Production of a Human Recombinant Polyclonal Fab Antivenom against Iranian Viper Echis carinatus

Archives of Razi Institute

M. M. Ranjbar¹  M. Esmaelizad²  H. Eizadi³  A. Khorasani³  S.M. Azimi³  M. H. Motedayen⁴  M. J. Rasaee⁵  G. Nikbakht Brujeni⁶  A. Zare Mirakabadi⁷ 

[1] DepartmentofVirology, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Tehran, Iran;Department of Biotechnology, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Tehran, Iran;Department of Foot and Mouth Disease, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Tehran, Iran;Department of Immunization and Plasma Production, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Karaj, Iran;Department of Medical Biotechnology, School of Medicine, Tarbiat Modares University, Tehran, Iran;Department of Microbiology and Immunology, Faculty of Veterinary Medicine, University of Tehran, Tehran, Iran;Department of Venomous Animals, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Tehran, Iran;

关键词: Echis carinatus;    Fab fragment;    Gene library;    Antivenom;    Polyclonal;   

DOI  :  10.22092/ari.2018.115499.1148

来源: DOAJ

【 摘 要 】

Venomous snakebite is a life-threatening injury in many tropical and subtropical areas including Iran. The gold standard treatment option for human envenomation is the use of antivenoms. Despite the unique effects of horse-derived antivenoms on the treatment of snakebite, they are not fully perfect and need improvements. In this study, human recombinant Fab fragment antivenom was produced in Rosetta-g bacterium using a gene library constructed in the previous study. The prepared Fab was purified in several steps, desalted, and lipopolysaccharide-depleted using ammonium sulfate solution and dialysis against phosphate buffer and Triton X-114 solution, respectively. Subsequently, the product was initially confirmed by the sodium dodecyl sulfate polyacrylamide gel electrophoresis and enzyme-linked immunosorbent assay (ELISA), respectively. Finally, the neutralization potency of the product was investigated in laboratory Syrian Mice. The obtained results showed corresponding reduced bands to Fab fragment with the molecular weight of about 28 kDa at a concentration of 3.1 mg/ml. There was a significant difference between the groups in terms of ELISA test (P

【 授权许可】

Unknown