Article Figures & Data
Figures
- FIG. 1.
Schematic diagram (A) of GST fusion protein constructs containing full-length or truncated nucleocapsid fragments of PPRV and Western immunoblot confirmation (B) of E. coli-expressed products using goat anti-PPRV serum.
- FIG. 2.
Reactivity of anti-PPRV nucleocapsid MAbs with native (A), baculovirus-expressed recombinant (B), or E. coli-expressed recombinant GST fusion nucleocapsid proteins (C) in an indirect ELISA.
- FIG. 3.
Mapping of MAb epitopes using GST fusion proteins containing partially overlapped fragments of PPRV nucleocapsid protein. GST-N1-525 (B), GST-N1-262 (C), GST-N1-447 (D), and GST-N405-521 (E) were separated electrophoretically and then transferred to nitrocellulose membranes. Baculovirus-expressed N protein rPPRV-N (A) was used as control. The binding of each MAb to GST fusion proteins on the membranes was detected using Western immunoblotting.
- FIG. 4.
Immunogenicity of seven epitopes on the nucleocapsid of PPRV as determined by the degree of blocking of their binding to the baculovirus-expressed recombinant PPRV N protein by anti-PPRV caprine sera (PPR 2-65, PPR 2-66, PPR 2-69, PPR 2-73, and PPR 2-81), PPRV hyperimmune serum (RPV positive), or anti-PRV bovine sera (RP K9061 and K9062) at dilutions of 1:20 (A) and 1:400 (B). Each epitope is designated by the name of each detector MAb.
- FIG. 5.
Average humoral antibody response to four immunodominant epitopes (MAbs 38-4, P-3H12, P-13A9, and P-11A6) of PPRV N protein in three goats experimentally infected with PPRV of lineage I as measured by a competitive ELISA.
Tables
- TABLE 1.
Mapping of epitopes on the N protein of PPRV Nig75/1 straina
Competing MAb (isotype) Domain Labeled MAb 33-4 P-3H12 P-13A9 38-4 P-14C6 P-9H10 P-11A6 33-4 (IgG1) A-I ++ − − − − − − P-3H12 (IgG2a) A-II − +++ ++ − − − − P-13A9 (IgG2b) A-II − +++ +++ + − − − 38-4 (IgG1) A-II − +++ +++ +++ − − − P-14C6 (IgM) C-I − ++ ++ − ++ − − P-9H10 (IgG1) C-II − + + − − +++ − P-11A6 (IgG2b) C-II − +++ +++ − − +++ +++ ↵ a −, <50% competition by unlabeled MAb at 1:100; +, >50% competition by unlabeled MAb at 1:100; ++, >50% competition by unlabeled MAb at 1:1,000; +++, >50% competition by unlabeled MAb at 1:10,000.
