TY - JOUR
T1 - Directed evolution of retrovirus envelope protein cytoplasmic tails guided by functional incorporation into lentivirus particles
AU - Merten, Christoph A.
AU - Stitz, Jörn
AU - Braun, Gundula
AU - Poeschla, Eric M.
AU - Cichutek, Klaus
AU - Buchholz, Christian J.
PY - 2005/1
Y1 - 2005/1
N2 - In contrast to most gammaretrovirus envelope proteins (Env), the Gibbon ape leukemia virus (GaLV) Env protein does not mediate the infectivity of human immunodeficiency virus type 1 (HIV-1) particles. We made use of this observation to set up a directed evolution system by creating a library of GaLV Env variants diversified at three critical amino acids, all located around the R-peptide cleavage site within the cytoplasmic tail. This library was screened for variants that were able to functionally pseudotype HIV-1 vector particles. All selected Env variants mediated the infectivity of HIV-1 vector particles and encoded novel cytoplasmic tail motifs. They were efficiently incorporated into HIV particles, and the R peptide was processed by the HIV protease. Interestingly, in some of the selected variants, the R-peptide cleavage site had shifted closer to the C terminus. These data demonstrate a valuable approach for the engineering of chimeric viruses and vector particles.
AB - In contrast to most gammaretrovirus envelope proteins (Env), the Gibbon ape leukemia virus (GaLV) Env protein does not mediate the infectivity of human immunodeficiency virus type 1 (HIV-1) particles. We made use of this observation to set up a directed evolution system by creating a library of GaLV Env variants diversified at three critical amino acids, all located around the R-peptide cleavage site within the cytoplasmic tail. This library was screened for variants that were able to functionally pseudotype HIV-1 vector particles. All selected Env variants mediated the infectivity of HIV-1 vector particles and encoded novel cytoplasmic tail motifs. They were efficiently incorporated into HIV particles, and the R peptide was processed by the HIV protease. Interestingly, in some of the selected variants, the R-peptide cleavage site had shifted closer to the C terminus. These data demonstrate a valuable approach for the engineering of chimeric viruses and vector particles.
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U2 - 10.1128/JVI.79.2.834-840.2005
DO - 10.1128/JVI.79.2.834-840.2005
M3 - Article
C2 - 15613311
AN - SCOPUS:11144229400
SN - 0022-538X
VL - 79
SP - 834
EP - 840
JO - Journal of virology
JF - Journal of virology
IS - 2
ER -