Identification of R-peptides in envelope proteins of C-type retroviruses
| Autor: | Maria Bobkova, Martin Engelstädter, Joern Stitz, Klaus Cichutek, Christian J. Buchholz |
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| Předmět: |
viruses
medicine.medical_treatment Molecular Sequence Data Endogenous retrovirus Sequence alignment Biology Transfection Cleavage (embryo) Membrane Fusion Virus Cell Line Dogs Viral Envelope Proteins Western blot Virology Endopeptidases medicine Animals Humans Amino Acid Sequence Spleen Focus-Forming Viruses Recombination Genetic Reporter gene Protease Virulence medicine.diagnostic_test Lipid bilayer fusion Molecular biology Leukemia Virus Murine Retroviridae Leukemia Virus Gibbon Ape Peptides Sequence Alignment Retroviridae Infections |
| Zdroj: | Scopus-Elsevier |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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