Commercial monovalent antivenoms in Australia are polyvalent.
Monovalent antivenoms have a lower volume of specific antibodies that may reduce reactions but require accurate snake identification to be used. Polyvalent antivenoms are larger volume and may have a higher reaction rate. However, they avoid the problem of snake identification and may be more cost-effective to manufacture. We have previously shown cross-neutralisation of two Australian elapid venoms, tiger snake (Notechis scutatus) and brown snake (Pseudonaja textilis) venoms, by their respective monovalent antivenoms. In this study enzyme immunoassays were used to quantify the amount of monovalent antivenom (quantity of monovalent antibodies to a specific snake venom) in vials of commercially produced antivenom in Australia. All antivenoms tested appeared to be polyvalent and contain varying amounts of all five terrestrial snake monovalent antibodies based on their binding to the five representative venoms. Redback spider antivenom did not have any measurable binding affinity for any of the five snake venoms, showing that the observed binding is not due to non-specific interactions with equine protein. The antivenoms had expire dates over a 15 year period, suggesting that the antivenoms have been mixtures for at least this time. This study cannot be used to rationalise hospital stocks of antivenom in Australia because there is no guarantee that the antivenoms will remain as mixtures. However, it would be possible for the manufacturer to reduce the number of types of snake antivenoms available in Australia to two polyvalent antivenoms which would simplify treatment of snakebite.
Department of Clinical Toxicology and Pharmacology, Calvary Mater Newcastle Hospital, Newcastle, NSW, Australia.
Margaret A
MA
O'Leary
Geoffrey K
GK
Isbister
D000818:Animals; D017837:Bothrops / Q000502:physiology*; D006801:Humans; D007249:Inflammation / Q000139:chemically induced* / Q000473:pathology; D045726:Metalloproteases / Q000737:chemistry / Q000633:toxicity; D010146:Pain / Q000139:chemically induced / Q000473:pathology; D054467:Phospholipases A2 / Q000737:chemistry / Q000633:toxicity; D012697:Serine Endopeptidases / Q000737:chemistry / Q000633:toxicity; D014757:Viper Venoms / Q000737:chemistry / Q000201:enzymology / Q000633:toxicity*
D014757:Viper Venoms; D054467:Phospholipases A2; D045726:Metalloproteases; D012697:Serine Endopeptidases