fragmentation and cleavage of poly(ADP-ribose) polymerase molecules. The detergent concentration required for apoptosis was below the critical micellar concentration. Induction of apoptosis was not restricted to human cells but similarly occurred in a variety of other vertebrate cell lines. Unstimulated peripheral blood mononuclear cells were susceptible to apoptosis induction by detergent suggesting that apoptosis in this circumstance is not mediated by CD95. Cell death was not due to influx of calcium from the medium. Apoptosis was blocked and cytolysis prevented by treatment with peptide inhibitors of caspases. These findings suggest a process of apoptosis that is initiated upon nonspecific alterations at the cell membrane level. Physiologic correlates of this process still have to be defined.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...