title: Impact of regional variation in Bothrops asper snake venom on the design of antivenoms: integrating antivenomics and neutralization approaches.
abstract: Intraspecific snake venom variations have implications in the preparation of venom pools for the generation of antivenoms. The impact of such variation in the cross-reactivity of antivenoms against Bothrops asper venom was assessed by comparing two commercial and four experimental antivenoms. All antivenoms showed similar immunorecognition pattern toward the venoms from adult and neonate specimens. They completely immunodepleted most P-III snake venom metalloproteinases (SVMPs), l-amino acid oxidases, serine proteinases, DC fragments, cysteine-rich secretory proteins (CRISPs), and C-type lectin-like proteins, and partially immunodepleted medium-sized disintegrins, phospholipases A(2) (PLA(2)s), some serine proteinases, and P-I SVMPs. Although all antivenoms abrogated the lethal, hemorrhagic, coagulant, proteinase, and PLA(2) venoms activities, monospecific experimental antivenoms were more effective than the polyspecific experimental antivenom. In addition, the commercial antivenoms, produced in horses subjected to repeated immunization cycles, showed higher neutralization than experimental polyspecific antivenom, produced by a single round of immunization. Overall, a conspicuous pattern of cross-neutralization was evident for all effects by all antivenoms, and monospecific antivenoms raised against venom from the Caribbean population were effective against venom from the Pacific population, indicating that geographic variations in venom proteomes of B. asper from Costa Rica do not result in overt variations in immunological cross-reactivity between antivenoms.
authors.affiliation: Instituto Clodomiro Picado, Facultad de Microbiologia, Universidad de Costa Rica, San Jose, Costa Rica. jose.gutierrez@ucr.ac.cr
authors.forename: José María
authors.initials: JM
authors.lastname: Gutiérrez
authors.forename: Libia
authors.initials: L
authors.lastname: Sanz
authors.forename: Marietta
authors.initials: M
authors.lastname: Flores-Díaz
authors.forename: Lucía
authors.initials: L
authors.lastname: Figueroa
authors.forename: Marvin
authors.initials: M
authors.lastname: Madrigal
authors.forename: María
authors.initials: M
authors.lastname: Herrera
authors.forename: Mauren
authors.initials: M
authors.lastname: Villalta
authors.forename: Guillermo
authors.initials: G
authors.lastname: León
authors.forename: Ricardo
authors.initials: R
authors.lastname: Estrada
authors.forename: Adolfo
authors.initials: A
authors.lastname: Borges
authors.forename: Alberto
authors.initials: A
authors.lastname: Alape-Girón
authors.forename: Juan J
authors.initials: JJ
authors.lastname: Calvete
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000997:Antivenins / Q000737:chemistry* / Q000378:metabolism; D015153:Blotting, Western; D017837:Bothrops / Q000235:genetics* / Q000378:metabolism; D003435:Crotalid Venoms / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D054501:Group II Phospholipases A2 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D009500:Neutralization Tests; D030162:Reptilian Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D000997:Antivenins; D003435:Crotalid Venoms; D030162:Reptilian Proteins; D054501:Group II Phospholipases A2