A new virus was isolated from a finch in quarantine in Northern Irelan
d in 1973. The virus had the morphological characteristics of a paramy
xovirus, and was named Banger virus (BaV). In order to identify the st
ructural proteins of BaV and to investigate the biological characteriz
ation of the virus, 28 monoclonal antibodies (mAbs) directed against B
aV were prepared. Eight of these mAbs reacted with the nucleocapsid pr
otein (NP), 10 with hemagglutinin-neuraminidase (HN) protein, and 10 w
ith fusion (F) protein. With the aid of these mAbs, the structural pro
teins of BaV were determined, namely, p52, gp74, gp63, and gp51 were i
dentified as the NP, HN, F0, and F1 proteins, respectively. The biolog
ical activities of the mAbs directed against the envelope glycoprotein
s of BaV were examined. Intriguingly, ir was found in the neutralizati
on assay that four mAbs directed against the HN protein of BaV can enh
ance the fusion of HeLa cells infected with BaV, showing the presence
of a potential third function of the HN protein that affects the fusio
n activity of the F protein. Furthermore, all of the anti-F protein mA
bs showed neutralizing activity.