Cloning of a synthetic chimeric gene containing recombinant Mycoplasma hyopneumoniae antigens for expression in Pichia pastoris

Background Mycoplasma hyopneumoniae is the primary etiologic agent of Swine Enzootic Pneumonia (EP), one of the most common respiratory disease that affects swine worldwide, causing considerable economic losses. Vaccination constitute one of the main practices to control EP. The production of recombinant experimental vaccines against EP has been considered an important approach towards the development of an improved vaccine [1]. This study aimed to clone a synthetic gene composed by the fusion of M. hyopneumoniae antigens R1 (P97), P42 and NrdF to Escherichia coli fragment B of the heat labile enterotoxin (LTB) into the vectors pPICZB (intracellular expression) and pPICZaB (secreted expression), in order to produce this chimeric recombinant protein in Pichia pastoris and to test it as a vaccine candidate. The M. hyopneumoniae antigens were selected due to their capacity to confer partial protection in pigs when evaluated individually [2-4]. These antigens were associated to LTB, a potent mucosal and parenteral adjuvant.