Mechanism of antibodies purification by protein A

Protein A, a major cell wall component of Staphylococcus aureus, is one of the first immunoglobulin-binding proteins that is discovered about 80 years ago. However, a great deal of development in both purification methods and application of antibodies in treatment have been done. There are many publications based on the untargeted (size exclusion, ion exchange and hydrophobic interactions) and targeted (affinity) methods by scientists in academic/industry groups. In this review, we have focused on the study of both native and engineered Protein A to understand its mechanism in the purification of antibodies. What domain of Protein A dose interact with antibody? Where are contact regions? What is the non-covalent interaction mechanism of Protein A and antibody? Does alkaline condition, in the washing step, influence on antibody structure and activity? On the other hand, the immobilization of Protein A on various sorbents such as agarose, silica, polysaccharide, polymers, and magnetic nanoparticles have investigated. Also, the application of Protein A as biosensor for detection of the antibody is discussed. We have tried to find interesting and stimulating answers to all these questions. [Display omitted] •Voluminous overview on Protein A affinity sorbents and immobilization methods.•Introducing the different beds, linkers and protein A prepared for IgG purification.•Comparative study the structure of different types of modified Protein A and evaluation their affinity to antibody.•Highlighting the outstanding developments in Protein A affinity sorbents.•Description of significant applications of Protein A in the purification of IgG.