Impact of regional variation in Bothrops asper snake venom on the design of antivenoms: integrating antivenomics and neutralization approaches.
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.
Gutiérrez
José María
JM
Instituto Clodomiro Picado, Facultad de Microbiologia, Universidad de Costa Rica, San Jose, Costa Rica. jose.gutierrez@ucr.ac.cr
Sanz
Libia
L
Flores-Díaz
Marietta
M
Figueroa
Lucía
L
Madrigal
Marvin
M
Herrera
María
M
Villalta
Mauren
M
León
Guillermo
G
Estrada
Ricardo
R
Borges
Adolfo
A
Alape-Girón
Alberto
A
Calvete
Juan J
JJ
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
D000997:Antivenins; D003435:Crotalid Venoms; D030162:Reptilian Proteins; D054501:Group II Phospholipases A2