Interaction between duck hepatitis B virus and a 170-kilodalton cellular protein is mediated through a neutralizing epitope of the pre-S region and occurs during viral infection

Abstract

Identification of cell surface viral binding proteins is important for understanding viral attachment and internalization. We have fused the pre-S domain of the duck hepatitis B virus (DHBV) large envelope protein to glutathione S-transferase and demonstrated a 170-kDa binding protein (p170) in [ 35 S]methionine-labeled duck hepatocyte lysates. This glycoprotein was found abundantly in all extrahepatic tissues infectible withDHBV and in some noninfectible tissues, though it is not secreted into the blood. The interaction of pre-S fusion protein with p170 was competitively inhibited by wild-type DHBV in a dose-dependent manner. In addition, infection of hepatocytes with DHBV blocked the binding of pre-S fusion protein to p170, which suggests a biological role for p170 during natural infection. The p170 binding site was mapped to a conserved sequence of 16 amino acid residues (positions 87 to 102) by using 24 pre-S deletion mutants; this binding domain coincides with a major virus-neutralizing antibody epitope. Furthermore, site-directed mutagenesis revealed that an arginine residue at position 97 is critical for p170 binding. p170 was purified by a combination of ion-exchange and affinity chromatographies, and four peptide sequences were obtained. Two peptides showed significant similarities to human and animal carboxypeptidases H, M, and N. Taken together, these results raise the possibility that the p170 binding protein is important during the replication cycle of DHBV.

Interaction of virus populations with their hosts

“…Virus-antibody complex structures show epitopes at receptor recognition sites Tseng et al (2015) Bovine herpesvirus-1 Antiidiotypic antibodies bind to cellular receptors Thaker et al (1994), Varthakavi and Minocha (1996) Human cytomegalovirus Antiidiotypic antibodies bind to cellular receptors Keay et al (1989), Keay and Baldwin (1991) Herpes simplex virus Antiidiotypic antibodies bind to cellular receptors Huang and Campadelli-Fiume (1996) Overlap between a receptor-binding domain in gD and an antigenic site Whitbeck et al (1999) Hepatitis B virus Antiidiotypic antibodies that mimic cellular structures bind to small HBV surface antigen. Synthetic peptide analog is recognized by antiHBV antibodies and cell receptors Neurath et al (1986) Antiidiotypic antibodies bind to cellular receptors Petit et al (1992), Hertogs et al (1994), Budkowska et al (1995) Duck hepatitis B virus Residues involved in the interaction with cells are also critical for virus neutralization Tong et al (1995), Li et al (1996), Sunyach et al (1999 4.5 Trait coevolution: mutual influences between antigenic variation and tropism change…”

Evolution of Cell Recognition by Viruses: A Source of Biological Novelty with Medical Implications

“…Mab recognized epitopes involved in the binding of virions to cellular receptors (Kubo et al, 1993(Kubo et al, , 1994 Flaviviridae BVDV Anti-idiotypic antibodies mimicking viral antigens bind to cellular receptors (Xue and Minocha, 1993;Minocha et al, 1997) Dengue virus Amino acid residues critical for mouse neurovirulence are involved in antibody binding (Hiramatsu et al, 1996) Yellow fever virus Amino acid residues critical for virus neurotropism are involved in antibody binding (Jennings et al, 1994) Hepadnaviridae Duck hepatitis B virus Residues critical for virus neutralization are involved in the interaction with cells (Tong et al, 1995;Li et al, 1996;Sunyach et al, 1999) Hepatitis B virus Anti-idiotypic antibodies mimicking viral antigens bind to cellular receptors (Petit et al, 1992;Hertogs et al, 1994;Budkowska et al, 1995) Anti-idiotypic antibodies mimicking cellular structures bind to small hepatitis B surface antigen (Neurath et al, 1986) A synthetic peptide analogue is recognized by both cell receptors and anti-HBV antibodies (Neurath et al, 1986) Herpesviridae BHV-1 Anti-idiotypic antibodies mimicking viral antigens bind to cellular receptors (Thaker et al, 1994;Varthakavi and Minocha, 1996) HCMV Anti-idiotypic antibodies mimicking viral antigens bind to cellular receptors (Keay et al, 1989;Keay and Baldwin, 1991) HSV Anti-idiotypic antibodies mimicking viral antigens bind to cellular receptors (Huang and Campadelli-Fiume, 1996) Overlap between major neutralizing antigenic site and a receptor-binding domain of gD (Whitbeck et al, 1999) (continues)…”

Interaction of Virus Populations with Their Hosts

“…Residues involved in the interaction with cells are also critical for virus neutralization Tong et al 1995, Li et al (1996, Sunyach et al (1999) Yeates et al (1991)…”