Antigenic polymorphism of the "short" scorpion toxins able to block K+ channels.

BmTX3 is a toxin recently characterised from the venom of the Chinese scorpion Buthus martensi Karch, which specifically blocks a transient A-type K+ current in striatum neurons in culture and binds to rat brain synaptosomes with high affinity. With Aa1 and AmmTX3, it belongs to the new alpha-KTx15 subfamily from "short-chain" scorpion toxins, which specifically block different types of K+ channels. Here, a highly specific polyclonal antiserum was raised in rabbit against a C-terminal deleted BmTX3 analogue (BmTX-del YP). Using liquid-phase radioimmunoassay, we have studied its selectivity for the toxins from the alpha-KTx15 subfamily. We have also demonstrated that no/or poor cross-reactivity was observed with a panel of "short-chain" scorpion toxins representative of other structurally different subfamilies. These results suggest that a wide antigenic polymorphism, similar to that previously observed for "long-chain" scorpion toxins acting as modulators of voltage-activated Na+ channels, is also the rule for the "short-chain" scorpion toxins able to block K+ channels.