Open AccessMonoclonal Antibodies Providing Topological Information on the Duck Hepatitis B Virus Core Protein and Avihepadnaviral Nucleocapsid Structure
Author(s) -
Jolanta Vorreiter,
Immanuel Leifer,
Christine Rösler,
Ludmila Jackeviča,
Paul Pumpens,
Michael Nassal
Publication year - 2007
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.00847-07
Subject(s) - biology , virology , monoclonal antibody , core protein , antibody , core (optical fiber) , hepatitis a virus , hepatitis b virus , virus , genetics , physics , optics
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.