Molecular Cloning and Expression of Anaplasma marginale Major Surface Protein 5

Anaplasma marginale major surface protein 5 gene was amplified by polymerase chain reaction, cloned and expressed in Escherichia coli using a prokaryotic expression vector. The recombinant protein was purified under denaturing conditions by Ni-NTA affinity purification and suboptimal level of the expressed recombinant protein was achieved. Major surface protein 5 is a transmembrane protein with N-terminal transmembrane domain causing the expressed protein to form insoluble aggregates. The recombinant protein expressed in this study will be evaluated for its potential in the serodiagnosis of A. marginale infection in bovines.