title: Venomic and antivenomic analyses of the Central American coral snake, Micrurus nigrocinctus (Elapidae).
abstract: The proteome of the venom of Micrurus nigrocinctus (Central American coral snake) was analyzed by a "venomics" approach. Nearly 50 venom peaks were resolved by RP-HPLC, revealing a complex protein composition. Comparative analyses of venoms from individual specimens revealed that such complexity is an intrinsic feature of this species, rather than the sum of variable individual patterns of simpler composition. Proteins related to eight distinct families were identified by MS/MS de novo peptide sequencing or N-terminal sequencing: phospholipase A(2) (PLA(2)), three-finger toxin (3FTx), l-amino acid oxidase, C-type lectin/lectin-like, metalloproteinase, serine proteinase, ohanin, and nucleotidase. PLA(2)s and 3FTxs are predominant, representing 48 and 38% of the venom proteins, respectively. Within 3FTxs, several isoforms of short-chain α-neurotoxins as well as muscarinic-like toxins and proteins with similarity to long-chain κ-2 bungarotoxin were identified. PLA(2)s are also highly diverse, and a toxicity screening showed that they mainly exert myotoxicity, although some are lethal and may contribute to the known presynaptic neurotoxicity of this venom. An antivenomic characterization of a therapeutic monospecific M. nigrocinctus equine antivenom revealed differences in immunorecognition of venom proteins that correlate with their molecular mass, with the weakest recognition observed toward 3FTxs.
authors.affiliation: Instituto Clodomiro Picado, Facultad de Microbiología, Escuela de Medicina, Universidad de Costa Rica, San José, Costa Rica.
authors.forename: Julián
authors.initials: J
authors.lastname: Fernández
authors.forename: Alberto
authors.initials: A
authors.lastname: Alape-Girón
authors.forename: Yamileth
authors.initials: Y
authors.lastname: Angulo
authors.forename: Libia
authors.initials: L
authors.lastname: Sanz
authors.forename: José María
authors.initials: JM
authors.lastname: Gutiérrez
authors.forename: Juan J
authors.initials: JJ
authors.lastname: Calvete
authors.forename: Bruno
authors.initials: B
authors.lastname: Lomonte
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000997:Antivenins / Q000032:analysis*; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D004546:Elapid Venoms / Q000032:analysis* / Q000235:genetics / Q000633:toxicity; D017815:Elapidae; D045726:Metalloproteases / Q000737:chemistry; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000187:drug effects / Q000473:pathology; D009498:Neurotoxins / Q000032:analysis / Q000235:genetics; D010741:Phospholipases A / Q000737:chemistry; D020033:Protein Isoforms / Q000032:analysis / Q000235:genetics; D020543:Proteome / Q000032:analysis; D040901:Proteomics / Q000379:methods; D053719:Tandem Mass Spectrometry / Q000379:methods
chemical_list: D000997:Antivenins; D004546:Elapid Venoms; D009498:Neurotoxins; D020033:Protein Isoforms; D020543:Proteome; D010741:Phospholipases A; D045726:Metalloproteases