Bovine respiratory syncytial (BRS) virus can be divided into antigenic
subgroups based on the reactivity of monoclonal antibodies (mAbs) to
the attachment glycoprotein, G. Further, the polyclonal antibody respo
nse of calves vaccinated with recombinant vaccinia viruses expressing
the G protein of a particular subgroup is also subgroup-specific. To i
nvestigate the genetic basis for the antigenic heterogeneity of the BR
S virus G protein, the genes for the G protein from 6 BRS virus strain
s representative of the antigenic subgroups were cloned, sequenced, an
d compared with the prototype subgroup A strain, 391-2. There was only
10% nucleic acid difference and 15% amino acid difference between str
ains from different subgroups. These findings are in sharp contrast to
the situation with human RS virus, where there is a 45% difference in
amino acid identity between subgroups. In fact, the extent of amino a
cid difference between BRS virus subgroups is similar to the level of
heterogeneity observed within human subgroups. Analysis of the reactiv
ity of mAbs with peptides from the cysteine-rich region (174-188) of t
he G protein representing each antigenic subgroup indicated that amino
acids at positions 180, 183, and possibly 184 are important in subgro
up distinction. Taken together, these data suggest that although the g
enetic variation responsible for the antigenic differences determining
subgroups among BRS viruses is more limited than that observed among
human RS virus subgroups, the amino acid differences that exist have a
profound effect upon antibody recognition. (C) 1997 Academic Press.