A comparative analysis of the proteomes and biological activities of the venoms from two sea snakes, Hydrophis curtus and Hydrophis cyanocinctus, from Hainan, China

Wang, Bo; Wang, Qianqian; Chao, Wang; Wang, Beilei; Qiu, Lei‐Lei; Zou, Shuaijun; Zhang, Fuhai; Liu, Guoyan; Zhang, Liming

doi:10.1016/j.toxicon.2020.08.012

Cited by 11 publications

(11 citation statements)

References 63 publications

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“…Here, we deployed a classic snake venomic workflow combined with RP-HPLC, SDA-PAGE and MS analyses [34] to decomplex the venomic profile of a pooled crude venom sample of H. cyanocinctus. With regard to the relative abundance of toxins at the protein level, 3-FTx and PLA 2 could be defined as predominant toxin families, and this was similar to two previous venomic studies using samples from populations from Hara, Iran [19], and Haikou, Hainan, China [21]. However, the Xisha population exhibited the lowest abundance of 3-FTx but the highest abundance of PLA 2 among the three populations and a comparatively low divergence between these two toxin families.…”

Section: Discussionsupporting

confidence: 85%

“…Compared with their terrestrial relatives, sea snakes tend to simplify venom components to the extreme at the protein level [ 18 ]. Sea-snake venoms are mainly comprised of three-finger toxins (3-FTxs) and phospholipase A 2 (PLA 2 ) [ 19 , 20 , 21 , 22 , 23 , 24 ], with the short- and long-chain neurotoxins of 3-FTxs being the major and strong neurotoxic components [ 25 , 26 ]. Most sea snakes have to deal with fast-moving prey and, as such, the lethal neurotoxic venom can help them to quickly paralyze or kill prey almost instantaneously without letting them escape and avoid hurting themselves in the prey struggle [ 18 ].…”

Section: Introductionmentioning

confidence: 99%

“…In order to better understand and protect H. cyanocinctus , we need to know more about the diversity, evolution and function of its venom. The profiles of H. cyanocinctus venom at the omics level remain a sparsely studied area, with only two previous studies on the proteomic diversity of venom samples from Haikou, China [ 21 ], and Hara, Iran [ 19 , 21 ]. Here, we investigated the venom composition profile of H. cyanocinctus from the Xisha (Paracel) Islands in the South China Sea (Hainan, China) using a classical strategy for venomic analysis [ 34 ] and the toxin-coding genes profile in the venom-gland transcriptome with a de novo NGS technique.…”

Section: Introductionmentioning

confidence: 99%

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Venom of the Annulated Sea Snake Hydrophis cyanocinctus: A Biochemically Simple but Genetically Complex Weapon

Zhao

Sun

et al. 2021

Toxins

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Given that the venom system in sea snakes has a role in enhancing their secondary adaption to the marine environment, it follows that elucidating the diversity and function of venom toxins will help to understand the adaptive radiation of sea snakes. We performed proteomic and de novo NGS analyses to explore the diversity of venom toxins in the annulated sea snake (Hydrophis cyanocinctus) and estimated the adaptive molecular evolution of the toxin-coding unigenes and the toxicity of the major components. We found three-finger toxins (3-FTxs), phospholipase A2 (PLA2) and cysteine-rich secretory protein (CRISP) in the venom proteome and 59 toxin-coding unigenes belonging to 24 protein families in the venom-gland transcriptome; 3-FTx and PLA2 were the most abundant families. Nearly half of the toxin-coding unigenes had undergone positive selection. The short- (i.p. 0.09 μg/g) and long-chain neurotoxin (i.p. 0.14 μg/g) presented fairly high toxicity, whereas both basic and acidic PLA2s expressed low toxicity. The toxicity of H. cyanocinctus venom was largely determined by the 3-FTxs. Our data show the venom is used by H. cyanocinctus as a biochemically simple but genetically complex weapon and venom evolution in H. cyanocinctus is presumably driven by natural selection to deal with fast-moving prey and enemies in the marine environment.

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Section: Discussionsupporting

confidence: 85%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Venom of the Annulated Sea Snake Hydrophis cyanocinctus: A Biochemically Simple but Genetically Complex Weapon

Zhao

Sun

et al. 2021

Toxins

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“…This protein family has only been recorded from cobra venoms with two exceptions, the sea snake Hydrophis cyanocinctus (0.2%), and the pit viper Trimeresurus insularis (1%) (Jones et al 2019;Wang et al 2020). The largest amounts recorded were in king cobra Ophiophagus hannah (2.8 to 5.5%) (Tan et al 2015;Vonk et al 2013).…”

Section: Cobra Venom Factor (Cvf)mentioning

confidence: 99%

A current perspective on snake venom composition and constituent protein families

Tasoulis

2022

Arch Toxicol

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Snake venoms are heterogeneous mixtures of proteins and peptides used for prey subjugation. With modern proteomics there has been a rapid expansion in our knowledge of snake venom composition, resulting in the venom proteomes of 30% of vipers and 17% of elapids being characterised. From the reasonably complete proteomic coverage of front-fanged snake venom composition (179 species-68 species of elapids and 111 species of vipers), the venoms of vipers and elapids contained 42 different protein families, although 18 were only reported in < 5% of snake species. Based on the mean abundance and occurrence of the 42 protein families, they can be classified into 4 dominant, 6 secondary, 14 minor, and 18 rare protein families. The dominant, secondary and minor categories account for 96% on average of a snake's venom composition. The four dominant protein families are: phospholipase A 2 (PLA 2 ), snake venom metalloprotease (SVMP), three-finger toxins (3FTx), and snake venom serine protease (SVSP). The six secondary protein families are: L-amino acid oxidase (LAAO), cysteine-rich secretory protein (CRiSP), C-type lectins (CTL), disintegrins (DIS), kunitz peptides (KUN), and natriuretic peptides (NP). Venom variation occurs at all taxonomic levels, including within populations. The reasons for venom variation are complex, as variation is not always associated with geographical variation in diet. The four dominant protein families appear to be the most important toxin families in human envenomation, being responsible for coagulopathy, neurotoxicity, myotoxicity and cytotoxicity. Proteomic techniques can be used to investigate the toxicological profile of a snake venom and hence identify key protein families for antivenom immunorecognition.

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“…The venoms of the spine-bellied sea snake Hydrophis curtus and the annulated sea snake Hydrophis cyanocinctus aroused the greatest interest. Both venom proteomes [ 215 , 216 , 217 , 218 , 219 , 220 ] and venom gland transcriptomes [ 219 , 220 , 221 ] were characterized for these species of different geographical origin. The main finding of all these works is that the α-neurotoxins of both short-chain and long-chain types represent the most abundant toxin family in these snakes.…”

Section: Marine Protein Ligands Of Nachr—still An Open Field For Rese...mentioning

confidence: 99%

Marine Origin Ligands of Nicotinic Receptors: Low Molecular Compounds, Peptides and Proteins for Fundamental Research and Practical Applications

et al. 2022

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The purpose of our review is to briefly show what different compounds of marine origin, from low molecular weight ones to peptides and proteins, offer for understanding the structure and mechanism of action of nicotinic acetylcholine receptors (nAChRs) and for finding novel drugs to combat the diseases where nAChRs may be involved. The importance of the mentioned classes of ligands has changed with time; a protein from the marine snake venom was the first excellent tool to characterize the muscle-type nAChRs from the electric ray, while at present, muscle and α7 receptors are labeled with the radioactive or fluorescent derivatives prepared from α-bungarotoxin isolated from the many-banded krait. The most sophisticated instruments to distinguish muscle from neuronal nAChRs, and especially distinct subtypes within the latter, are α-conotoxins. Such information is crucial for fundamental studies on the nAChR revealing the properties of their orthosteric and allosteric binding sites and mechanisms of the channel opening and closure. Similar data are provided by low-molecular weight compounds of marine origin, but here the main purpose is drug design. In our review we tried to show what has been obtained in the last decade when the listed classes of compounds were used in the nAChR research, applying computer modeling, synthetic analogues and receptor mutants, X-ray and electron-microscopy analyses of complexes with the nAChRs, and their models which are acetylcholine-binding proteins and heterologously-expressed ligand-binding domains.

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A comparative analysis of the proteomes and biological activities of the venoms from two sea snakes, Hydrophis curtus and Hydrophis cyanocinctus, from Hainan, China

Cited by 11 publications

References 63 publications

Venom of the Annulated Sea Snake Hydrophis cyanocinctus: A Biochemically Simple but Genetically Complex Weapon

Venom of the Annulated Sea Snake Hydrophis cyanocinctus: A Biochemically Simple but Genetically Complex Weapon

A current perspective on snake venom composition and constituent protein families

Marine Origin Ligands of Nicotinic Receptors: Low Molecular Compounds, Peptides and Proteins for Fundamental Research and Practical Applications

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