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Journal of General Virology (2002), 83, 2241-2246.
© 2002 Society for General Microbiology


Animal: RNA Viruses

Identification of R-peptides in envelope proteins of C-type retroviruses

Maria Bobkova1, Joern Stitz1, Martin Engelstädter1, Klaus Cichutek1 and Christian J. Buchholz1

Department of Medical Biotechnology, Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 51–59, 63225 Langen, Germany1

Author for correspondence: Christian Buchholz. Fax: +49 6103/771255. e-mail bucch{at}pei.de

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.




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