Sequences of the hepatitis delta virus (HDV) vary to different degrees amon
g isolates. A monoclonal antibody, designated as HP6A1, against the antigen
of HDV (HDAg) has been characterized for its specificity. HP6A1 bound to H
DAg of isolate 25 (genotype I) that was used for immunization, but not to o
thers of both genotypes I and II. The epitope recognized by HP6A1 was then
determined by a phage library displaying various heptapeptides. A consensus
peptide deduced has the best match with that of residues 4-10 of HDAg (iso
late 25). To confirm the phage mapping result, Escherichia coil recombinant
proteins containing different lengths and various segments of HPAg (isolat
e 25) were constructed. The shortest HDAg segment contained in the fusion p
rotein that reacted with HP6A1 was residues 1-10. When this peptide was add
ed to the N-terminus of a heterologous protein engineered for eucaryotic ex
pression, the fusion protein was detected by HP6A1. It is concluded that HP
6A1 recognizes an epitope located at the N-terminus of HDAg (isolate 25). S
ince viruses of quasi-species exist in natural infections, a question of ho
w different viral strains interact in vivo remains to be explored. The high
ly specific MAb opens a possibility to examine the fate of one strain in th
e presence of other related species in a cell transfection system. (C) 2000
Elsevier Science B.V. All rights reserved.