Tags

Type your tag names separated by a space and hit enter

Venom Proteome of Spine-Bellied Sea Snake (Hydrophis curtus) from Penang, Malaysia: Toxicity Correlation, Immunoprofiling and Cross-Neutralization by Sea Snake Antivenom.
Toxins (Basel). 2018 12 23; 11(1)T

Abstract

The venom proteome of Hydrophis curtus (synonym: Lapemis hardwickii) from Penang, Malaysia was investigated with nano-electrospray ionization-liquid chromatography tandem mass spectrometry (ESI-LCMS/MS) of the reverse-phase high-performance liquid chromatography (HPLC) venom fractions. Thirty distinct protein forms were identified as toxins from ten families. The three major protein families were phospholipase A₂ (PLA₂, 62.0% of total venom proteins), three-finger toxin (3FTX, 26.33%) and cysteine-rich secretory protein (CRiSP, 9.00%). PLA₂ comprises diverse homologues (11 forms), predominantly the acidic subtypes (48.26%). 3FTX composed of one short alpha-neurotoxin (SNTX, 22.89%) and four long alpha-neurotoxins (LNTX, 3.44%). Both SNTX and LNTX were lethal in mice (intravenous LD50 = 0.10 and 0.24 μg/g, respectively) but the PLA₂ were non-lethal (LD50 >1 μg/g). The more abundant and toxic SNTX appeared to be the main driver of venom lethality (holovenom LD50 = 0.20 μg/g). The heterologous Sea Snake Antivenom (SSAV, Australia) effectively cross-neutralized the venom (normalized potency = 9.35 mg venom neutralized per g antivenom) and the two neurotoxins in vivo, with the LNTX being neutralized more effectively (normalized potency = 3.5 mg toxin/g antivenom) than SNTX (normalized potency = 1.57 mg/g). SSAV immunorecognition was strong toward PLA₂ but moderate-to-weak toward the alpha-neurotoxins, indicating that neutralization of the alpha-neurotoxins should be further improved.

Authors+Show Affiliations

Department of Pharmacology, Faculty of Medicine, University of Malaya, Kuala Lumpur 50603, Malaysia. tanch@um.edu.my.Department of Molecular Medicine, Faculty of Medicine, University of Malaya, Kuala Lumpur 50603, Malaysia. kytan_kae@um.edu.my.Department of Molecular Medicine, Faculty of Medicine, University of Malaya, Kuala Lumpur 50603, Malaysia. ngtzushan@um.edu.my.Department of Pharmacology, Faculty of Medicine, University of Malaya, Kuala Lumpur 50603, Malaysia. debrasim@um.edu.my.Department of Molecular Medicine, Faculty of Medicine, University of Malaya, Kuala Lumpur 50603, Malaysia. tanngethong@yahoo.com.sg.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

30583590

Citation

Tan, Choo Hock, et al. "Venom Proteome of Spine-Bellied Sea Snake (Hydrophis Curtus) From Penang, Malaysia: Toxicity Correlation, Immunoprofiling and Cross-Neutralization By Sea Snake Antivenom." Toxins, vol. 11, no. 1, 2018.
Tan CH, Tan KY, Ng TS, et al. Venom Proteome of Spine-Bellied Sea Snake (Hydrophis curtus) from Penang, Malaysia: Toxicity Correlation, Immunoprofiling and Cross-Neutralization by Sea Snake Antivenom. Toxins (Basel). 2018;11(1).
Tan, C. H., Tan, K. Y., Ng, T. S., Sim, S. M., & Tan, N. H. (2018). Venom Proteome of Spine-Bellied Sea Snake (Hydrophis curtus) from Penang, Malaysia: Toxicity Correlation, Immunoprofiling and Cross-Neutralization by Sea Snake Antivenom. Toxins, 11(1). https://doi.org/10.3390/toxins11010003
Tan CH, et al. Venom Proteome of Spine-Bellied Sea Snake (Hydrophis Curtus) From Penang, Malaysia: Toxicity Correlation, Immunoprofiling and Cross-Neutralization By Sea Snake Antivenom. Toxins (Basel). 2018 12 23;11(1) PubMed PMID: 30583590.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Venom Proteome of Spine-Bellied Sea Snake (Hydrophis curtus) from Penang, Malaysia: Toxicity Correlation, Immunoprofiling and Cross-Neutralization by Sea Snake Antivenom. AU - Tan,Choo Hock, AU - Tan,Kae Yi, AU - Ng,Tzu Shan, AU - Sim,Si Mui, AU - Tan,Nget Hong, Y1 - 2018/12/23/ PY - 2018/11/11/received PY - 2018/12/14/revised PY - 2018/12/19/accepted PY - 2018/12/26/entrez PY - 2018/12/26/pubmed PY - 2019/10/11/medline KW - Lapemis hardwickii KW - alpha-neurotoxins KW - envenomation KW - immunoreactivity KW - neutralization KW - phospholipase A2 KW - three-finger toxins JF - Toxins JO - Toxins (Basel) VL - 11 IS - 1 N2 - The venom proteome of Hydrophis curtus (synonym: Lapemis hardwickii) from Penang, Malaysia was investigated with nano-electrospray ionization-liquid chromatography tandem mass spectrometry (ESI-LCMS/MS) of the reverse-phase high-performance liquid chromatography (HPLC) venom fractions. Thirty distinct protein forms were identified as toxins from ten families. The three major protein families were phospholipase A₂ (PLA₂, 62.0% of total venom proteins), three-finger toxin (3FTX, 26.33%) and cysteine-rich secretory protein (CRiSP, 9.00%). PLA₂ comprises diverse homologues (11 forms), predominantly the acidic subtypes (48.26%). 3FTX composed of one short alpha-neurotoxin (SNTX, 22.89%) and four long alpha-neurotoxins (LNTX, 3.44%). Both SNTX and LNTX were lethal in mice (intravenous LD50 = 0.10 and 0.24 μg/g, respectively) but the PLA₂ were non-lethal (LD50 >1 μg/g). The more abundant and toxic SNTX appeared to be the main driver of venom lethality (holovenom LD50 = 0.20 μg/g). The heterologous Sea Snake Antivenom (SSAV, Australia) effectively cross-neutralized the venom (normalized potency = 9.35 mg venom neutralized per g antivenom) and the two neurotoxins in vivo, with the LNTX being neutralized more effectively (normalized potency = 3.5 mg toxin/g antivenom) than SNTX (normalized potency = 1.57 mg/g). SSAV immunorecognition was strong toward PLA₂ but moderate-to-weak toward the alpha-neurotoxins, indicating that neutralization of the alpha-neurotoxins should be further improved. SN - 2072-6651 UR - https://www.unboundmedicine.com/medline/citation/30583590/Venom_Proteome_of_Spine_Bellied_Sea_Snake__Hydrophis_curtus__from_Penang_Malaysia:_Toxicity_Correlation_Immunoprofiling_and_Cross_Neutralization_by_Sea_Snake_Antivenom_ L2 - https://www.mdpi.com/resolver?pii=toxins11010003 DB - PRIME DP - Unbound Medicine ER -