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Many disease-causing bacteria use the same system to deliver damaging chemicals, called 'virulence effector proteins', into host cells. This 'type III protein-secretion system' involves customized chaperone molecules, which bind to virulence effectors and ensure their effective movement.
This week in Nature (Vol. 414, No. 6859, pp. 77-81, 01 Nov 2001), C. Erec Stebbins and Jorge Galán of Yale School of Medicine, New Haven, Connecticut, describe one such interaction. They have elucidated the crystal structure of the binding domain of a Salmonella virulence protein, and its chaperone. Structural information like this could help in drug design, as type III protein-secretion mechanisms may represent a target for many diseases. Craig L. Smith and Scott J. Hultgren discuss the ramifications of this work in an accompanying News and Views article. CONTACT: Jorge Galán
tel +1 203 737 2404
e-mail jorge.galan@yale.edu Scott J. Hultgren
tel +1 314 362 6772
e-mail hultgren@borcim.wustl.edu
(C) Nature press release.
Message posted by: Trevor M. D'Souza
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