Access
To read this story in full you will need to login or make a payment (see right).
News and Views
Nature 450, 361-362 (15 November 2007) | doi:10.1038/450361a; Published online 14 November 2007
Open Innovation Challenges
-
Fast Growth of Transformed Soybean Shoots
A method for accelerating growth of soybean shoots is desired.
-
Protect Enzyme from In Planta Degradation
A proposal for stable expression of an enzyme in corn seed is desired.
- More Challenges
- Powered by:
nature jobs
Developer - Variation (Bioinformatician)
- European Bioinformatics Institute (EBI)
- Cambridge CB10 1SD United Kingdom
Biochemical Pharmacologist
- Eisai London Research Laboratories Ltd
- Hatfield, United Kingdom
Microbiology: Pathogen drop-kick
Suzanne Pfeffer1
Abstract
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.
The bacterium Legionella pneumophila is the main agent responsible for both Legionnaires' disease, which leads to pneumonia, and Pontiac fever, an illness that resembles acute influenza. This pathogen is engulfed by immune cells known as macrophages and, once inside, exploits proteins mediating intracellular trafficking to form an organelle called an L. pneumophila
- Suzanne Pfeffer is in the Department of Biochemistry, 279 Campus Drive, Room B400, Stanford University School of Medicine, Stanford, California 94305-5307, USA.
Email: pfeffer@stanford.edu
To read this story in full you will need to login or make a payment (see right).
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
Research HighlightsNature Structural & Molecular Biology News and Views (01 Nov 2007)
No exchange without receiptNature News and Views (05 May 1994)
See all 4 matches for News And ViewsRESEARCH
Legionella pneumophila proteins that regulate Rab1 membrane cyclingNature Article (15 Nov 2007)
The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factorNature Cell Biology Letter (01 Sep 2006)
See all 9 matches for Research