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J Gen Virol 87 (2006), 1577-1581; DOI 10.1099/vir.0.81231-0

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© 2006 Society for General Microbiology

Short Communication

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

Jörn Stitz1,2,{dagger}, Nina Wolfrum1,{dagger}, Christian J. Buchholz1 and Klaus Cichutek1

1 Division of Medical Biotechnology, Paul Ehrlich Institute, Paul-Ehrlich-Strasse 51-59, D-63225 Langen, Germany
2 Institute for Chemical and Bio-Engineering (ICB), Swiss Federal Institute of Technology, Wolfgang-Pauli-Strasse 10, HCI F107, CH-8093 Zurich, Switzerland

Correspondence
Jörn Stitz
joern.stitz{at}chem.ethz.ch

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.

{dagger}These authors contributed equally to this work.







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Copyright © 2006 by the Society for General Microbiology.