Scientists made a leap forward in the decoding of multi-resistant pathogens

23 November 2018

GMP News

Researchers at the University of Tübingen and the German Center for Infection Research (DZIF) have achieved a breakthrough in the decoding of multi-resistant pathogens.

According to a study published at the beginning of November, there were around 670,000 diseases caused by multi-resistant pathogens in the EU alone in 2015 and 33,000 patients died.

The team led by Professor Andreas Peschel and Professor Thilo Stehle was able to decode the structure and function of a previously unknown protein used by dreaded pathogens such as Staphylococcus aureus like a magic cloak to protect themselves against the human immune system. The study was published in Nature, an international journal dedicated to the latest advancement of natural sciences.

Most antibiotics are meanwhile ineffective against resistant pathogens. Effective replacement antibiotics and a protective vaccine against Methicillin-resistant Staphylococcus aureus (MRSA) are not yet in sight. A precise understanding of the defense mechanisms could therefore lead to new therapies against the bacteria.

Researchers at the University of Tübingen have now described how MRSA bacteria become invisible to the immune system. They were able to show that many of the particularly frequent MRSA bacteria have acquired a previously unknown protein that prevents the pathogens from being detected by antibodies. The Tübingen scientists gave the protein the name TarP (short for teichoic acid ribitol P).

The scientists assume that the bacterial camouflage is the result of an exchange between the pathogens and their natural enemies, known as bacteriophages. Phages are a class of viruses that attack bacteria, use them as host cells and feed on them. In this case, phages seem to have reprogrammed their host using the TarP protein and thus altered the surface of the bacterium. The first authors of the study, David Gerlach and Yinglan Guo, succeeded in clarifying the mechanism and structure of TarP. The structure-function analysis of TarP forms an excellent basis for the development of new drugs that block TarP allowing the immune system to detect the pathogens.

An interdisciplinary approach, involving scientists from Denmark, Germany, Great Britain, Italy, the Netherlands and South Korea, was particularly important for the success of this work.

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