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The accumulation of hazardous waste during manufacturing of complex pharmaceuticals is a serious environmental concern. Typically, it takes several synthetic steps and requires flammable, organic solvents to produce structurally complex compounds. Starting from renewable lignocellulose (woodchips), researchers from the University of Groningen and the Helmholtz Institute for Pharmaceutical Research Saarland (HIPS) have devised a surprisingly simple catalytical method for this purpose that only requires two or three steps and generates water as the only waste. The scientists reported their process in the journal ACS Central Science.

Mammalian cells have highly specialized defence programs to protect themselves from invading pathogens. To do this, the cells change the expression of their genes; previously inactive genes are switched on or active genes are no longer expressed. Genes encode the blueprint for making proteins. If a gene is expressed, this information is first converted into RNA (ribonucleic acid) before protein production begins. However, not all RNA transcripts are templates for protein synthesis. Long non-coding RNAs (lncRNAs) have many similar properties to protein-coding messenger RNAs, but are not translated into proteins. Instead, lncRNAs interact with DNA, RNA and proteins and thereby regulate various cellular functions. Since July 2019, Dr. Mathias Munschauer's Helmholtz Young Investigator group “Long non-coding RNA and Infection Biology” at the Helmholtz Institute for RNA-based Infection Research (HIRI) investigates the function of lncRNAs in the host defence against pathogens. The HIRI is a joint institution of the Helmholtz Centre for Infection Research (HZI) in Braunschweig and the Julius Maximilian University of Würzburg (JMU). Munschauers Young Investigator group is the eighth research group at HIRI, which was founded in 2017.

A delegation of seven researchers from the leading Canadian university McGill recently spent two days at the Helmholtz Centre for Infection Research (HZI) in Braunschweig as part of a working visit. HZI and McGill University are currently establishing a cooperation from which the partners expect strong synergy effects. Especially in the field of individualized medicine, the institutions pursue common interests and want to work closely together in the future.

An influenza vaccination causes the body to form antibodies that circulate in the blood, but which are directed against constantly changing virus components. This means that the vaccine must be re-administered each year. Researchers at the Helmholtz Centre for Infection Research (HZI) in Braunschweig have now shown that the antibody-independent, cellular arm of the immune system can also provide immune protection against influenza. The researchers integrated an influenza antigen into cytomegaloviruses (CMV) and triggered a strong response from the T lymphocytes. The special thing about it: The hybrid viruses, when administered via the nose, attract T cells from the bloodstream into the mucous membranes of the respiratory tract. These immune cells are quickly activated when they come into contact with influenza viruses and then act as guards that block the virus at the most common entry point in the body. The results were published in the journal PLoS Pathogens.

The Centre for Individualised Infection Medicine (CiiM) is continuing to gain structure and establishment is progressing rapidly. Since summer 2019, this has been accompanied by the new dual leadership of CiiM directors Yang Li and Markus Cornberg.

For a long time, itaconic acid was only known as a metabolic product of fungi. Its function was unknown, but for decades it has been used industrially for polymer production. In 2013, it was surprisingly discovered as an important metabolic product in the immune system. This newly described role has sparked a search for potential clinical applications. Researchers at the Helmholtz Centre for Infection Research (HZI) and TWINCORE-Centre for Experimental and Clinical Infection Research, jointly founded by the HZI and the Hanover Medical School, have now solved the crystal structure of the itaconic acid-synthesizing enzyme cis-aconitate decarboxylase (CAD). Their findings provide the basis for an improved understanding of itaconic acid synthesis, the evolutionary origin of this important metabolic step, and the role of itaconic acid in the immune system. In particular, the researchers identified naturally occurring and possibly clinically important variations in the human CAD enzyme.