Hourioux C, Sureau C, Poisson F, Brand D, Goudeau A, Roingeard P
Laboratoire de Virologie EP CNRS 117, Faculté de Médecine, Tours, France.
J Gen Virol. 1998 May;79 ( Pt 5):1115-9. doi: 10.1099/0022-1317-79-5-1115.
Hepatitis delta virus (HDV) packaging requires prenylation of the HDV large protein (p27), as well as a direct protein-protein interaction between HDV proteins and hepatitis B virus (HBV) envelope protein domains. To investigate this interaction, we have analysed the binding capacity of baculovirus-expressed delta p24 and p27 proteins to synthetic peptides specific for the HBV envelope. Although a higher degree of binding was observed with p27, both p24 and p27 could bind HBV envelope peptides. One such peptide corresponded to residues 56-80 located in the cytosolic loop of the small HBV envelope protein, and another corresponded to 23 carboxy-terminal residues of the pre-S1 specific to the large HBV envelope protein. This indicates that in addition to p27, p24 may contribute to packaging of HDV through a protein-protein interaction with HBV envelope domains, and that an interaction between the pre-S1 polypeptide and delta proteins may play a role in infectivity.
丁型肝炎病毒（HDV）的包装需要HDV大蛋白（p27）的异戊二烯化，以及HDV蛋白与乙型肝炎病毒（HBV）包膜蛋白结构域之间直接的蛋白质-蛋白质相互作用。为了研究这种相互作用，我们分析了杆状病毒表达的δ p24和p27蛋白与HBV包膜特异性合成肽的结合能力。尽管观察到p27具有更高程度的结合，但p24和p27都能结合HBV包膜肽。其中一种肽对应于位于HBV小包膜蛋白胞质环中的56-80位氨基酸残基，另一种对应于HBV大包膜蛋白特异性的前S1的23个羧基末端残基。这表明，除了p27之外，p24可能通过与HBV包膜结构域的蛋白质-蛋白质相互作用而有助于HDV的包装，并且前S1多肽与δ蛋白之间的相互作用可能在感染性中起作用。
