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- W2157514015 endingPage "2246" @default.
- W2157514015 startingPage "2241" @default.
- W2157514015 abstract "Activation of the murine leukaemia virus (MLV) envelope protein (Env) requires proteolytic cleavage of the R-peptide, a 16 amino acid C-terminal part of the cytoplasmic tail (C-tail) of Env. This paper demonstrates the presence of R-peptides in Env proteins of C-type retroviruses of simian, avian and porcine origin. Sequence alignment with the MLV C-tail led to the identification of a conserved hydrophobic protease cleavage motif located in the centre of retroviral Env protein C-tails. Expression of Env proteins, truncated at the predicted cleavage sites, of spleen necrosis virus (SNV), gibbon ape leukaemia virus and porcine endogenous retroviruses resulted in cell–cell fusion as monitored by microscopy and reporter gene fusion assays. Western blot analysis of MLV particles pseudotyped with the SNV Env protein demonstrated proteolytic cleavage of the SNV R-peptide by the MLV protease. Our data suggest that activation of membrane fusion by R-peptide cleavage is a common mode in C-type retroviruses." @default.
- W2157514015 created "2016-06-24" @default.
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- W2157514015 date "2002-09-01" @default.
- W2157514015 modified "2023-09-23" @default.
- W2157514015 title "Identification of R-peptides in envelope proteins of C-type retroviruses" @default.
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- W2157514015 doi "https://doi.org/10.1099/0022-1317-83-9-2241" @default.
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