Abstract

The formula for preparation of the polyvalent antivenom used in treatment of poisonous snakebite in the United States has not been changed in over 30 years, yet our knowledge of venom composition has changed drastically in this period of time. Use of this antivenom is the only consistent therapy for poisonous snakebite. There are two main problems with the polyvalent antivenom. It is not very effective in preventing local tissue damage induced by snake venom poisoning, and its administration frequently results in allergic reactions.
A specific aim of this research is to characterize venoms from U.S. poisonous snakes by high resolution liquid chromatography and electrophoresis, to determine the biological activities of their major components and to select the best venoms to use as immunogens to prepare a polyvalent antivenom for use in the United States to neutralize all of the biological activities of a wide range of venoms. To address the problem of allergic reactions, the antivenom will be purified by affinity chromatography to yield an antivenom which contains only antibodies to biologically important venom components. The long-term objective is to develop an improved antivenom for the treatment of poisonous snakebite in the United States which prevents systemic and local effects of a wide variety of venoms and does not induce allergic reactions.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI026923-07
Application #
2063634
Study Section
Pathology B Study Section (PTHB)
Project Start
1988-03-01
Project End
1995-02-28
Budget Start
1994-03-01
Budget End
1995-02-28
Support Year
7
Fiscal Year
1994
Total Cost
Indirect Cost

  Institution

Name
Oklahoma State University Stillwater
Department
Physiology
Type
Schools of Veterinary Medicine
DUNS #
City
Stillwater
State
OK
Country
United States
Zip Code
74078

  Publications

Crosbie, Rachelle H; Dovico, Sherri A; Flanagan, Jason D et al. (2002) Characterization of aquaporin-4 in muscle and muscular dystrophy. FASEB J 16:943-9
Ownby, C L; Powell, J R; Jiang, M S et al. (1997) Melittin and phospholipase A2 from bee (Apis mellifera) venom cause necrosis of murine skeletal muscle in vivo. Toxicon 35:67-80
Ownby, C L; Colberg, T R; White, S P (1997) Isolation, characterization and crystallization of a phospholipase A2 myotoxin from the venom of the prairie rattlesnake (Crotalus viridis viridis). Toxicon 35:111-24
Anderson, S G; Ownby, C L (1997) Systemic hemorrhage induced by proteinase H from Crotalus adamanteus (eastern diamondback rattlesnake) venom. Toxicon 35:1301-13
Anderson, S G; Ownby, C L (1997) Pathogenesis of hemorrhage induced by proteinase H from eastern diamondback rattlesnake (Crotalus adamanteus) venom. Toxicon 35:1291-300
Li, Q; Ownby, C L (1996) Immunological studies of rabbit antibodies against hemorrhagic fractions of Crotalus viridis viridis venom: role of crossreacting antibodies in neutralization. Comp Biochem Physiol A Physiol 114:167-73
Ownby, C L; Colberg, T R; Li, Q (1994) Presence of heat-stable hemorrhagic toxins in snake venoms. Toxicon 32:945-54
Li, Q; Ownby, C L (1994) Development of an enzyme-linked immunosorbent assay (ELISA) for identification of venoms from snakes in the Agkistrodon genus. Toxicon 32:1315-25
Johnson, E K; Ownby, C L (1994) The role of extracellular ions in the pathogenesis of myonecrosis induced by a myotoxin isolated from Broad-Banded copperhead (Agkistrodon contortrix laticinctus) venom. Comp Biochem Physiol Pharmacol Toxicol Endocrinol 107:359-66
Ownby, C L; Fletcher, J E; Colberg, T R (1993) Cardiotoxin 1 from cobra (Naja naja atra) venom causes necrosis of skeletal muscle in vivo. Toxicon 31:697-709

Showing the most recent 10 out of 19 publications