Literature DB >> 33894246

Neutralization of crotamine by polyclonal antibodies generated against two whole rattlesnake venoms and a novel recombinant fusion protein.

Roberto Ponce-López1, Edgar Neri-Castro1, Felipe Olvera-Rodríguez1, Elda E Sánchez2, Alejandro Alagón1, Alejandro Olvera-Rodríguez3.   

Abstract

Crotamine is a paralyzing toxin (MW: ~5 kDa) found in different proportions in some rattlesnake venoms (up to 62%). Mexican pit viper antivenoms have shown low immunoreactivity against crotamine, which is an urgent quality to be improved. The objective of this work was to evaluate the ability of a novel recombinant fusion protein composed of sphingomyelinase D and crotamine, and two whole venoms from Crotalus molossus nigrescens and C. oreganus helleri to produce neutralizing antibodies against crotamine. These immunogens were separately used for immunization procedures in rabbits. Then, we generated three experimental antivenoms to test their cross-reactivity via western-blot against crotamine from 7 species (C. m. nigrescens, C. o. helleri, C. durissus terrificus, C. scutulatus salvini, C. basiliscus, C. culminatus and C. tzabcan). We also performed pre-incubation neutralization experiments in mice to measure the neutralizing potency of each antivenom against crotamine induced hind limb paralysis. Our antivenoms showed broad recognition across crotamine from most of the tested species. Also, neutralization against crotamine paralysis symptom was successfully achieved by our three antivenoms, albeit with different efficiencies. Our results highlight the use of crotamine enriched venoms and our novel recombinant fusion protein as promising immunogens to improve the neutralizing potency against crotamine for the improvement of Mexican antivenoms.
Copyright © 2021 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  Antivenom; Crotamine; Immunogen; Rattlesnake; Recluse-spider

Mesh:

Substances:

Year:  2021        PMID: 33894246      PMCID: PMC8204659          DOI: 10.1016/j.toxicon.2021.04.005

Source DB:  PubMed          Journal:  Toxicon        ISSN: 0041-0101            Impact factor:   3.033


  52 in total

1.  The electrophoretic analysis of snake venoms.

Authors:  J M GONCALVES; A POLSON
Journal:  Arch Biochem       Date:  1947-05

2.  Cloning and nucleotide sequences of crotamine genes.

Authors:  L A Smith; J J Schmidt
Journal:  Toxicon       Date:  1990       Impact factor: 3.033

3.  A new small myotoxin from the venom of the prairie rattlesnake (Crotalus viridis viridis).

Authors:  P R Griffin; S D Aird
Journal:  FEBS Lett       Date:  1990-11-12       Impact factor: 4.124

4.  In vivo test of the ability of antiserum to myotoxin a from prairie rattlesnake (Crotalus viridis viridis) venom to neutralize local myonecrosis induced by myotoxin a and homologous crude venom.

Authors:  C L Ownby; T R Colberg; P L Claypool; G V Odell
Journal:  Toxicon       Date:  1984       Impact factor: 3.033

5.  The effects of hybridization on divergent venom phenotypes: Characterization of venom from Crotalus scutulatus scutulatus × Crotalus oreganus helleri hybrids.

Authors:  Cara Francesca Smith; Stephen P Mackessy
Journal:  Toxicon       Date:  2016-08-03       Impact factor: 3.033

6.  Quantitation of myonecrosis induced by myotoxin a from prairie rattlesnake (Crotalus viridis viridis) venom.

Authors:  C L Ownby; J M Gutiérrez; T R Colberg; G V Odell
Journal:  Toxicon       Date:  1982       Impact factor: 3.033

7.  Ability of antiserum to myotoxin alpha from prairie rattlesnake (Crotalus viridis viridis) venom to neutralize local myotoxicity and lethal effects of myotoxin alpha and homologous crude venom.

Authors:  C L Ownby; G V Odell; W M Woods; T R Colberg
Journal:  Toxicon       Date:  1983       Impact factor: 3.033

8.  Amino acid sequence of a myotoxin from venom of the eastern diamondback rattlesnake (Crotalus adamanteus).

Authors:  Y Samejima; Y Aoki; D Mebs
Journal:  Toxicon       Date:  1991       Impact factor: 3.033

9.  Generation and characterization of a recombinant chimeric protein (rCpLi) consisting of B-cell epitopes of a dermonecrotic protein from Loxosceles intermedia spider venom.

Authors:  T M Mendes; D Oliveira; L F M Figueiredo; R A Machado-de-Avila; C G Duarte; C Dias-Lopes; G Guimarães; L Felicori; J C Minozzo; C Chávez-Olortegui
Journal:  Vaccine       Date:  2013-05-07       Impact factor: 3.641

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