Cloning, expression, purification and expression condition optimization of alpha-enolase from Staphylococcus aureus in Escherichia coli

摘要

BACKGROUND: The multifunctional enzyme a-enolase belongs to a family of cytoplasmic and glycolytic enzymes, which is localized in the cytoplasm and at the surface of many eukaryotic and prokaryotic cells. alpha-enolase on the surface of Staphylococcus aureus (S. aureus) is a receptor with high affinity for laminin, the most abundant extracellular matrix component. Laminin-binding ability plays a considerable role in the pathogenesis of this microorganism. S. aureus is an opportunistic pathogen that causes major nosocomial infections and variety of diseases in human beings. This organism has a strong tendency to develop antibiotic resistance. Its property to spread of antibiotic resistance has intensified the need of novel antistaphylococcal techniques. a-enolase, as an important surface antigen, is a potential vaccine or immunotherapeutic candidate.