Abstract
Paralytic shellfish toxins (PSTs) are a group of toxins that cause paralytic shellfish poisoning through blockage of voltage-gated sodium channels. PSTs are produced by prokaryotic freshwater cyanobacteria and eukaryotic marine dinoflagellates. Proliferation of toxic algae species can lead to harmful algal blooms, during which seafood accumulate high levels of PSTs, posing a health threat to consumers. The existence of PST-transforming enzymes was first remarked due to the divergence of PST profiles and concentrations between contaminated bivalves and toxigenic organisms. Later, several enzymes involved in PST transformation, synthesis and elimination have been identified. The knowledge of PST-transforming enzymes is necessary for understanding the processes of toxin accumulation and depuration in mollusk bivalves. Furthermore, PST-transforming enzymes facilitate the obtainment of pure analogues of toxins as in natural sources they are present in a mixture. Pure compounds are of interest for the development of drug candidates and as analytical reference materials. PST-transforming enzymes can also be employed for the development of analytical tools for toxin detection. This review summarizes the PST-transforming enzymes identified so far in living organisms from bacteria to humans, with special emphasis on bivalves, cyanobacteria and dinoflagellates, and discusses enzymes’ biological functions and potential practical applications.
Highlights
Paralytic shellfish toxins (PSTs) are a group of potent neurotoxins that upon consumption cause paralytic shellfish poisoning (PSP) in fish, birds and mammals including humans
Key Contribution: This review summarizes the current knowledge of PST-transforming enzymes, which have been so far identified in bacteria, cyanobacteria, fish, humans, bivalves and dinoflagellates
This review summarizes the current knowledge about PST-transforming enzymes, which have been so far identified in bacteria, fish, humans, bivalves and dinoflagellates, with a special emphasis on the latter two
Summary
Paralytic shellfish toxins (PSTs) are a group of potent neurotoxins that upon consumption cause paralytic shellfish poisoning (PSP) in fish, birds and mammals including humans. Actions ofdescribed, PSTs consist of an the inhibition ofonly electrical conduction in have Other been identified and structurally toxicity of some ofand them was rare. Other rare R4 side chain substituents such as hydroxybenzoate, sulfated-benzoate and acetate have been identified and structurally described, the toxicity only ofofsome of [9,10,11]. Them was charged guanidinium groups thesodium tetrahydropurinic and hydroxyls atnerve the C12 position affinity of PSTs toin the channelsalthough is ring mainly due tointhe the positively cells byThe blocking voltage-gated sodium channels—proteins involved thepresence signal transduction havePSTs’. Physiological actions of consist of of an inhibition ofsignificantly electrical conduction in cells charged guanidinium groups thesodium tetrahydropurinic ring anddue hydroxyls at the C12of position [9,10,11]. K[9,10,11]
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