Brevetoxin PbTx-2 immunology: differential epitope recognition by antibodies from two goats.
The epitopic regions of the brevetoxin PbTx-3 molecule, produced by the marine dinoflagellate Ptychodiscus brevis, have been identified by structural modification at three distinct regions of the toxin. These are: the A-ring lactone region of the molecule, the K-ring side-chain and the H-ring. The modified PbTx-3 derivatives were tested for their ability to bind brevetoxin goat antisera directed against the PbTx-3 molecule, by radioimmunoassay. The results showed that at least two major epitopes and one minor epitope are recognized: the A-ring lactone region of the molecule and the K-ring side-chain, and the H-ring. The results illustrate the variety of antibodies which may be produced, even within a species, and suggests that epitope characterization is important in the development of assays which are to be employed in seafood safety issues.
Melinek
R
R
Marine and Freshwater Biomedical Sciences Center, University of Miami, FL 33149.
Rein
K S
KS
Schultz
D R
DR
Baden
D G
DG
D000818:Animals; D000917:Antibody Formation; D000918:Antibody Specificity; D001667:Binding, Competitive; D004141:Dinoflagellida; D000939:Epitopes / Q000276:immunology*; D006041:Goats; D007106:Immune Sera / Q000276:immunology; D008387:Marine Toxins / Q000276:immunology* / Q000378:metabolism; D009498:Neurotoxins / Q000276:immunology* / Q000378:metabolism; D035964:Oxocins; D011863:Radioimmunoassay; D000095702:Polyether Toxins
D000939:Epitopes; D007106:Immune Sera; D008387:Marine Toxins; D009498:Neurotoxins; D035964:Oxocins; C053342:brevetoxin; D000095702:Polyether Toxins