Hemolitic action of Naja naja atra cardiotoxin on erythrocytes from different animals

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Abstract

A comparative study on the sensitivity of erythrocytes from different vertebrate species (avian, mammalian and reptilian) to the hemolytic action caused by cardiotoxin isolated from Naja naja atra venom was carried out. Cardiotoxin was able to induce direct hemolysis in washed erythrocytes from several animals, except for llama. The EC50 values from hemolysis of the most sensitive (cat) and the most resistant (snake) animal varied approximately tenfold. According to the cell behavior, it was possible to characterize four types of behavior: The first was observed in cat, horse and human cells; the second in rat, rabbit and dog erythrocytes; and the third only in llama erythrocytes, which were resistant to cardiotoxin concentrations up to 300 µg/ml. Finally, avian and reptilian erythrocytes were more resistant to cardiotoxin III-induced hemolysis than those of the mammalian species.

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Lipid composition of erythrocytes in various mammalian species

Gary Nelson (1967)

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Two distinct types of cardiotoxin as revealed by the structure and activity relationship of their interaction with zwitterionic phospholipid dispersions.

Y C Hseu, Chang-wen Wu, B Rule … (1994)

Cardiotoxins (CTXs) are a group of homologous proteins found in cobra snake venom and consist of 60-62 amino acid residues. Although CTXs are known to consist of three extended beta-sheet loops similar to neurotoxins, the target and interaction of CTXs with membranes unlike those of neurotoxins are not well understood. Herein, we report comparative studies of 10 CTXs purified from Taiwan cobra (Naja naja atra) and Mozambique spitting cobra (Naja mossambica mossambica) snake venoms with respect to their interactions with zwitterionic phospholipids. Based on the CTX-induced mixing of sphingomyelin vesicles and the binding of CTX to lysophosphatidylcholine micelles, two distinct types of CTX, i.e. P- and S-type CTX, are identified. P-type CTXs are characterized by the presence of Pro-31 within a putative phospholipid binding site near the tip of loop 2; whereas S-type CTXs are characterized by the presence of Ser-29 within the same but more hydrophilic region. Although binding of all CTXs to phospholipid membranes involves a phospholipid binding site at loop 1, P-type CTXs exhibit higher fusion and binding activity than S-type CTXs, presumably due to the additional phospholipid binding site at loop 2. The binding modes of P- and S-type CTX are thus different. Analysis of the primary structures of 46 CTXs from the genus Naja indicates that these two types of CTXs exist in all species examined. Reasonable structure/activity correlation can be detected for the effects of CTXs on muscle and red blood cells, although notable exceptions are also found. S-type CTXs are generally found to exhibit higher muscle cell depolarization activity, whereas P-type CTXs are found to possess a higher hemolytic activity. Thus the mechanism of action of CTXs seems to involve CTX-membrane interactions and depends on the type of the cell membrane and CTX molecules under study. The two lipid binding sites in P-type CTXs and one lipid binding site in S-type CTXs show large variation in their amino acid residues, but they do display some common distribution of residue type. Analogous to the signal sequences for protein import, these regions are characterized by the coexistence of an exposed hydrophobic surface flanked on either side by a cationic residue. A hypothesis is proposed to explain the general cytotoxic and specific cardiotoxic effect of CTXs based on the two CTX subtypes in snake venom.