Production of Monoclonal Antibodies to Flagella Core Protein of Vibrio parahaemolyticus

Abstract

Polar flagellar core protein was purified from Vibrio parahaemolyticus by differential centrifugation and cesium chloride isopycnic centrifugation. Twelve hybridomas secreting monoclonal antibodies against flagellar core protein ( MAb-flc ) were obtained from fusions. By chance, one purified flagella core preparation retained flagellar sheath and as a consequence, two hybridomas were detected which secreted anti-sheath antibodies ( MAb-fls ). MAb-flc and MAb-fls reacted specifically with their corresponding antigens as demonstrated by immunogold labeling. Coagglutination reagents prepared with MAb-flc and MAb-fls were tested against 35 strains of V. parahaemolyticus and 34 heterologous Vibrio species. The coagglutination results revealed that the flagellar core was species-specific while the flagellar sheath was not.