N-terminal myristylation of HBV preS1 domain enhances receptor recognition(417 views) De Falco S, Ruvo M, Verdoliva A, Scarallo A, Raimondo D, Raucci A, Fassina G
J Pept Res (ISSN: 1397-002x, 1397-002xlinking), 2001 May; 57(5): 390-400.
Keywords: Hepatitis B Virus, Myristylation, Pres1, Receptor Binding, Virus Envelope Protein, Amino Terminal Sequence, Article, Binding Affinity, Circular Dichroism, Human, Human Cell, Mass Spectrometry, Priority Journal, Protein Conformation, Protein Domain, Protein Interaction, Protein Processing, Protein Structure, Protein Synthesis, Virus Adsorption, Virus Infectivity, Amino Acid Sequence, Cell Line, Chromatography, High Pressure Liquid, Enzyme-Linked Immunosorbent Assay, Hepatitis B Surface Antigens, Molecular Sequence Data, Myristic Acid, Protein Precursors, Matrix-Assisted Laser Desorption-Ionization, Chemistry, Metabolism,
Affiliations: *** IBB - CNR ***
Biopharmaceuticals, TECNOGEN S.C.p.A, Piana di Monte Verna, Italy
Biopharmaceuticals TECNOGEN S.C.p.A, 81015 Piana di Monte Verna (CE), Italy
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Rhee, S. S., Hunter, E., Myristylation is required for intracellular transport but not for assembly of D-type retrovirus capsid (1987) J. Virol., 61, pp. 1045-1053
Krausslich, H. G., Holscher, C., Reuer, Q., Harber, J., Wimmer, E., Myristoylation of the poliovirus polyprotein is required for proteolytic processing of the capsid and for viral infectivity (1990) J. Virol., 64, pp. 2433-2436
Streuli, C. H., Griffin, B. E., Myristic acid is coupled to a structural protein of polyoma virus and SV40 (1987) Nature, 326, pp. 619-621
Macrrae, D. R., Bruss, V., Ganem, D., Myristylation of a duck hepatitis B virus envelope protein is essential for infectivity but not for virus assembly (1991) Virology, 181, pp. 359-363
Hubbard, A. L., Wall, D. A., Ma, A., Isolation of rat hepatocyte plasma membranes. Presence of the three major domain (1983) J. Cell. Biol., 96, pp. 217-229
Aden, D. P., Fogel, A., Plotkin, S., Damjanov, I., Knowles, B., Controlled synthesis oh HBsAg in a differentiated human liver carcinoma-derived cell line (1979) Nature, 282, pp. 615-616
Dash, S., Rao, K. V. S., Panda, S., Receptor for Pre-S1 (21-47) component of hepatitis B virus on the liver cells (1992) J. Med. Virol., 37, pp. 116-121
Ryu, C. J., Cho, D. Y., Gripon, P., Kim, H. S., Guguen-Guillouzo, C., Hong, H. J., An 80-kilodalton protein that binds to the PreS1 domain of hepatitis B virus (2000) J. Virol., 74, pp. 110-116
Persing, D. H., Varmus, H. E., Ganem, D., The preS1 protein of hepatitis B virus is acylated at its amino terminus with myristic acid (1987) J. Virol., 61, pp. 1672-1677
Towler, D. A., Gordon, J. I., The biology and enzymology of eukaryotic protein acylation (1988) Annu. Rev. Biochem., 57, pp. 69-99
Dawson, P. E., Muir, T. W., Clark-Lewis, I., Kent, S. B. H., Synthesis of proteins by native chemical ligation (1994) Science, 266, pp. 776-779
N-terminal myristylation of HBV preS1 domain enhances receptor recognition
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 Gly2 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.
N-terminal myristylation of HBV preS1 domain enhances receptor recognition
No results.
N-terminal myristylation of HBV preS1 domain enhances receptor recognition
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(435 views) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 ViewExport to BibTeXExport to EndNote