Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

MRSA’s ‘weak point’ visualised by scientists

20.01.2009
An enzyme that lives in MRSA and helps the dangerous bacterium to grow and spread infection through the human body has been visualised for the first time, according to a study out today in Proceedings of the National Academy of Sciences (PNAS).

Now, armed with detailed information about the structure of this enzyme, researchers hope to design new drugs that will seek it out and disable it, providing a new way of combating MRSA and other bacterial infections.

The enzyme, a ‘worker-protein’ called LtaS, produces an important component of the protective outer-layer that surrounds all Staphylococcus aureus cells as well as many other bacteria that cause disease.

Staphylococcus aureus is a type of bacterium that causes a variety of infections in the human body, including skin infections and abscesses, sometimes leading to blood poisoning and life-threatening lung or brain infections. MRSA is a particular strain of Staphylococcus aureus, which has evolved to be resistant to the antibiotic methicillin and a large number of other antibiotics, and can be life threatening.

To counter this drug resistance and ensure that it is possible to treat MRSA infection in the future, new antibiotics are needed that work differently, for example by attacking parts of the pathogen that are not targeted by current drugs.

The team from Imperial College London behind today’s study, funded by the Medical Research Council, thinks that LtaS might be a good candidate target for a new antibiotic to which MRSA will not be resistant. This is because its job is to build a polymer called lipoteichoic acid (LTA), which is an important structure found on the surface of Staphylococcus aureus cells.

Although the role of the cell surface polymer LTA is not fully understood, lab tests carried out by the same researchers have shown that if the LtaS enzyme is depleted, production of LTA on the cell surface draws to a halt. As a result growth of the Staphylococcus aureus cell is blocked. So in a patient infected with MRSA, inhibiting this enzyme could clear up the infection because the bacterial cells would be unable to grow properly. Many existing antibiotics work in a similar way by inhibiting the production of other such important structures on the surface of bacterial cells.

The trick, according to one of the paper’s lead authors, Dr Angelika Grundling from Imperial College London’s Division of Investigative Science, is to now find a way of using the new knowledge to develop a drug for use in real world scenarios:

“We’re not quite sure how it works, but we know that this surface structure called LTA is involved in cell growth and cell division – we have shown that without it the cell cannot grow properly, and eventually dies. Because LtaS is the ‘machine’, which builds LTA, developing a drug that knocks out the machine will provide us with a new way to disable the growth of these cells, which would represent a novel new treatment for MRSA and other Staphylococcus aureus infections.”

Dr Grundling and her colleagues have produced a detailed image of the molecular structure of the LtaS enzyme using X-ray crystallography techniques. The image includes a map of LtaS’s active binding site: the part of the enzyme which plays a key role in building LTA. This is the very part that researchers now need to home in on with a drug, in order to prevent the LtaS enzyme from doing its job.

Professor Paul Freemont from Imperial’s Division of Molecular Biosciences, co-lead-author of the paper, explains the importance of the information they have gained about this particular part of the enzyme:

“If we’re to develop a drug which disables LtaS from doing its job, then we need to make sure the drug molecule is as perfectly matched as possible to the enzyme’s binding site, so it can trick the enzyme into taking it up. Once the drug is bound to the enzyme it will be able start its job of sabotage.

“So the more detailed information about the binding site we have, the better we’ll be able to develop an effective drug to match it,” he said.

The two Imperial teams led by Professor Freemont and Dr Grundling now hope to work with the College’s Drug Discovery Centre to search for a biological agent that interacts with the LtaS binding site, as the basis for a new antibiotic drug.

They hope that in the future such a drug could be used to treat not just MRSA, but a whole host of infections caused by bacterial pathogens.

Additional funding for the research was obtained through the US National Institute of Health.

Danielle Reeves | alfa
Further information:
http://www.imperial.ac.uk

More articles from Life Sciences:

nachricht Designer cells: artificial enzyme can activate a gene switch
22.05.2018 | Universität Basel

nachricht Flow of cerebrospinal fluid regulates neural stem cell division
22.05.2018 | Helmholtz Zentrum München - Deutsches Forschungszentrum für Gesundheit und Umwelt

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: LZH showcases laser material processing of tomorrow at the LASYS 2018

At the LASYS 2018, from June 5th to 7th, the Laser Zentrum Hannover e.V. (LZH) will be showcasing processes for the laser material processing of tomorrow in hall 4 at stand 4E75. With blown bomb shells the LZH will present first results of a research project on civil security.

At this year's LASYS, the LZH will exhibit light-based processes such as cutting, welding, ablation and structuring as well as additive manufacturing for...

Im Focus: Self-illuminating pixels for a new display generation

There are videos on the internet that can make one marvel at technology. For example, a smartphone is casually bent around the arm or a thin-film display is rolled in all directions and with almost every diameter. From the user's point of view, this looks fantastic. From a professional point of view, however, the question arises: Is that already possible?

At Display Week 2018, scientists from the Fraunhofer Institute for Applied Polymer Research IAP will be demonstrating today’s technological possibilities and...

Im Focus: Explanation for puzzling quantum oscillations has been found

So-called quantum many-body scars allow quantum systems to stay out of equilibrium much longer, explaining experiment | Study published in Nature Physics

Recently, researchers from Harvard and MIT succeeded in trapping a record 53 atoms and individually controlling their quantum state, realizing what is called a...

Im Focus: Dozens of binaries from Milky Way's globular clusters could be detectable by LISA

Next-generation gravitational wave detector in space will complement LIGO on Earth

The historic first detection of gravitational waves from colliding black holes far outside our galaxy opened a new window to understanding the universe. A...

Im Focus: Entangled atoms shine in unison

A team led by Austrian experimental physicist Rainer Blatt has succeeded in characterizing the quantum entanglement of two spatially separated atoms by observing their light emission. This fundamental demonstration could lead to the development of highly sensitive optical gradiometers for the precise measurement of the gravitational field or the earth's magnetic field.

The age of quantum technology has long been heralded. Decades of research into the quantum world have led to the development of methods that make it possible...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

VideoLinks
Industry & Economy
Event News

Save the date: Forum European Neuroscience – 07-11 July 2018 in Berlin, Germany

02.05.2018 | Event News

Invitation to the upcoming "Current Topics in Bioinformatics: Big Data in Genomics and Medicine"

13.04.2018 | Event News

Unique scope of UV LED technologies and applications presented in Berlin: ICULTA-2018

12.04.2018 | Event News

 
Latest News

Achema 2018: New camera system monitors distillation and helps save energy

22.05.2018 | Trade Fair News

LZH showcases laser material processing of tomorrow at the LASYS 2018

22.05.2018 | Trade Fair News

Matabele ants: Travelling faster with detours

22.05.2018 | Life Sciences

VideoLinks
Science & Research
Overview of more VideoLinks >>>