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 Bolstering fat cells offers potential new leukemia treatment
17.10.2017 | McMaster University

nachricht Ocean atmosphere rife with microbes
17.10.2017 | King Abdullah University of Science & Technology (KAUST)

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Neutron star merger directly observed for the first time

University of Maryland researchers contribute to historic detection of gravitational waves and light created by event

On August 17, 2017, at 12:41:04 UTC, scientists made the first direct observation of a merger between two neutron stars--the dense, collapsed cores that remain...

Im Focus: Breaking: the first light from two neutron stars merging

Seven new papers describe the first-ever detection of light from a gravitational wave source. The event, caused by two neutron stars colliding and merging together, was dubbed GW170817 because it sent ripples through space-time that reached Earth on 2017 August 17. Around the world, hundreds of excited astronomers mobilized quickly and were able to observe the event using numerous telescopes, providing a wealth of new data.

Previous detections of gravitational waves have all involved the merger of two black holes, a feat that won the 2017 Nobel Prize in Physics earlier this month....

Im Focus: Smart sensors for efficient processes

Material defects in end products can quickly result in failures in many areas of industry, and have a massive impact on the safe use of their products. This is why, in the field of quality assurance, intelligent, nondestructive sensor systems play a key role. They allow testing components and parts in a rapid and cost-efficient manner without destroying the actual product or changing its surface. Experts from the Fraunhofer IZFP in Saarbrücken will be presenting two exhibits at the Blechexpo in Stuttgart from 7–10 November 2017 that allow fast, reliable, and automated characterization of materials and detection of defects (Hall 5, Booth 5306).

When quality testing uses time-consuming destructive test methods, it can result in enormous costs due to damaging or destroying the products. And given that...

Im Focus: Cold molecules on collision course

Using a new cooling technique MPQ scientists succeed at observing collisions in a dense beam of cold and slow dipolar molecules.

How do chemical reactions proceed at extremely low temperatures? The answer requires the investigation of molecular samples that are cold, dense, and slow at...

Im Focus: Shrinking the proton again!

Scientists from the Max Planck Institute of Quantum Optics, using high precision laser spectroscopy of atomic hydrogen, confirm the surprisingly small value of the proton radius determined from muonic hydrogen.

It was one of the breakthroughs of the year 2010: Laser spectroscopy of muonic hydrogen resulted in a value for the proton charge radius that was significantly...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

ASEAN Member States discuss the future role of renewable energy

17.10.2017 | Event News

World Health Summit 2017: International experts set the course for the future of Global Health

10.10.2017 | Event News

Climate Engineering Conference 2017 Opens in Berlin

10.10.2017 | Event News

 
Latest News

Ocean atmosphere rife with microbes

17.10.2017 | Life Sciences

Neutrons observe vitamin B6-dependent enzyme activity useful for drug development

17.10.2017 | Life Sciences

NASA finds newly formed tropical storm lan over open waters

17.10.2017 | Earth Sciences

VideoLinks
B2B-VideoLinks
More VideoLinks >>>