D. Deregt et al., MONOCLONAL-ANTIBODIES TO EQUINE ARTERITIS VIRUS PROTEINS IDENTIFY THEG(L) PROTEIN AS A TARGET FOR VIRUS NEUTRALIZATION, Journal of General Virology, 75, 1994, pp. 2439-2444
Monoclonal antibodies (MAbs) to equine arteritis virus (EAV) proteins
were produced and characterized. The protein specificities of eight MA
bs were determined definitively by immunoprecipitation of EAV proteins
expressed from vaccinia virus recombinants (VVRs). Included were two
new VVRs produced for this study, expressing the M and the G(L) protei
ns, respectively. Three MAbs were determined to be N-specific and five
MAbs recognized the G(L) protein. One G(L)-specific MAb, 17F5, of the
IgA class, efficiently neutralized EAV infectivity. In competitive bi
nding assays (CBAs), the N-specific MAbs defined a single antigenic do
main on this protein. Four G(L)-specific MAbs, including MAb 17F5, dem
onstrated strong reciprocal competition in binding to the G(L) protein
but differed in their virus-neutralizing ability. Thus the antigenic
domain defined by these MAbs is probably composed of overlapping or cl
osely adjacent epitopes. The fifth G(L)-specific MAb, a nonneutralizin
g antibody, may define an epitope adjacent to this antigenic domain as
reciprocal CBAs demonstrated lower competition.