Science, Technology and Engineering

Foley Laboratory

Department of Biochemistry

Anthrax

As part of the CRC for Diagnostics (CDx) effort to develop novel diagnostic platforms and reagents our laboratory is involved in identifying novel high affinity reagents with selectivity against a range of commercially important target molecules. We are exploiting the diversity of random peptide and protein domain libraries to identify new diagnostic or therapeutic approaches to infectious pathogens such as Epstein Barr Virus (Jo's page), diseases such as SARS, and agents of bioterrorism such as anthrax.

Peptides and compact protein domains (CPDs) have been obtained to a range of target molecules. A comprehensive characterization of binders from the peptide and CPD libraries has revealed that these libraries consist of a large diverse pool from which binding molecules with high affinity and exquisite specificity can be selected.

Peptides that bind to anthrax toxin: The lethal component of the anthrax toxin with peptide substrate (left; from Pannifer et al., 2001, Nature). Binding of peptide T1 to lethal factor (Right, blue bars)

In collaboration with DSTO our lab has identified a small peptide with affinity for a component of the anthrax toxin. The toxin from Bacillus anthracis is a three-molecule complex that is responsible for killing of the host when infection with the bacteria occurs. Peptides that bind to anthrax toxin may have a role in preventing the lethal effects of the toxin. The potential of peptides for diagnosis of agents of bioterrorism is currently being evaluated in our lab.

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