title: Brevetoxin PbTx-2 immunology: differential epitope recognition by antibodies from two goats.
abstract: 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.
authors.affiliation: Marine and Freshwater Biomedical Sciences Center, University of Miami, FL 33149.
authors.forename: R
authors.initials: R
authors.lastname: Melinek
authors.forename: K S
authors.initials: KS
authors.lastname: Rein
authors.forename: D R
authors.initials: DR
authors.lastname: Schultz
authors.forename: D G
authors.initials: DG
authors.lastname: Baden
mesh_terms: 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
chemical_list: D000939:Epitopes; D007106:Immune Sera; D008387:Marine Toxins; D009498:Neurotoxins; D035964:Oxocins; C053342:brevetoxin; D000095702:Polyether Toxins