N-terminal myristylation of HBV preS1 domain enhances receptor recognition (Articolo in rivista)

Type
Label
  • N-terminal myristylation of HBV preS1 domain enhances receptor recognition (Articolo in rivista) (literal)
Anno
  • 2001-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1034/j.1399-3011.2001.00848.x (literal)
Alternative label
  • De Falco S, Ruvo M, Verdoliva A, Scarallo, Raimondo D, Raucci A, Fassina G (2001)
    N-terminal myristylation of HBV preS1 domain enhances receptor recognition
    in The journal of peptide research
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • De Falco S, Ruvo M, Verdoliva A, Scarallo, Raimondo D, Raucci A, Fassina G (literal)
Pagina inizio
  • 390 (literal)
Pagina fine
  • 400 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 57 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 5 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • TECNOGEN SCpA, Biopharmaceut, I-81015 Piana Di Monte Verna, CE, Italy. (literal)
Titolo
  • N-terminal myristylation of HBV preS1 domain enhances receptor recognition (literal)
Abstract
  • The N-terminal portion of the large envelope protein of the human hepatitis B virus (HBV), the preS1 domain, plays a fundamental role in cell attachment and infectivity. Recent investigations have suggested that myristylation of preS1 Gly(2) residue is essential for viral infectivity, but the importance of this post-translational modification on HBV-receptor interaction has not been elucidated completely. In this study we produced, using stepwise solid-phase chemical synthesis, the entire preS1[1-119] domain (adw2 subtype), and compared its receptor binding activity with the myristylated form, myristyl-preS1[2-119] in order to define the importance of fatty acid modification. Both synthetic proteins were fully characterized in terms of structural identity using TOF-MALDI mass spectrometry and analysis of tryptic fragments. Circular dichroism measurements indicated a low content of ordered structure in the preS1 protein, while the propensity of the myristylated derivative to assume a conformationally defined structure was more evident. HBV-receptor binding assays performed with plasma membranes preparations from the hepatocyte carcinoma cell line HepG2 clearly showed that the preS1[1-119] domain recognizes the HBV receptor, and confirmed that binding is occurring through the 21-47 region. The myristylated derivative recognized HBV receptor preparations with higher affinity than the preS1 domain, suggesting that the conformational transitions induced in the preS1 moiety by fatty acid post-translational modification are important for efficient attachment of viral particles to HBV receptors. (literal)
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