Editor's Summary
15 November 2007
Living in a vacuole
One of the properties that makes the most common Legionnaires' disease pathogen so virulent is its ability to exploit the vacuole formed inside host macrophages when they ingest the bacterium. The vacuole is meant to be as far as the pathogen gets, the site where host enzymes destroy it. But Legionella pneumophila hijacks the vacuole and directs it to be transported to the endoplasmic reticulum, where the bacteria multiply. Two bacterial proteins involved in this process have now been identified. DrrA protein turns on a molecular switch, Rab1, and subverts its function to allow the endoplasmic reticulum and the vacuole to fuse. LepB then turns off the Rab1 switch once the bacteria are in the endoplasmic reticulum.
News and Views: Microbiology: Pathogen drop-kick
To set the scene for its replication, the bacterium Legionella pneumophila exploits its host cells' Rab1 protein. This pathogen seems to use minimal resources to mimic the normal cycle of Rab1 activity.
Suzanne Pfeffer
doi:10.1038/450361a
Article: Legionella pneumophila proteins that regulate Rab1 membrane cycling
Alyssa Ingmundson, Anna Delprato, David G. Lambright & Craig R. Roy
doi:10.1038/nature06336
Abstract | Full Text | PDF (477K) | Supplementary information