Amino acid variation at the mitochondrial binding site of Antimycin A is proposed to reflect sensitivity and toxicity differences among fish species

To better understand differential sensitivities among fish species to the piscicidal compound Antimycin-A (ANT-A), we hypothesized that variations in amino acids at the ANT-A binding site may reflect toxicity differences. Protein sequences for six motifs comprising the ANT-A binding site were obtained and compared for invasive carp species (N = 515) and seven non-target species (N = 277); a consensus was delineated from each species. The carp species, Common Carp (Cyprinus carpio), Silver Carp (Hypophthalmichthys molitrix), Bighead Carp (Hypophthalmichthys nobilis), Grass Carp (Ctenopharyngodon idella), and Black Carp (Mylopharyngodon piceus), showed the same amino acids at the site; thus, it was termed the carp consensus motif sequence (CCM). Channel Catfish (Ictalurus punctatus) showed the most amino acid polymorphisms, with three motifs 96–100% different from CCM. Within a species, Bluegill (Lepomis macrochirus) and Fathead Minnow (Pimephales promelas) variation per motif was most dissimilar (46.7% and 21.6%, respectively). Organismal mortality data from the literature indicated Yellow Perch (Perca flavescens), Walleye (Sander vitreus), and American Gizzard Shad (Dorosoma cepedianum) to be most sensitive to the piscicide, Catfish least sensitive, and all others intermediate. The protein sequence variations of the binding site appeared to be in accord with organismal sensitivity categories when they differed from the CCM; the motifs in Gizzard Shad and Walleye were the same as in CCM. The physical/chemical nature of ANT-A is important to consider in organismal response comparisons. This cellular approach of studying ANT-A binding at its target enzyme is a non-destructive way to predict piscicidal efficacy of ANT-A against fishes of interest, informs management decisions in control efforts for invasives, and can be used to forecast effects on sympatric species.