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J Biol Chem, Vol. 274, Issue 9, 5707-5715, February 26, 1999

A Soluble Form of the Avian Hepatitis B Virus Receptor
BIOCHEMICAL CHARACTERIZATION AND FUNCTIONAL ANALYSIS OF THE RECEPTOR LIGAND COMPLEX

From the Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany

Avian hepatitis B virus infection is initiated by the specific interaction of the extracellular preS part of the large viral envelope protein with carboxypeptidase D (gp180), the primary cellular receptor. To functionally and biochemically characterize this interaction, we purified a soluble form of duck carboxypeptidase D from a baculovirus expression system, confirmed its receptor function, and investigated the contribution of different preS sequence elements to receptor binding by surface plasmon resonance analysis. We found that preS binds duck carboxypeptidase D with a 1:1 stoichiometry, thereby inducing conformational changes but not oligomerization. The association constant of the complex was determined to be 2.2 × 10⁷ M¹ at 37 °C, pH 7.4, with an association rate of 4.0 × 10⁴ M¹ s¹ and a dissociation rate of 1.9 × 10³ s¹, substantiating high affinity interaction of avihepadnaviruses with their receptor carboxypeptidase D. The separately expressed receptor-binding domain, comprising about 50% of preS as defined by mutational analysis, exhibits similar constants. The domain consists of an essential element, probably responsible for the initial receptor contact and a part that contributes to complex stabilization in a conformation sensitive manner. Together with previous results from cell biological studies these data provide new insights into the initial step of hepadnaviral infection.

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