Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Legionnaire's bacterial proteins work together to survive

25.10.2007
Proteins within the bacteria that cause Legionnaire’s disease can kidnap their own molecular “coffin” and carry it to a safe place within the cell, ensuring their survival, Yale School of Medicine researchers report in Nature Wednesday.

“This supposedly simple organism continues to fascinate us with new tricks that enable it to manipulate cells in our body that normally protect us against bacterial infections,” said the lead author, Craig Roy, associate professor of microbial pathogenesis at Yale.

Legionnaire’s disease acquired its name in 1976 when an outbreak of pneumonia occurred among people attending a convention of the American Legion in Philadelphia. The bacteria that causes it—Legionella pneumophila—replicates inside macrophage, which are cells that are part of the immune system and “eat” cellular debris and toxins. Macrophages kill bacteria by transporting them in storage bubbles known as vacuoles to organelles that have enzymes to then break down the intruders.

“What makes this pathogen special is that it can control transport of the vacuole formed after macrophages ingest the bacterium,” Roy said. “It hijacks the vacuole and directs it to be transported to a nutrient-rich organelle called the endoplasmic reticulum, where the bacteria replicate in high numbers.”

Roy and his colleagues identified the Legionella proteins that are involved in the hijacking. They found that one protein, DrrA, that turns on a molecular switch, Rab1, and subverts its function. This allows the Legionella to fuse the endoplasmic reticulum and the vacuole, creating a compartment that ensures bacterial survival. They also found a second bacterial protein, LepB, that turns off the Rab1 switch once the bacteria have successfully entered the endoplasmic reticulum.

“In other words,” Roy said, “you can think of Legionella as being a crafty burglar that enters a cell and uses the protein DrrA to turn on a light, Rab1, that will illuminate the location of the safe, the endoplasmic reticulum. Once Legionella has cracked the safe, LepB, turns off the light to avoid detection.”

Jacqueline Weaver | EurekAlert!
Further information:
http://www.yale.edu

Further reports about: Legionella bacterial endoplasmic endoplasmic reticulum vacuole

More articles from Life Sciences:

nachricht 127 at one blow...
18.01.2017 | Stiftung Zoologisches Forschungsmuseum Alexander Koenig, Leibniz-Institut für Biodiversität der Tiere

nachricht How gut bacteria can make us ill
18.01.2017 | Helmholtz-Zentrum für Infektionsforschung

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: How gut bacteria can make us ill

HZI researchers decipher infection mechanisms of Yersinia and immune responses of the host

Yersiniae cause severe intestinal infections. Studies using Yersinia pseudotuberculosis as a model organism aim to elucidate the infection mechanisms of these...

Im Focus: Interfacial Superconductivity: Magnetic and superconducting order revealed simultaneously

Researchers from the University of Hamburg in Germany, in collaboration with colleagues from the University of Aarhus in Denmark, have synthesized a new superconducting material by growing a few layers of an antiferromagnetic transition-metal chalcogenide on a bismuth-based topological insulator, both being non-superconducting materials.

While superconductivity and magnetism are generally believed to be mutually exclusive, surprisingly, in this new material, superconducting correlations...

Im Focus: Studying fundamental particles in materials

Laser-driving of semimetals allows creating novel quasiparticle states within condensed matter systems and switching between different states on ultrafast time scales

Studying properties of fundamental particles in condensed matter systems is a promising approach to quantum field theory. Quasiparticles offer the opportunity...

Im Focus: Designing Architecture with Solar Building Envelopes

Among the general public, solar thermal energy is currently associated with dark blue, rectangular collectors on building roofs. Technologies are needed for aesthetically high quality architecture which offer the architect more room for manoeuvre when it comes to low- and plus-energy buildings. With the “ArKol” project, researchers at Fraunhofer ISE together with partners are currently developing two façade collectors for solar thermal energy generation, which permit a high degree of design flexibility: a strip collector for opaque façade sections and a solar thermal blind for transparent sections. The current state of the two developments will be presented at the BAU 2017 trade fair.

As part of the “ArKol – development of architecturally highly integrated façade collectors with heat pipes” project, Fraunhofer ISE together with its partners...

Im Focus: How to inflate a hardened concrete shell with a weight of 80 t

At TU Wien, an alternative for resource intensive formwork for the construction of concrete domes was developed. It is now used in a test dome for the Austrian Federal Railways Infrastructure (ÖBB Infrastruktur).

Concrete shells are efficient structures, but not very resource efficient. The formwork for the construction of concrete domes alone requires a high amount of...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

12V, 48V, high-voltage – trends in E/E automotive architecture

10.01.2017 | Event News

2nd Conference on Non-Textual Information on 10 and 11 May 2017 in Hannover

09.01.2017 | Event News

Nothing will happen without batteries making it happen!

05.01.2017 | Event News

 
Latest News

Explaining how 2-D materials break at the atomic level

18.01.2017 | Materials Sciences

Data analysis optimizes cyber-physical systems in telecommunications and building automation

18.01.2017 | Information Technology

Reducing household waste with less energy

18.01.2017 | Ecology, The Environment and Conservation

VideoLinks
B2B-VideoLinks
More VideoLinks >>>