Anaplasma OmpA
Escherichia Coli.
Sterile Filtered clear solution.
Greater than 95.0% as determined by SDS-PAGE.
Description
Anaplasma OmpA produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 24kDa. Anaplasma OmpA is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.
Product Specs
Escherichia Coli.
Product Science Overview
One of the critical components of Anaplasma phagocytophilum is its Outer Membrane Protein A (OmpA). OmpA is a peptidoglycan-associated lipoprotein that plays a significant role in the pathogenesis of the disease . It belongs to the porin superfamily, characterized by a beta-barrel structure . This protein is essential for the bacterium’s ability to adhere to and invade host cells.
Recombinant OmpA refers to the artificially produced version of the OmpA protein. This recombinant protein is used in research to study the interactions between the bacterium and host cells, as well as to develop potential vaccines and therapeutic interventions. The recombinant OmpA has been shown to bind to host cells and inhibit the infection process, making it a promising candidate for vaccine development .
Research has identified specific domains within the OmpA protein that are crucial for its binding to host cells. For instance, residues 59 to 74 of OmpA have been found to be essential for its interaction with the host cell receptor, sialyl Lewis x (sLe x)-capped P-selectin glycoprotein ligand 1 . Polyclonal antibodies generated against this peptide have been shown to inhibit A. phagocytophilum infection of host cells .
Additionally, studies have demonstrated that amino acid substitutions at specific positions within the OmpA protein can significantly impact its binding capacity. For example, the substitution of lysine at position 64 (K64) was found to be necessary for the recombinant OmpA to bind to host cells and competitively inhibit the infection .
The conservation of the OmpA protein across different strains of Anaplasma phagocytophilum makes it a valuable target for vaccine development. Research has shown that antibodies directed against the recombinant OmpA can neutralize the bacterium’s ability to bind and infect host cells . This highlights the potential of OmpA as a highly conserved vaccine candidate that could provide cross-protection against multiple strains of the bacterium .
In conclusion, the study of Anaplasma phagocytophilum OmpA recombinant protein is crucial for understanding the pathogenesis of human granulocytic anaplasmosis and developing effective vaccines and therapeutic interventions. The recombinant OmpA protein’s ability to inhibit infection and its conservation across different strains make it a promising candidate for future research and vaccine development.
