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Envelope proteins of spleen necrosis virus form infectious human immunodeficiency virus type 1 pseudotype vector particles, but fail to incorporate upon substitution of the cytoplasmic domain with that of Gibbon ape leukemia virus.
Journal article

Envelope proteins of spleen necrosis virus form infectious human immunodeficiency virus type 1 pseudotype vector particles, but fail to incorporate upon substitution of the cytoplasmic domain with that of Gibbon ape leukemia virus.

  • Stitz J Institute for Chemical and Bio-Engineering (ICB), Swiss Federal Institute of Technology, Wolfgang-Pauli-Strasse 10, HCI F107, CH-8093 Zurich, Switzerland.
  • Wolfrum N Division of Medical Biotechnology, Paul Ehrlich Institute, Paul-Ehrlich-Strasse 51-59, D-63225 Langen, Germany.
  • Buchholz CJ Division of Medical Biotechnology, Paul Ehrlich Institute, Paul-Ehrlich-Strasse 51-59, D-63225 Langen, Germany.
  • Cichutek K Division of Medical Biotechnology, Paul Ehrlich Institute, Paul-Ehrlich-Strasse 51-59, D-63225 Langen, Germany.
  • 2006-05-13
Published in:
  • The Journal of general virology. - 2006
Animals
Cell Line
Gammaretrovirus
Genetic Vectors
HIV-1
Humans
Leukemia Virus, Gibbon Ape
Recombinant Fusion Proteins
Retroviridae Proteins, Oncogenic
Viral Envelope Proteins
Virion
English The wild-type (wt) envelope (Env) proteins of spleen necrosis virus (SNV), together with the transmembrane (TM) protein fused to antibody domains (scFv), have been used for the generation of stable packaging cell lines releasing pseudotyped cell targeting vectors derived from SNV and Murine leukemia virus (MLV). As a first step towards assessing whether HIV-1(SNV/TM-scFv) packaging cells could be established for the production of lentiviral cell targeting vectors, it is reported here that infectious HIV-1-derived particles pseudotyped with wt SNV Env proteins could be generated. Using novel chimeric SNV-derived Env proteins encompassing wt and engineered cytoplasmic domains (C-tail) of the Gibbon ape leukemia virus (GaLV) TM protein, it was further shown that the wt C-tail not only excludes the GaLV TM protein from incorporation into HIV-1 particles, but confers this phenotype to other retroviral envelopes upon C-terminal fusion.
Language
  • English
Open access status
bronze
Identifiers
Persistent URL
https://sonar.ch/global/documents/139766
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