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Titolo:
N-terminal myristylation of HBV preS1 domain enhances receptor recognition
Autore:
De Falco, S; Ruvo, M; Verdoliva, A; Scarallo, A; Raimondo, D; Raucci, A; Fassina, G;
Indirizzi:
TECNOGEN SCpA, Biopharmaceut, I-81015 Piana Di Monte Verna, CE, Italy TECNOGEN SCpA Piana Di Monte Verna CE Italy I-81015 onte Verna, CE, Italy
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 5, volume: 57, anno: 2001,
pagine: 390 - 400
SICI:
1397-002X(200105)57:5<390:NMOHPD>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEPATITIS-B VIRUS; LARGE ENVELOPE PROTEIN; TRANSMEMBRANE TOPOLOGY; PLASMA-MEMBRANES; PRE-S1 DOMAIN; MYRISTIC ACID; CELL; INFECTIVITY; BINDING; SITE;
Keywords:
hepatitis B virus; myristylation; preS1; receptor binding;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Fassina, G TECNOGEN SCpA, Biopharmaceut, I-81015 Piana Di Monte Verna, CE,Italy TECNOGEN SCpA Piana Di Monte Verna CE Italy I-81015 CE, Italy
Citazione:
S. De Falco et al., "N-terminal myristylation of HBV preS1 domain enhances receptor recognition", J PEPT RES, 57(5), 2001, pp. 390-400

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 myristylatedderivative 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/02/20 alle ore 15:11:06