Structure-function study and engineering of eubacterial flagellin

In the past few decades biology has been revolutionized by the advances in molecular biology and genetic engineering. Bacterial systems have been in the forefront of this revolution and our understanding of life has been extended by their genetic manipulation. This work explores the feasibility of engineering the flagellin protein of Salmonella typhimurium to display proteins/peptides and create bio-nanotubes. Flagellin protein that forms the fiber is the major component of bacterial flagellar system. Due to its abundance and export to the cell surface it forms an ideal platform for displaying desired proteins/ peptides. The central domain of the protein that is exposed to the periphery of the fiber is highly variable and can be deleted to a large extent. This makes it possible to insert different proteins and peptides in the middle domain and display them on surface of the fiber. Such system can have important applications in the display of commercially important proteins/peptides, antibody epitopes and bio-degrading enzymes. The current work also explores the protein structure of hyperthermostable flagellin that can serve as a thermostable display system.

Autorentext

Dr. Malapaka was born in India and completed his graduate studies in the United States at Western Michigan University. His graduate research was focused on engineering of the flagellin protein of Salmonella typhimurium. Currently he is pursuing post-doctoral fellowship at Van Andel Research Institute, MI, USA.