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10.1128/JVI.75.15.7078-7085.2001

http://scihub22266oqcxt.onion/10.1128/JVI.75.15.7078-7085.2001
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C114436!114436!11435588
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suck abstract from ncbi


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pmid11435588      J+Virol 2001 ; 75 (15): 7078-85
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  • N-Terminal Domain of Borna Disease Virus G (p56) Protein Is Sufficient for Virus Receptor Recognition and Cell Entry? #MMPMID11435588
  • Perez M; Watanabe M; Whitt MA; de la Torre JC
  • J Virol 2001[Aug]; 75 (15): 7078-85 PMID11435588show ga
  • Borna disease virus (BDV) surface glycoprotein (GP) (p56) has a predicted molecular mass of 56 kDa. Due to extensive posttranslational glycosylation the protein migrates as a polypeptide of 84 kDa (gp84). The processing of gp84 by the cellular protease furin generates gp43, which corresponds to the C-terminal part of gp84. Both gp84 and gp43 have been implicated in viral entry involving receptor-mediated endocytosis and pH-dependent fusion. We have investigated the domains of BDV p56 involved in virus entry. For this, we used a pseudotype approach based on a recently developed recombinant vesicular stomatitis virus (VSV) in which the gene for green fluorescent protein was substituted for the VSV G protein gene (VSV?G*). Complementation of VSV?G* with BDV p56 resulted in infectious VSV?G* pseudotypes that contained both BDV gp84 and gp43. BDV-VSV chimeric GPs that contained the N-terminal 244 amino acids of BDV p56 and amino acids 421 to 511 of VSV G protein were efficiently incorporated into VSV?G* particles, and the resulting pseudotype virions were neutralized by BDV-specific antiserum. These findings indicate that the N-terminal part of BDV p56 is sufficient for receptor recognition and virus entry.
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