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Purification of a mouse monoclonal antibody against Erns protein from classical swine fever virus

Journal of Bacteriology & Mycology: Open Access
Jose Miguel Fernandez Torres,1 Alianny Lazara Rojo Sanchez,2 Onel Valdivia Perez,1 Reinaldo Blanco Aguila,1 Dayamí Dorta Hernandez,1 Carlos Hernandez,1 Yeosvany Cabrera Artiles,1 Dalia Borges Pérez,1 Daymí Abreu Remedio1

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With the aim to follow large scale production of recombinant Erns from Classical Swine Fever Virus, a monoclonal specific antibody was obtained and optimized it downstream lab scale purification. The anti-Erns gamma globulins were purified through Protein A and Protein G affinity chromatography from ascites fluid. Three binding factors were assessed (pH, flow rate and buffer) to define dynamic binding capacity. The best binding condition to Protein a (6.6 mg/mL of matrix) was in phosphate buffer, pH 8.0 and linear flow rate of 78cm/h with a purity of 90 %. For Protein G, the best arrangement of factors was phosphate buffer, pH 7.0 and linear flow 178cm/h with 6.45mg/mL of adsorbed antibody with a purity of 95 %. The nProtein-A Sepharose matrix allowed 1.21 times more recovery than the nProtein-G Sepharose matrix. However, the elutions obtained with the G-protein were more pure.


swine fever virus, monoclonal antibody, Erns, glycoprotein, biological marker, hybridoma