Publication:
Corrigendum to: “venomics of the poorly studied hognosed pitvipers porthidium arcosae and porthidium volcanicum”

dc.contributor.authorRuiz Campos, Marco
dc.contributor.authorSanz, Libia
dc.contributor.authorBonilla Murillo, Fabián
dc.contributor.authorMahmood M., Sasa
dc.contributor.authorLomonte Vigliotti, Bruno
dc.contributor.authorZaruma Torres, Fausto Leonardo
dc.contributor.authorTeran Zavala, Maria Del carmen
dc.contributor.authorFernandez Ulate, Julian
dc.contributor.authorCalvete Chornet, Juan José
dc.contributor.authorCaldeira, Cleópatra Alves da Silva
dc.contributor.authorDa Silva, Saulo Luis
dc.date.accessioned2022-03-02T16:54:42Z
dc.date.available2022-03-02T16:54:42Z
dc.date.issued2019
dc.description.abstractWe report the first proteomics analyses of the venoms of two poorly studied snakes, the Manabi hognosed pitviper Porthidium arcosae endemic to the western coastal province of Manabí (Ecuador), and the Costa Rican hognosed pitviper P. volcanicum with distribution restricted to South Pacific Costa Rica and western Panamá. These venom proteomes share a conserved compositional pattern reported in four other congeneric species within the clade of South American Porthidium species, P. nasutum, P. lansbergii, P. ophryomegas, and P. porrasi. The paraspecific immunorecognition profile of antivenoms produced in Costa Rica (ICP polyvalent), Perú (Instituto Nacional de Salud) and Brazil (soro antibotrópico pentavalente, SAB, from Instituto Butantan) against the venom of P. arcosae was investigated through a third-generation antivenomics approach. The maximal venom-binding capacities of the investigated antivenoms were 97.1 mg, 21.8 mg, and 25.7 mg of P. arcosae venom proteins per gram of SAB, ICP, and INS-PERU antibody molecules, respectively, which translate into 28.4 mg, 13.1 mg, and 15.2 mg of total venom proteins bound per vial of SAB, ICP, and INS-PERU AV. The antivenomics results suggest that 21.8%, 7.8% and 6.1% of the SAB, ICP, and INS-PERU antibody molecules recognized P. arcosae venom toxins. The SAB antivenom neutralized P. arcosae venom's lethality in mice with an ED50 of 31.3 mgV/g SAB AV. This preclinical neutralization paraspecificity points to Brazilian SAB as a promising candidate for the treatment of envenomings by Ecuadorian P. arcosae. BIOLOGICAL SIGNIFICANCE: Assessing the preclinical efficacy profile of antivenoms against homologous and heterologous medically relevant snake venoms represents an important goal towards defining the biogeographic range of their clinical utility. This is particularly relevant in regions, such as Mesoamerica, where a small number of pharmaceutical companies produce antivenoms against the venoms of a small number of species of maximum medical relevance among the local rich herpetofauna, leaving a wide range of snakes of secondary medical relevance, but also causing life-threatening human envenomings without nominal clinical coverage. This work is part of a larger project aiming at mapping the immunological characteristics of antivenoms generated in Latin American countries towards venoms of such poorly studied snakes of the local and neighboring countries' herpetofauna. Here we report the proteomics characterization of the Manabi hognosed pitviper Porthidium arcosae endemic to the western coastal province of Manabí (Ecuador), and the Costa Rican hognosed pitviper P. volcanicum with distribution restricted to southwestern Costa Rica, the antivenomics assessment of three bothropoid commercial antivenoms produced in Costa Rica, Perú, and Brazil against the venom components of P. arcosae, and the in vivo capacity of the Brazilian soro antibotrópico pentavalente (SAB) from Instituto Butantan to neutralize the murine lethality of P. arcosae venom. The preclinical paraspecific ED50 of 31.3 mg of P. arcosae venom per gram of antivenom points to Brazilian SAB as a promising candidate for the treatment of envenomings by the Manabi hognosed pitviper P. arcosae.
dc.identifier.doi10.1016/j.jprot.2021.104391
dc.identifier.issn1874-3919
dc.identifier.urihttps://www.scopus.com/record/display.uri?eid=2-s2.0-85116833150&origin=inward&txGid=4ef08defc21c52e43e3ca2519714bce4
dc.language.isoes_ES
dc.sourceJournal of Proteomics
dc.subjectAntivenomics
dc.subjectGenus porthidium
dc.subjectLatin American antivenoms
dc.subjectPorthidium arcosae
dc.subjectPorthidium volcanicum
dc.subjectSnake venomics
dc.titleCorrigendum to: “venomics of the poorly studied hognosed pitvipers porthidium arcosae and porthidium volcanicum”
dc.typeARTÍCULO
dc.ucuenca.afiliacionRuiz, M., Universidad de Costa Rica, San José, Costa rica
dc.ucuenca.afiliacionSanz, L., Laboratorio de Venómica Evolutiva y Traslacional, Valencia, España
dc.ucuenca.afiliacionBonilla, F., Universidad de Costa Rica, San José, Costa rica
dc.ucuenca.afiliacionMahmood, S., Universidad de Costa Rica, San José, Costa rica
dc.ucuenca.afiliacionLomonte, B., Universidad de Costa Rica, San José, Costa rica
dc.ucuenca.afiliacionZaruma, F., Universidad de Cuenca, Facultad de Ciencias Químicas, Cuenca, Ecuador
dc.ucuenca.afiliacionTeran, M., Instituto Nacional de Investigación en Salud Pública (INSPI), Guayaquil, Ecuador
dc.ucuenca.afiliacionFernandez, J., Universidad de Costa Rica, San José, Costa rica
dc.ucuenca.afiliacionCalvete, J., Laboratorio de Venómica Evolutiva y Traslacional, Valencia, España
dc.ucuenca.afiliacionCaldeira, C., Ministério da Saúde, Centro de Estudos de Biomoléculas Aplicadas á Saúde (CEBio), Porto Velho, Brasil
dc.ucuenca.afiliacionDa, S., Universidad de Cuenca, Facultad de Ciencias Químicas, Cuenca, Ecuador
dc.ucuenca.areaconocimientofrascatiamplio1. Ciencias Naturales y Exactas
dc.ucuenca.areaconocimientofrascatidetallado1.6.4 Bioquímica y Biología Molecular
dc.ucuenca.areaconocimientofrascatiespecifico1.6 Ciencias Biológicas
dc.ucuenca.areaconocimientounescoamplio09 - Salud y Bienestar
dc.ucuenca.areaconocimientounescodetallado0914 - Tecnologías de Diagnóstico y Tratamiento Médico
dc.ucuenca.areaconocimientounescoespecifico091 - Salud
dc.ucuenca.correspondenciaCalvete Chornet, Juan José, jcalvete@ibv.csic.es
dc.ucuenca.cuartilQ1
dc.ucuenca.factorimpacto1.067
dc.ucuenca.idautor0000-0001-7841-472X
dc.ucuenca.idautor0000-0003-4991-9598
dc.ucuenca.idautor0000-0002-5095-2750
dc.ucuenca.idautor0000-0003-0118-5142
dc.ucuenca.idautorSgrp-5077-005
dc.ucuenca.idautor1102127980
dc.ucuenca.idautor0919153874
dc.ucuenca.idautorSgrp-5077-008
dc.ucuenca.idautor0000-0001-5026-3122
dc.ucuenca.idautor0000-0003-1670-5227
dc.ucuenca.idautor1757872526
dc.ucuenca.indicebibliograficoSCOPUS
dc.ucuenca.numerocitaciones3191
dc.ucuenca.urifuentehttps://www.sciencedirect.com/journal/journal-of-proteomics/vol/250/suppl/C
dc.ucuenca.versionVersión publicada
dc.ucuenca.volumenVolumen 250
dspace.entity.typePublication
relation.isAuthorOfPublicationbef04eb7-e7cb-4a41-a360-9c091399935d
relation.isAuthorOfPublication.latestForDiscoverybef04eb7-e7cb-4a41-a360-9c091399935d

Files

Original bundle

Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
documento.pdf
Size:
484.43 KB
Format:
Adobe Portable Document Format
Description:
document

Collections