Engineered protein containing crotoxin epitopes induces neutralizing antibodies in immunized rabbits

Molina, Denis Alexis Molina; Guerra-Duarte, Clara; Costal-Oliveira, Fernanda; Rocha, Elizângela Almeida; Rodrigues, Carolina Rego; Machado-de-Ávila, Ricardo Andrez; Soccol, Vanete Thomaz; Chávez-Olórtegui, Carlos

doi:10.1016/j.molimm.2020.01.012

Cited by 5 publications

(2 citation statements)

References 28 publications

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“…In parallel, transcriptomic/proteomic studies of other medically important species could help demonstrate the degree of shared components along the basin. As a consequence of such studies, preparation of chimeric proteins containing epitopes from main toxic and immunogenic Tityus venom components of the LCA/Colombian/Amazonian corridor, as similarly designed for crotoxin [ 105 ], would be instrumental as representative antigens for the preparation of neutralizing antibodies with a broad range of efficacy.…”

Section: Antivenom Neutralization Efficiency and Antigenicity Of Amazonian Scorpion Toxic Componentsmentioning

confidence: 99%

Amazonian scorpions and scorpionism: integrating toxinological, clinical, and phylogenetic data to combat a human health crisis in the world’s most diverse rainfores

Borges

Graham

Cândido

et al. 2021

J. Venom. Anim. Toxins incl. Trop. Dis

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Venom from Amazonian scorpions of the genus Tityus contains components capable of eliciting a distinct clinical, mostly neurological, syndrome. This contrasts with the mainly autonomic manifestations produced after envenomation by congeneric southern and northern South American species. Herein, we summarize Pan-Amazonian scorpionism by synthesizing available toxinological, clinical, and molecular data gathered from all affected areas in Amazonia, including Brazil, Ecuador, Colombia, Peru, Venezuela, and French Guiana. We searched multiple databases, as well as our own records, for reports of scorpion envenomations in Amazonia by confirmed Tityus spp., and compared the clinical manifestations. To help uncover clinical and venom relationships among problematic species, we explored phylogenetic relationships with a rate-calibrated analysis of mitochondrial COI data from available species. The possible existence of diversity gradients for venom toxic and immunogenic components despite the predicted strong phylogenetic association among species is underscored by discussed clinical and toxinological findings. A multicentric effort, involving all nations affected by this neglected disease, is urgently needed to offer alternatives for treating and understanding this pathology, including the preparation of neutralizing antibodies with a broad range of efficacy.

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Section: Antivenom Neutralization Efficiency and Antigenicity Of Amazonian Scorpion Toxic Componentsmentioning

confidence: 99%

Amazonian scorpions and scorpionism: integrating toxinological, clinical, and phylogenetic data to combat a human health crisis in the world’s most diverse rainfores

Borges

Graham

Cândido

et al. 2021

J. Venom. Anim. Toxins incl. Trop. Dis

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“…Concerning Crotalus envenomation, crotoxin complex CA/CB and Crotamine are the main toxins associated with poisonings, besides the enzymatic activities of proteases in the crotalid venoms; therefore, the neutralization of these proteins, as well as some proteases, are key in the production process of commercial antivenoms against Crotalus spp. [10]. It is known that some commercial antivenoms have shown a lower affinity to the crotoxin complex or the CB region thereof when they have been compared with antivenoms obtained by immunization only with Crotoxin (CA/CB) or with only the CB subunit [11,12].…”

Section: Introductionmentioning

confidence: 99%

Crotoxin B: Heterologous Expression, Protein Folding, Immunogenic Properties, and Irregular Presence in Crotalid Venoms

Mejía-Sánchez

Clement

Corrales-García

et al. 2022

Toxins

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Crotoxin complex CA/CB and crotamine are the main toxins associated with Crotalus envenomation besides the enzymatic activities of phospholipases (PLA2) and proteases. The neutralization at least of the crotoxin complex by neutralizing the subunit B could be a key in the production process of antivenoms against crotalids. Therefore, in this work, a Crotoxin B was recombinantly expressed to evaluate its capacity as an immunogen and its ability to produce neutralizing antibodies against crotalid venoms. A Crotoxin B transcript from Crotalus tzabcan was cloned into a pCR®2.1-TOPO vector (Invitrogen, Waltham, MA, USA) and subsequently expressed heterologously in bacteria. HisrCrotoxin B was extracted from inclusion bodies and refolded in vitro. The secondary structure of HisrCrotoxin B was comparable to the secondary structure of the native Crotoxin B, and it has PLA2 activity as the native Crotoxin B. HisrCrotoxin B was used to immunize rabbits, and the obtained antibodies partially inhibited the activity of PLA2 from C. tzabcan. The anti-HisrCrotoxin B antibodies neutralized the native Crotoxin B and the whole venoms from C. tzabcan, C. s. salvini, and C. mictlantecuhtli. Additionally, anti-HisrCrotoxin B antibodies recognized native Crotoxin B from different Crotalus species, and they could discriminate venom in species with high or low levels of or absence of Crotoxin B.

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Biological and proteomic characterization of the venom from Peruvian Andes rattlesnake Crotalus durissus

Rodrigues

Molina

Souza

et al. 2022

Toxicon

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Engineered protein containing crotoxin epitopes induces neutralizing antibodies in immunized rabbits

Cited by 5 publications

References 28 publications

Amazonian scorpions and scorpionism: integrating toxinological, clinical, and phylogenetic data to combat a human health crisis in the world’s most diverse rainfores

Amazonian scorpions and scorpionism: integrating toxinological, clinical, and phylogenetic data to combat a human health crisis in the world’s most diverse rainfores

Crotoxin B: Heterologous Expression, Protein Folding, Immunogenic Properties, and Irregular Presence in Crotalid Venoms

Biological and proteomic characterization of the venom from Peruvian Andes rattlesnake Crotalus durissus

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