Glu-C plays a significant role in the pathogenicity of Staphylococcus aureus. It aids in the adherence and colonization of host cells, which is crucial for the bacteria’s ability to infect and cause disease . Additionally, Glu-C helps the bacteria evade the host’s immune system by fragmenting human immunoglobulins IgG, IgM, and IgA . This fragmentation weakens the host’s immune response, allowing the bacteria to persist and proliferate.
Recombinant Glutamyl Endopeptidase from Staphylococcus aureus is produced using Escherichia coli as the expression system . The recombinant form is a non-glycosylated protein monomer, consisting of 267 amino acids and having a molecular mass of approximately 28.9 kDa . The production process involves the expression of the enzyme in E. coli, followed by purification to achieve high purity levels suitable for research applications .
The recombinant Glu-C is typically provided as a sterile filtered, white lyophilized (freeze-dried) powder . It is formulated in a 10 mM sodium phosphate buffer at pH 7.5 . The lyophilized product is stable at -20°C, and once reconstituted, it should be aliquoted and stored at -20°C with a carrier protein (such as 0.1% HSA or BSA) to ensure long-term stability .
Recombinant Glutamyl Endopeptidase is primarily used in research settings. It is valuable for studying protein structure and function, as well as for various biochemical assays . The enzyme’s ability to specifically cleave at glutamate and aspartate residues makes it a useful tool for protein sequencing and analysis .