Fish Cytolysins in All Their Complexity

Abstract

The majority of the effects observed upon envenomation by scorpaenoid fish species can be reproduced by the cytolysins present in their venoms. Fish cytolysins are multifunctional proteins that elicit lethal, cytolytic, cardiovascular, inflammatory, nociceptive, and neuromuscular activities, representing a novel class of protein toxins. These large proteins (MW 150–320 kDa) are composed by two different subunits, termed α and β, with about 700 amino acid residues each, being usually active in oligomeric form. There is a high degree of similarity between the primary sequences of cytolysins from different fish species. This suggests these molecules share similar mechanisms of action, which, at least regarding the cytolytic activity, has been proved to involve pore formation. Although the remaining components of fish venoms have interesting biological activities, fish cytolysins stand out because of their multifunctional nature and their ability to reproduce the main events of envenomation on their own. Considerable knowledge about fish cytolysins has been accumulated over the years, although there remains much to be unveiled. In this review, we compiled and compared the current information on the biochemical aspects and pharmacological activities of fish cytolysins, going over their structures, activities, mechanisms of action, and perspectives for the future.

The perspective of fish venom: An overview of the physiology, evolution, molecular and genetics

“…Karatoxin 110kDa It is well known that fish venom is still largely unexplored as reported by (Silva et al, 2018;Xie et al, 2019;Gorman et al, 2020;Campos et al, 2021;Lopes-Ferreira et al, 2022) and in previous sections of this paper. Because there are few fish toxin sequences available as references, most of them are from Scorpaenidae and Synanceiidae families, it is challenging to research fish toxins and to create quick and effective techniques for wide exploration of toxin proteins or genes (Xie et al, 2017).…”

“…Because there are few fish toxin sequences available as references, most of them are from Scorpaenidae and Synanceiidae families, it is challenging to research fish toxins and to create quick and effective techniques for wide exploration of toxin proteins or genes (Xie et al, 2017). Some recent studies have isolated and provided several toxins sequences using different techniques (Smith and Wheeler, 2006;Xie et al, 2016;Costa et al, 2018;Xie et al, 2019;Campos et al, 2021;Lopes-Ferreira et al, 2022), but due to a given number of venomous fish (>2000 species) (Saggiomo et al, 2021), it would be just a small portion of it.…”

“…However, this method takes a long time and uses a lot of crude venoms. Studies have shown, cDNA cloning and genomic sequencing were used to identify the full amino acids sequences of various toxins including SNTX (Chun, 2004), verrucotoxin (VTX) (Ziegman and Alewood, 2015), cytolysins (Campos et al, 2021), lectin (Nakagawa et al, 2015;Ziegman et al, 2019;Lopes-Ferreira et al, 2022), Sp-CTx (Costa et al, 2018), and hyaluronidases (Ziegman et al, 2019) and among the others in which most of them exhibit high sequence identity among and between species.…”

Patofiziološki mehanizmi djelovanja životinjskih i biljnih toksina

“…Uz to, verukotoksin može lizirati membrane trombocita u krvi. 35 Kardiotoksičnost otrova manifestira se dvofaznim padom arterijskog tlaka u prvoj fazi, kasnijim dvofaznim porastom i naposljetku padom venskog tlaka. Smatra se da su promjene krvnog tlaka povezane s oslobađanjem endogenog acetilkolina iz muskarinskih receptora kao odgovora našeg organizma na otrov, iako to nije sasvim razjašnjeno.…”

Celebrating 120 Years of Butantan Institute Contributions for Toxinology

“…The venom of snakes was approached in different aspects as the structural and functional variability in the composition of venoms from individual snakes [1], the mechanisms of action of whole venoms [2,3], the mechanisms of action of individual components as crotoxin [4], phospholipases A2 [5], metalloproteinases [6][7][8], and the oral immunity induced by whole venoms and their components [9]. Venoms from other animals are also reported; the venoms of centipedes [10], scorpions [11,12], fishes [13,14], and caterpillars [15], including microbial toxins [16]. The great potential for molecules derived from animal venoms as drug leads was also reviewed [17], and the antimicrobial [18], anticoagulant [19,20], and analgesic [21,22] effects have been highlighted in original studies reported here.…”