Next Article in Journal
In Vitro Induction of Erythrocyte Phosphatidylserine Translocation by the Natural Naphthoquinone Shikonin
Next Article in Special Issue
Diagnosis of Snakebite and the Importance of Immunological Tests in Venom Research
Previous Article in Journal
Role of Fc in Antibody-Mediated Protection from Ricin Toxin
Toxins 2014, 6(5), 1526-1558; doi:10.3390/toxins6051526
Article

Ophiophagus hannah Venom: Proteome, Components Bound by Naja kaouthia Antivenin and Neutralization by N. kaouthia Neurotoxin-Specific Human ScFv

1
, 2
, 3
, 4
, 4
, 4,5
, 6
, 5
, 4,7
 and 4,5,*
1 Graduate Program in Immunology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok 10700, Thailand 2 Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University, Bangkok 10400, Thailand 3 Department of Research and Development, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok 10700, Thailand 4 Laboratory for Research and Technology Development, Department of Parasitology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok 10700, Thailand 5 Graduate Program in Biomedical Science, Faculty of Allied Health Sciences, Thammasat University, Pathumthani 12120, Thailand 6 Center for Agriculture Biotechnology and Department of Veterinary Pathology, Faculty of Veterinary Medicine, Kasetsart University, Kam-paeng-saen Campus, Nakhon-pathom 73140, Thailand 7 Department of Microbiology and Immunology, Faculty of Veterinary Medicine, Kasetsart University, Bangkok 10900, Thailand
* Author to whom correspondence should be addressed.
Received: 15 February 2014 / Revised: 20 April 2014 / Accepted: 5 May 2014 / Published: 13 May 2014
(This article belongs to the Special Issue Antivenom and Venom Therapeutics)
View Full-Text   |   Download PDF [1418 KB, 14 May 2014; original version 13 May 2014]   |   Browse Figures

Abstract

Venomous snakebites are an important health problem in tropical and subtropical countries. King cobra (Ophiophagus hannah) is the largest venomous snake found in South and Southeast Asia. In this study, the O. hannah venom proteome and the venom components cross-reactive to N. kaouthia monospecific antivenin were studied. O. hannah venom consisted of 14 different protein families, including three finger toxins, phospholipases, cysteine-rich secretory proteins, cobra venom factor, muscarinic toxin, L-amino acid oxidase, hypothetical proteins, low cysteine protein, phosphodiesterase, proteases, vespryn toxin, Kunitz, growth factor activators and others (coagulation factor, endonuclease, 5’-nucleotidase). N. kaouthia antivenin recognized several functionally different O. hannah venom proteins and mediated paratherapeutic efficacy by rescuing the O. hannah envenomed mice from lethality. An engineered human ScFv specific to N. kaouthia long neurotoxin (NkLN-HuScFv) cross-neutralized the O. hannah venom and extricated the O. hannah envenomed mice from death in a dose escalation manner. Homology modeling and molecular docking revealed that NkLN-HuScFv interacted with residues in loops 2 and 3 of the neurotoxins of both snake species, which are important for neuronal acetylcholine receptor binding. The data of this study are useful for snakebite treatment when and where the polyspecific antivenin is not available. Because the supply of horse-derived antivenin is limited and the preparation may cause some adverse effects in recipients, a cocktail of recombinant human ScFvs for various toxic venom components shared by different venomous snakes, exemplified by the in vitro produced NkLN-HuScFv in this study, should contribute to a possible future route for an improved alternative to the antivenins.
Keywords: antivenin; human ScFv (HuScFv); paraspecificity; Naja kaouthia; Ophiophagus hannah; proteome antivenin; human ScFv (HuScFv); paraspecificity; Naja kaouthia; Ophiophagus hannah; proteome
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Share & Cite This Article

Export to BibTeX |
EndNote


MDPI and ACS Style

Danpaiboon, W.; Reamtong, O.; Sookrung, N.; Seesuay, W.; Sakolvaree, Y.; Thanongsaksrikul, J.; Dong-din-on, F.; Srimanote, P.; Thueng-in, K.; Chaicumpa, W. Ophiophagus hannah Venom: Proteome, Components Bound by Naja kaouthia Antivenin and Neutralization by N. kaouthia Neurotoxin-Specific Human ScFv. Toxins 2014, 6, 1526-1558.

View more citation formats

Related Articles

Article Metrics

Comments

Citing Articles

[Return to top]
Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert