We have identified a 180-kDa cellular glycoprotein (gp180) that binds
with high affinity to duck hepatitis B virus (DHBV) particles. The pro
tein was detected by coprecipitating labeled duck hepatocyte proteins
with virions or recombinant DHBV envelope proteins, using nonneutraliz
ing monoclonal antibodies to the virion envelope. Binding of gp180 req
uires only the pre-S region of the viral large envelope protein, since
recombinant fusion proteins bearing only this region efficiently copr
ecipitate gp180. The DHBV-gp180 interaction is blocked by two independ
ent neutralizing monoclonal antibodies. The protein is found on both i
nternal and surface membranes of the cell, and the species distributio
n of gp180 binding activity mirrors the known host range of DHBV infec
tion. Functional gp180 is expressed in a wide variety of tissues in su
sceptible ducks.