FEBS Letters · 1999 · 58 citations · 31 references
PharmacyBiotechnologyMolecular BiologyAntibody EngineeringMonoclonal AntibodiesProtein EngineeringAntibody CharacterizationAntibody Specificity EngineeringRecombinant AntibodiesRecombinant Antibody ExpressionRecombinant Antibody ProductionVenom BiologyAntibody-mediated Toxin NeutralizationCloningEscherichia ColiReptile Venom BiologyScorpion EnvenomationSnake Venom ToxicologyToxin CharacterizationVenom Pharmacology
Monoclonal antibody 4C1 specifically binds to and neutralizes the most potent neurotoxin (AahII) of the scorpion Androctonus australis. The cDNAs encoding the variable regions of this antibody were isolated by PCR-mediated cloning. A single-chain Fv gene was engineered and expressed in Escherichia coli. The recombinant protein had neutralizing activity similar to that of the intact antibody in vitro and in vivo. We have thus neutralized the pharmacological and biological properties of a scorpion neurotoxin with a single-chain Fv, which opens new perspectives for the treatment of envenomizations.
31
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms.
Takashi Yokota, Diane E. Milenic, Marc Whitlow et al. · PubMed · 1992 · 826 citations
Pharmacy, Oncology, Pharmacokinetics +17