Haris Atmoko

• BSc (Hons) Biochemistry
• Mutation of potential binding sites for lipopolysaccharide on OmpF and how they affect colicin N toxicity.

Colicin N is a toxin to certain E. coli that is produced by specific strains of E. coli. It is believed that colicin N interacts with the surface protein OmpF to enter and lyse cells. Moreover, lipopolysaccharide is known to bind to OmpF, but it is not known exactly how the three interact. The focus of our project was whether the binding of lipopolysaccharide to OmpF is required for colicin N to interact with OmpF and kill cells. To do this we attempted to mutate certain residues of OmpF that we believed were possible LPS binding sites.

Funding source: Newcastle University