Fine Mapping of Neutralization Epitopes on Duck Hepatitis B Virus (DHBV) pre-S Protein Using Monoclonal Antibodies and Overlapping Peptides

Virology ◽  
1993 ◽  
Vol 192 (1) ◽  
pp. 217-223 ◽  
Author(s):  
Sylvie Chassot ◽  
Véronique Lambert ◽  
Alan Kay ◽  
Catherine Godinot ◽  
Bernard Roux ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Fine Mapping ◽  
Duck Hepatitis B Virus ◽  
S Protein ◽  
Duck Hepatitis ◽  
B Virus

scholarly journals Glycine Decarboxylase Mediates a Postbinding Step in Duck Hepatitis B Virus Infection

2004 ◽  
Vol 78 (4) ◽  
pp. 1873-1881 ◽  
Author(s):  
Jisu Li ◽  
Shuping Tong ◽  
Hong Bock Lee ◽  
Ana Luisa Perdigoto ◽  
Hans Christian Spangenberg ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Envelope Protein ◽  
Viral Envelope ◽  
Glycine Decarboxylase ◽  
Virus Family ◽  
Duck Hepatitis B Virus ◽  
S Protein ◽  
Duck Hepatitis ◽  
B Virus

ABSTRACT Envelope protein precursors of many viruses are processed by a basic endopeptidase to generate two molecules, one for receptor binding and the other for membrane fusion. Such a cleavage event has not been demonstrated for the hepatitis B virus family. Two binding partners for duck hepatitis B virus (DHBV) pre-S envelope protein have been identified. Duck carboxypeptidase D (DCPD) interacts with the full-length pre-S protein and is the DHBV docking receptor, while duck glycine decarboxylase (DGD) has the potential to bind several deletion constructs of the pre-S protein in vitro. Interestingly, DGD but not DCPD expression was diminished following prolonged culture of primary duck hepatocytes (PDH), which impaired productive DHBV infection. Introduction of exogenous DGD promoted formation of protein-free viral genome, suggesting restoration of several early events in viral life cycle. Conversely, blocking DGD expression in fresh PDH by antisense RNA abolished DHBV infection. Moreover, addition of DGD antibodies soon after virus binding reduced endogenous DGD protein levels and impaired production of covalently closed circular DNA, the template for DHBV gene expression and genome replication. Our findings implicate this second pre-S binding protein as a critical cellular factor for productive DHBV infection. We hypothesize that DCPD, a molecule cycling between the cell surface and the trans-Golgi network, targets DHBV particles to the secretary pathway for proteolytic cleavage of viral envelope protein. DGD represents the functional equivalent of other virus receptors in its interaction with processed viral particles.

scholarly journals Monoclonal Antibodies Providing Topological Information on the Duck Hepatitis B Virus Core Protein and Avihepadnaviral Nucleocapsid Structure

2007 ◽  
Vol 81 (23) ◽  
pp. 13230-13234 ◽  
Author(s):  
Jolanta Vorreiter ◽  
Immanuel Leifer ◽  
Christine Rösler ◽  
Ludmila Jackevica ◽  
Paul Pumpens ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Structural Model ◽  
Core Protein ◽  
Duck Hepatitis B Virus ◽  
Virus Core ◽  
Duck Hepatitis ◽  
B Virus ◽  
High Resolution Structure

ABSTRACT The icosahedral capsid of duck hepatitis B virus (DHBV) is formed by a single core protein species (DHBc). DHBc is much larger than HBc from human HBV, and no high-resolution structure is available. In an accompanying study (M. Nassal, I. Leifer, I. Wingert, K. Dallmeier, S. Prinz, and J. Vorreiter, J. Virol. 81:13218-13229, 2007), we used extensive mutagenesis to derive a structural model for DHBc. For independent validation, we here mapped the epitopes of seven anti-DHBc monoclonal antibodies. Using numerous recombinant DHBc proteins and authentic nucleocapsids from different avihepadnaviruses as test antigens, plus a panel of complementary assays, particle-specific and exposed plus buried linear epitopes were revealed. These data fully support key features of the model.

Identification of Major Antigenic Domains of Duck Hepatitis B Virus Pre-S Protein by Peptide Scanning

Virology ◽  
1994 ◽  
Vol 200 (1) ◽  
pp. 72-78 ◽  
Author(s):  
Sylvie Chassot ◽  
Veronique Lambert ◽  
Alan Kay ◽  
Catherine Godinot ◽  
Christian Trepo ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Duck Hepatitis B Virus ◽  
S Protein ◽  
Duck Hepatitis ◽  
B Virus ◽  
Antigenic Domains

In vivo neutralization of duck hepatitis B virus by antibodies specific to the N-terminal portion of pre-S protein

Virology ◽  
1991 ◽  
Vol 185 (1) ◽  
pp. 446-450 ◽  
Author(s):  
Véronique Lambert ◽  
Sylvie Chassot ◽  
Alan Kay ◽  
Christian Trepo ◽  
Lucyna Cova
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Terminal Portion ◽  
Duck Hepatitis B Virus ◽  
S Protein ◽  
Duck Hepatitis ◽  
B Virus

scholarly journals Epitope mapping of neutralizing monoclonal antibodies against duck hepatitis B virus.

1989 ◽  
Vol 63 (6) ◽  
pp. 2445-2451 ◽  
Author(s):  
R C Cheung ◽  
W S Robinson ◽  
P L Marion ◽  
H B Greenberg
Keyword(s):  
Monoclonal Antibodies ◽  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Epitope Mapping ◽  
Duck Hepatitis B Virus ◽  
Duck Hepatitis ◽  
B Virus

scholarly journals St, a Truncated Envelope Protein Derived from the S Protein of Duck Hepatitis B Virus, Acts as a Chaperone for the Folding of the Large Envelope Protein

2005 ◽  
Vol 79 (9) ◽  
pp. 5346-5352 ◽  
Author(s):  
Elizabeth V. L. Grgacic ◽  
David A. Anderson
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Envelope Protein ◽  
Cellular Localization ◽  
Transmembrane Domain ◽  
Molar Ratio ◽  
Duck Hepatitis B Virus ◽  
S Protein ◽  
Duck Hepatitis ◽  
B Virus

ABSTRACT Envelope proteins of hepadnaviruses undergo a unique folding mechanism which results in the posttranslational translocation of 50% of the large envelope protein (L) chains across the endoplasmic reticulum. This mechanism is essential for the eventual positioning of the receptor-binding domain on the surface of the virus particle and in duck hepatitis B virus (DHBV) is dependent on the small (S) envelope protein as part of the assembly process. In this study, we report the identification of a third envelope protein, St, derived from the S protein and carrying functions previously attributed to S. Antibody mapping and mutagenesis studies indicated St to be C terminally truncated, spanning the N-terminal transmembrane domain (TM1) plus the adjacent cysteine loop. We have previously shown that the mutation of two conserved polar residues in TM1 of S (SAA) eliminates L translocation and assembly. A plasmid expressing a functional equivalent of St was able to rescue assembly, demonstrating that this assembly defect is due to mutations of the corresponding residues in St and not in S per se. Immunofluorescence analysis showed that St directly affects L protein cellular localization. These results indicate that St acts as a viral chaperone for L folding, remaining associated with the DHBV envelope upon secretion. The presence of St at a molar ratio of half that of L suggests that it is St which regulates L translocation to 50%.

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