Structural studies of bacterial pore-forming protein toxins [ 2006 - 2008 ]

Also known as: Study of bacterial toxins as the basis for the design of new antibiotics

Research Grant

[Cite as]

Researchers: Prof Michael Parker (Principal investigator)

Brief description In this project the three-dimensional structures of proteins that form pores in membrane cell walls will be determined. These proteins are bacterial toxins and knowledge of their structure may prove useful in the design of new antibiotics. This project will focus on a class of toxins called the cholesterol-dependent cytolysins which are released by Gram positive bacteria such as Clostridia and Streptococcus and which cause a variety of nasty infectious diseases such as gas gangrene, pneumonia and meningitis. The three-dimensional structures will be elucidated using X-ray crystallography. Protein crystallography is the study of three-dimensional shapes of proteins at near atomic resolution. In this method proteins are made to form crystals. X-ray beams are then shone on the crystals causing the X-rays to scatter in a pattern which is characteristic of the protein's three-dimensional shape. Knowledge of the structure of proteins is necessary for the complete understanding of their biological activity and is also very useful for the rational design of new drugs that may alter their activity.

Funding Amount $AUD 509,017.61

Funding Scheme NHMRC Project Grants

Notes Standard Project Grant

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