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10.1007/s00705-010-0645-9

http://scihub22266oqcxt.onion/10.1007/s00705-010-0645-9
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20333534!ä!20333534

suck abstract from ncbi


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pmid20333534      Arch+Virol 2010 ; 155 (5): 789-93
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  • Protein kinase C-dependent phosphorylation of Borna disease virus P protein is required for efficient viral spread #MMPMID20333534
  • Schmid S; Metz P; Prat CM; Gonzalez-Dunia D; Schwemmle M
  • Arch Virol 2010[May]; 155 (5): 789-93 PMID20333534show ga
  • Mutational analysis of the phosphate acceptor sites of the Borna disease virus (BDV) phosphoprotein (P) has suggested a role of phosphorylation for viral spread. However, the studied mutant viruses also had two amino acid exchanges in the X protein, because the reading frames of P and X overlap. To determine the relative contribution of P and X to viral attenuation, we studied a P variant with serine-to-leucine substitutions (P(S26L,S28L)) in which the wild-type X sequence was conserved. Viral spread of rBDV-P(S26L,S28L) was impaired in human oligodendroglioma cells and in adult rats. Thus, BDV-P phosphorylation contributes to efficient viral dissemination.
  • |Animals[MESH]
  • |Borna disease virus/*physiology[MESH]
  • |Cells, Cultured[MESH]
  • |Humans[MESH]
  • |Phosphoproteins/*metabolism[MESH]
  • |Phosphorylation[MESH]
  • |Protein Kinase C/chemistry/*physiology[MESH]
  • |Rats[MESH]
  • |Rats, Inbred Lew[MESH]


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