Jr. Crowther et al., CHARACTERIZATION OF MONOCLONAL-ANTIBODIES AGAINST A TYPE SAT-2 FOOT-AND-MOUTH-DISEASE VIRUS, Epidemiology and infection, 111(2), 1993, pp. 391-406
This paper is the first to describe characterization of monoclonal ant
ibodies (MAbs) against a South African Territories 2 (SAT 2) foot-and-
mouth disease virus (isolate Rho 1/48). Twelve MAbs which neutralized
homologous virus were characterized in indirect and sandwich ELISA usi
ng purified Rho 1/48 virus particles, subunits, trypsin-treated, and c
hemically denatured virus. All the Mabs inhibited haemagglutination by
parental virus. Binding of the MAbs to 73 SAT 2 field isolates was me
asured in a sandwich ELISA and defined four distinct antigenic regions
. Preliminary characterization of escape mutants selected with some of
the MAbs using virus neutralization tests, ELISA, and amino acid sequ
encing is included. MAbs 2, 25, 40, 48 and 64, reacted with a linear e
pitope on the VP1 loop region. An amino acid change at position 149 (v
aline to glutamic acid) was detected in mutants selected by MAb 2 and
40 and this eliminated binding and neutralization by all the other MAb
. This epitope was conformation-dependent and was conserved in all 73
isolates of SAT 2 examined. Escape mutants isolated with MAb 41 and 44
, had changes at positions 156 (glycine to aspartic acid), or 158 (ser
ine to leucine) respectively. These MAbs bound with Rho 1/48 only out
of 73 field strain viruses studies and the reactions of MAbs from the
other groups was unaltered. MAb 27, 28 and 37 reacted with a conformat
ion-dependent epitope on VP1 which was not conserved in field isolates
. All mutants selected by these MAbs had a single amino acid substitut
ion at position 149 (valine to alanine). The same change was always fo
und in field isolates which did not bind MAbs from this group. MAb 11
reacted with a linear epitope associated with amino acids 147 or 148 o
n VP1 and showed similar binding characteristics to a conformation dep
endent MAb 7, no amino acid residue changes were found within VP1 for
monoclonal antibody 7 mutants.