Press releases

Using bacteria of the Bartonella henselae species, researchers from Goethe University, Frankfurt University Hospital, the Paul Ehrlich Federal Institute for Vaccines and Biomedicines in Langen, and the University of Oslo demonstrated for the first time that antibodies can prevent certain surface proteins of bacterial pathogens from entering host cells. The findings are important for the development of new drugs against highly resistant infectious agents.

FRANKFURT. Infections, especially those with highly resistant pathogens, pose a significant threat to human health. It is dangerous when pathogens manage to colonize the organism and subsequently cause severe infections. The first step in such an infection always consists of the pathogens attaching themselves to the host cells' surface. From here, the infections spread, resulting, for example, in infections of deeper tissue layers and organs.

A group of scientists surrounding Prof. Volkhard Kempf from Frankfurt University Hospital's Institute of Microbiology and Hospital Hygiene has now succeeded in blocking this adhesion mechanism in a bacterium, thereby preventing the infection of host cells. For this purpose, the researchers examined the pathogen Bartonella henselae, usually causing cat scratch disease. Transmitted by cats, the disease mainly affects young children, whose symptoms include swollen and hardened lymph nodes around the site of infection – usually following a scratch or bite injury caused by infected cats.

Bartonella bacteria infect so-called endothelial cells, which line the blood vessels. Via their surface protein Bartonella adhesin A (BadA), they attach themselves to a protein (fibronectin) of the so-called "extracellular matrix", a network of protein fibers that lie on top of the endothelial cells.

To determine which parts of the BadA protein are important in the bacterial adhesion process, the researchers equipped Bartonella bacteria with various genetically modified BadA variants, among others, and then analyzed the extent to which these variants were still able to bind fibronectin. Once it was clear which BadA segments were responsible for the binding, the team produced antibodies against them, using cell culture experiments to show for the first time that such antibodies can prevent infection by such bacteria.

Prof. Volkhard Kempf explains: "Bartonella henselae is not a very dangerous pathogen, and in most cases, cat scratch disease does not require any specific medical treatment. However, for us Bartonella henselae is a very important model organism for far more dangerous pathogens such as Acinetobacter baumannii, a serious pathogen that usually causes wound infection or pneumonia and often shows resistance to several last-choice antibiotics. The BadA protein of Bartonella henselae belongs to the so-called 'trimeric autotransporter adhesins', which are also responsible for adhesion to human cells in Acinetobacter and a number of other pathogens. A drug-induced blocking of these adhesins is therefore a promising novel and future approach to combat dangerous bacterial infections."

The research was supported by the Viral and Bacterial Adhesin Network Training (ViBrANT) program; a HORIZON 2020 research and innovation program of the European Union under the Marie Skłodowska-Curie grant agreement; the Robert Koch Institute, Berlin, Germany; the “PROXYDRUGS" project of the Federal Ministry of Education and Research; as well as the German Research Foundation DFG.

Publication: Arno Thibau, Diana J. Vaca, Marlene Bagowski, Katharina Hipp, Daniela Bender, Wibke Ballhorn, Dirk Linke, Volkhard A. J. Kempf: Adhesion of Bartonella henselae to Fibronectin Is Mediated via Repetitive Motifs Present in the Stalk of Bartonella Adhesin A. https://journals.asm.org/doi/10.1128/spectrum.02117-22

Background: How bacteria adhere to cells: Basis for the development of a new class of antibiotics (22 June 2022) https://www.goethe-university-frankfurt.de/74958144?search=kempf

Picture download:
https://www.kgu.de/fileadmin/redakteure/Presse/Bilder_Pressmitteilungen/2022/Bartonella_henselae.jpg

Caption: Adhesion of Bartonella henselae (blue) to human blood vessel cells (red). The bacterium's adhesion to the host cells could be blocked with the help of so-called “anti-ligands". Credit: https://www.mdpi.com/2075-4418/11/7/1259

Further information:
Professor Volkhard A. J. Kempf
Director of the Institute of Medical Microbiology and Hospital Hygiene
University Hospital Frankfurt
Goethe University Frankfurt
Phone: +49 (0)69 6301–5019
volkhard.kempf@kgu.de
Website: https://www.kgu.de/einrichtungen/institute/zentrum-der-hygiene/medizinische-mikrobiologie-und-krankenhaushygiene

If a therapy for chronic back pain is tailored specifically to a patient's individual requirements, the chances of success are far greater than with standard forms of treatment. Accompanied by a psychotherapeutic procedure in the shape of cognitive behavioural therapy, the pain can be alleviated even more effectively. This is the result of a meta-analysis by Goethe University Frankfurt, in which the data of over 10,000 patients were combined and analysed. It can be concluded from the study that multimodal therapies should be promoted on a larger scale in the German healthcare system, in line with the National Disease Management Guidelines.

FRANKFURT. Lack of exercise, bad posture, overexertion, constant stress at work or at home – back pain is a widespread condition with many causes. For a not insignificant number of sufferers, the symptoms are even chronic, meaning they persist for a long time or recur again and again. Sport and exercise therapies under instruction can bring relief. Common treatment methods include physiotherapy as well as strength and stability exercises. But how can the therapy be as successful as possible? Which approach alleviates pain most effectively? A meta-analysis by Goethe University Frankfurt, published recently in the Journal of Pain, has delivered new insights.

The starting point was data from 58 randomised controlled trials (RCTs) of over 10,000 patients worldwide with chronic low back pain. First, the data relevant to the topic were filtered out of the original manuscripts and then evaluated in groups. When evaluating these data, the researchers examined on the one hand whether and to what extent standard forms of treatment and individualised treatment differ in terms of the result. “Individualised" means that there is some type of personal coaching, where therapists specifically target the potentials and requirements of each patient and decide together with them how their therapy should look.

The study concluded that individualised treatment for chronic back pain led to a significantly increased effect in comparison to standard exercise therapies. The success rate in pain relief was 38 percent higher than with standard treatment. “The higher effort required for individual treatment is worthwhile because patients benefit to an extent that is clinically important," says lead author Dr Johannes Fleckenstein from the Institute of Sport Sciences at Goethe University Frankfurt.

However, the study went even further. The research team in Frankfurt compared a third group of treatment methods alongside the standard and individualised ones. In this group, individualised training sessions were combined with cognitive behavioural therapy (CBT). This procedure – a type of talk therapy – is based on the assumption that negative thoughts and behaviours surrounding pain tend to exacerbate it. Through CBT, pain patients learn to change the way they handle it. They stop being afraid to move or are taught tactics for coping with pain. This makes them realise that they are by no means helpless. But what does the psychotherapeutic support through CBT actually contribute to the success of the treatment? Analysis of the data revealed the following: When an individualised approach and CBT were combined, the success rate in terms of pain relief was an impressive 84 percent higher than with standard treatment. The combined therapy, also called multimodal therapy, thus led to the best result by far.

Fleckenstein sees in the study “an urgent appeal to public health policy" to promote combined therapies both in terms of patient care and remuneration. “Compared to other countries, such as the USA, we are in a relatively good position in Germany. For example, we issue less prescriptions for strong narcotic drugs such as opiates. But the number of unnecessary X-rays, which, by the way, can also contribute to pain chronicity, and inaccurate surgical indications is still very high." This is also due, according to Fleckenstein, to economic incentives, that is, the relatively high remuneration for such interventions. The situation is different for organisations working in the area of pain therapy, he says. Although these are not unprofitable, they are not a cash cow for investors either. In his view, it is important here to improve the economic conditions. After all, pain therapy saves a lot of money in the long run as far as health economics are concerned, whereas tablets and operations rarely lead to medium and long-term pain relief.

Publication: Johannes Fleckenstein, Philipp Floessel, Tilman Engel, Laura Krempel, Josefine Stoll, Martin Behrens, Daniel Niederer. Individualized Exercise in Chronic Non-Specific Low Back Pain: A Systematic Review with Meta-Analysis on the Effects of Exercise Alone or in Combination with Psychological Interventions on Pain and Disability. The Journal of Pain (2022) https://doi.org/10.1016/j.jpain.2022.07.005

Picture download:

https://www.uni-frankfurt.de/126745085

Caption: People who sit a lot and do not exercise often develop back pain. Credits: Markus Bernards for Goethe University Frankfurt

Further information:

Dr. Johannes Fleckenstein
Sports Medicine and Exercise Physiology
Institute of Sports Sciences
Goethe University Frankfurt
johannes.fleckenstein@sport.uni-frankfurt.de
Instagram: @docfleckenstein

Editor: Dr Markus Bernards, Science Editor, PR & Communication Office, Theodor-W.-Adorno-Platz 1, 60323 Frankfurt am Main, Tel: -49 (0) 69 798-12498, Fax: +49 (0) 69 798-763 12531, bernards@em.uni-frankfurt.de.

For an adequate immune response, it is essential that T lymphocytes recognise infected or degenerated cells. They do so by means of antigenic peptides, which these cells present with the help of specialised surface molecules (MHC I molecules). Using X-ray structure analysis, a research team from Frankfurt has now been able to show how the MHC I molecules are loaded with peptides and how suitable peptides are selected for this purpose.

FRANKFURT. As task forces of the adaptive immune system, T lymphocytes are responsible for attacking and killing infected or cancerous cells. Such cells, like almost all cells in the human body, present on their surface fragments of all the proteins they produce inside. If these include peptides that a T lymphocyte recognises as foreign, the lymphocyte is activated and kills the cell in question. It is therefore important for a robust T-cell response that suitable protein fragments are presented to the T lymphocyte. The research team led by Simon Trowitzsch and Robert Tampé from the Institute of Biochemistry at Goethe University Frankfurt has now shed light on how the cell selects these protein fragments or peptides.

Peptide presentation takes place on so-called major histocompatibility complex class I molecules (MHC I). MHC I molecules are a group of very diverse surface proteins that can bind myriads of different peptides. They are anchored in the cell membrane and form a peptide-binding pocket with their outward-facing part. Like all surface proteins, MHC I molecules take the so-called secretory pathway: they are synthesised into the cell's cavity system (endoplasmic reticulum (ER) and Golgi apparatus) and folded there. Small vesicles then bud off from the cavity system, migrate to the cell membrane and fuse with it.

The maturation process of the MHC I molecules is very strictly controlled: in the ER, proteins known as “chaperones" help them fold. The chaperone tapasin is essential for peptide loading in this process. “When an MHC I molecule has bound a peptide, tapasin checks how tight the binding is," says Trowitzsch, explaining the chaperone's task. “If the bond is unstable, the peptide is removed and replaced by a tightly binding one." However, it has not yet been possible to clarify how exactly tapasin performs this task – especially because the loading process is extremely fast.

The biochemists and structural biologists from Goethe University Frankfurt have now succeeded for the first time in visualising the short-lived interaction between chaperone and MHC I molecule by means of X-ray structure analysis. To do this, they produced variants of the two interaction partners that were no longer embedded in the membrane, purified them and brought them together. A trick helped to capture the loading complex in action for crystallisation: first, the research team loaded the MHC I molecule with a high-affinity peptide so that a stable complex was created. A light signal triggered cleavage of the peptide, which greatly reduced its ability to bind the MHC I molecule. Immediately, tapasin entered the scene and remained bound to the MHC I molecule that lacks its peptide. “The photo-induced cleavage of the peptide was pivotal to the success of our experiment," says Tampé. “With the help of this optochemical biology, we can now systematically reproduce complex cellular processes one by one."

X-ray structure analysis of the crystals revealed how tapasin widens the peptide-binding pocket of the MHC I molecule, thereby testing the strength of the peptide bond. For this purpose, the interaction partners form a large contact area; for stabilisation, a loop of tapasin sits on top of the widened binding pocket. “This is the first time we have shown the process of loading at high resolution," Tampé is pleased to report. The images also reveal how a single chaperone can interact with the enormous diversity of MHC I molecules, says the biochemist: “Tapasin binds precisely the non-variable regions of the MHC I molecules." However, the new structure not only improves our understanding of the complex processes involved in loading MHC I molecules. It should also help select suitable candidates for vaccine development.

Publication: Ines Katharina Müller, Christian Winter, Christoph Thomas, Robbert M. Spaapen, Simon Trowitzsch, Robert Tampé. Structure of an MHC I–tapasin–ERp57 editing complex defines chaperone promiscuity. Nature Communications (2022) https://www.nature.com/articles/s41467-022-32841-9

Further information:
Professor Robert Tampé / Dr Simon Trowitzsch
CRC 1507 – Protein Assemblies and Machineries in Cell Membranes
Institute of Biochemistry, Biocenter
Goethe University Frankfurt
Tel.: +49 69 798-29475
tampe@em.uni-frankfurt.de
trowitzsch@biochem.uni-frankfurt.de
Website: https://www.biochem.uni-frankfurt.de/index.php?id=10

The transition zone between the Earth's upper and lower mantle contains considerable quantities of water, according to an international study involving the Institute for Geosciences at Goethe University in Frankfurt. The German-Italian-American research team analysed a rare diamond formed 660 kilometres below the Earth's surface using techniques including Raman spectroscopy and FTIR spectrometry. The study confirmed something that for a long time was only a theory, namely that ocean water accompanies subducting slabs and thus enters the transition zone. This means that our planet's water cycle includes the Earth's interior. (Nature Geoscience, DOI 10.1038/s41561-022-01024-y)

FRANKFURT. The transition zone (TZ) is the name given to the boundary layer that separates the Earth's upper mantle and the lower mantle. It is located at a depth of 410 to 660 kilometres. The immense pressure of up to 23,000 bar in the TZ causes the olive-green mineral olivine, which constitutes around 70 percent of the Earth's upper mantle and is also called peridot, to alter its crystalline structure. At the upper boundary of the transition zone, at a depth of about 410 kilometres, it is converted into denser wadsleyite; at 520 kilometres it then metamorphoses into even denser ringwoodite. 

“These mineral transformations greatly hinder the movements of rock in the mantle," explains Prof. Frank Brenker from the Institute for Geosciences at Goethe University in Frankfurt. For example, mantle plumes – rising columns of hot rock from the deep mantle – sometimes stop directly below the transition zone. The movement of mass in the opposite direction also comes to standstill. Brenker says, “Subducting plates often have difficulty in breaking through the entire transition zone. So there is a whole graveyard of such plates in this zone underneath Europe."

However, until now it was not known what the long-term effects of “sucking" material into the transition zone were on its geochemical composition and whether larger quantities of water existed there. Brenker explains: “The subducting slabs also carry deep-sea sediments piggy-back into the Earth's interior. These sediments can hold large quantities of water and CO2. But until now it was unclear just how much enters the transition zone in the form of more stable, hydrous minerals and carbonates – and it was therefore also unclear whether large quantities of water really are stored there." 

The prevailing conditions would certainly be conducive to that. The dense minerals wadsleyite and ringwoodite can (unlike the olivine at lesser depths) store large quantities of water– in fact so large that the transition zone would theoretically be able to absorb six times the amount of water in our oceans. “So we knew that the boundary layer has an enormous capacity for storing water," Brenker says. “However, we didn't know whether it actually did so."

An international study in which the Frankfurt geoscientist was involved has now supplied the answer. The research team analysed a diamond from Botswana, Africa. It was formed at a depth of 660 kilometres, right at the interface between the transition zone and the lower mantle, where ringwoodite is the prevailing mineral. Diamonds from this region are very rare, even among the rare diamonds of super-deep origin, which account for only one percent of diamonds. The analyses revealed that the stone contains numerous ringwoodite inclusions – which exhibit a high water content. Furthermore, the research group was able to determine the chemical composition of the stone. It was almost exactly the same as that of virtually every fragment of mantle rock found in basalts anywhere in the world. This showed that the diamond definitely came from a normal piece of the Earth's mantle. “In this study we have demonstrated that the transition zone is not a dry sponge, but holds considerable quantities of water," Brenker says, adding: “This also brings us one step closer to Jules Verne's idea of an ocean inside the Earth." The difference is that there is no ocean down there, but hydrous rock which, according to Brenker, would neither feel wet nor drip water.

Hydrous ringwoodite was first detected in a diamond from the transition zone as early as 2014. Brenker was involved in that study, too. However, it was not possible to determine the precise chemical composition of the stone because it was too small. It therefore remained unclear how representative the first study was of the mantle in general, as the water content of that diamond could also have resulted from an exotic chemical environment. By contrast, the inclusions in the 1.5 centimetre diamond from Botswana, which the research team investigated in the present study, were large enough to allow the precise chemical composition to be determined, and this supplied final confirmation of the preliminary results from 2014.

The transition zone's high water content has far-reaching consequences for the dynamic situation inside the Earth. What this leads to can be seen, for example, in the hot mantle plumes coming from below, which get stuck in the transition zone. There, they heat up the water-rich transition zone, which in turn leads to the formation of new smaller mantle plumes that absorb the water stored in the transition zone. If these smaller water-rich mantle plumes now migrate further upwards and break through the boundary to the upper mantle, the following happens: The water contained in the mantle plumes is released, which lowers the melting point of the emerging material. It therefore melts immediately and not just before it reaches the surface, as usually happens. As a result, the rock masses in this part of the Earth's mantle are no longer as tough overall, which gives the mass movements more dynamism. The transition zone, which otherwise acts as a barrier to the dynamics there, suddenly becomes a driver of the global material circulation.

Publication: Tingting Gu, Martha G. Pamato, Davide Novella, Matteo Alvaro, John Fournelle, Frank E. Brenker, Wuyi Wang, Fabrizio Nestola: Hydrous peridotitic fragments of Earth's mantle 660 km discontinuity sampled by a diamond. Nature Geoscience (https://www.nature.com/articles/s41561-022-01024-y) 

Picture download: https://www.uni-frankfurt.de/125674824

Caption: The diamond from Botswana revealed to the scientists that considerable amounts of water are stored in the rock at a depth of more than 600 kilometres. Photo: Tingting Gu, Gemological Institute of America, New York, NY, USA 

Further Information:
Professor Frank Brenker
Department of Geoscience Mineralogy
Phone: +49 (0)69 798-40134
Mobile: +49 (0)151 68109472
f.brenker@em.uni-frankfurt.de

Immunologists Frederick W. Alt (73) of Harvard Medical School and David G. Schatz (64) of Yale School of Medicine are to receive the 2023 Paul Ehrlich and Ludwig Darmstaedter Prize, as the Scientific Council of the Paul Ehrlich Foundation announced today. The two researchers are being acknowledged for their discovery of molecules and mechanisms that enable our immune system to perform the astounding feat of recognizing billions of different antigens on first contact.

FRANKFURT. Both the antibodies produced by B cells and structures on the surface of T cells are able to capture antigens. Collectively, they are referred to as antigen receptors. In the first instance, their tremendous variety is thanks to different gene fragments combining at random to form functional genes. Almost 50 years ago, this principle was first demonstrated for the production of antibodies. However, the finer details of this somatic recombination remained largely in the dark until Alt and Schatz increasingly shed light on the subject. “The picture we have today of the diversification of antigen receptors in the immune system of vertebrates is above all thanks to the two prize winners," says Professor Thomas Boehm, Chairman of the Scientific Council of the Paul Ehrlich Foundation. “They have raised our knowledge of the development of the immune system to a new level." 

Antigen receptors are proteins consisting of constant and variable parts. In each antibody, for example, two heavy and two light chains are joined together in a Y-shape. Which antigen an antibody can recognize depends on the variable parts in the arms of the Y. In each of our B cells, an antibody with different claws matures during its development in the bone marrow. In total, our body can build approximately ten billion different antibodies, although it has only about 20,000 protein blueprints in the form of genes. It achieves this by means of an extraordinarily daring procedure that makes cutting up and re-assembling the genetic information DNA on certain chromosomes of maturing lymphocytes the norm. 

The enzyme complex RAG1/2 discovered by David Schatz and colleagues conducts these cuts at pre-designated sites. For the formation of the variable portions of heavy antibody chains, for example, these sites are located on chromosome 14. There, they flank relatively widely spaced segments in three different regions called V (for variable), D (for diversity), and J (for joining). RAG1/2 conducts cuts at a randomly selected segment from each of these regions for each antibody. Subsequently, DNA repair enzymes assemble a VDJ gene to encode a heavy chain variable region. Frederick Alt discovered the repair enzymes that work together to join the ends of the cut-out segments. In the next step of B cell maturation, the light chains are formed in a similar way, but only a VJ recombination occurs there in this case.

The RAG enzymes do not, however, wander aimlessly through the cell nucleus of immature lymphocytes. On the contrary, they draw the chromatin filaments together, in which the DNA is coiled up in a space-saving way, temporarily and again and again to form V(D)J recombination centers. There, they perform chromatin scanning. In this process, a chromatin loop, which can be more than one million DNA letters long, passes through the recombination center so that widely separated sections of text can be reliably linked together. The loop extrusion mechanism of V(D)J recombination elucidated by Frederick Alt elegantly explains how these loops are created and pulled through the recombination center.

Frederick Alt made further decisive contributions to the understanding of antigen receptor diversity. For example, he succeeded in showing that combinatorial diversity is increased many-fold by the enzymatic insertion of very short random DNA sequences, called N-nucleotides, at the interfaces of the gene segments to be joined. In B cells, antibody diversity is further potentiated by the phenomenon of somatic hypermutation. In this process, the normal rate of mutations affecting only one DNA letter is increased millions of times in the regions of the V segments by an enzyme. Alt, Schatz, and others showed how this enzyme performs its work with pinpoint accuracy. They thus provided a framework for solving the question of how B cells can take advantage of the enormous mutational capacity of AID for antibody maturation without running the risk of suffering tumor-inducing mutations.

Without the recombination-activating enzyme complex RAG1/2, the diversification of antigen receptors is impossible, the maturation of the lymphocytes is disrupted, and a severe immune defect is the consequence. It is all the more remarkable that this molecule apparently originates from a jumping gene – a transposon. These are selfish DNA parasites that crept into our genome at some point and can move from one place to another as jumping genes. Because of their uncontrolled distribution, they can be involved in the development of disease. RAG1/2, however, according to David Schatz's findings, descends from a transposon that all jawed vertebrates, including us humans, tamed for their own purposes very early in evolution. To prevent it from jumping on, they had to fix it in the genome. Schatz has shown which biochemical mechanisms enable this fixation. He was also able, on the basis of structural biological studies in an ancient invertebrate RAG gene to reproduce the act of transposition over several stages. He is thus giving science a fascinating look back at a revolutionary process at the beginning of vertebrate evolution: the development of the adaptive immune system in addition to already existing innate immunity. Building on this view from basic research, translational research will be able to open up new therapeutic perspectives for diseases in which our immune system plays a crucial role.

Frederick W. Alt (Website) is the Charles A. Janeway Professor of Pediatrics and Director of the Program in Cellular and Molecular Medicine at Boston Children's Hospital, a Howard Hughes Medical Institute Investigator, and a Professor of Genetics at Harvard Medical School.

David G. Schatz (Website) is Professor of Molecular Biophysics and Biochemistry at Yale University and Chairperson of the Department of Immunobiology at Yale School of Medicine.

Photos of the award winners are available for use at www.paul-ehrlich-stiftung.de.

Background information with the title “Protected by a tamed parasite"

The prizes will be awarded by the Chairman of the Scientific Council of the Paul Ehrlich Foundation on 14 March 2023 at 5 p.m. in Frankfurt's Paulskirche. We kindly ask you to take this into consideration when planning your diary. Please do not hesitate to contact us if you have any questions.

Further information
Press Office
Paul Ehrlich Foundation
Joachim Pietzsch
Tel.: +49 (0)69 36007188
Email: j.pietzsch@wissenswort.com
www.paul-ehrlich-stiftung.de

The Paul Ehrlich and Ludwig Darmstaedter Prize is Germany's most renowned medical award, endowed with 120,000 euros. It is traditionally awarded on Paul Ehrlich's birthday, 14 March, in Frankfurt's Paulskirche. It honours scientists who have made special contributions in areas of research represented by Paul Ehrlich's achievements, namely in immunology, cancer research, haematology, microbiology and chemotherapy. The prize, which has been awarded since 1952, is funded by the Federal Ministry of Health, the German Association of Research-based Pharmaceutical Companies (Verband Forschender Arzneimittelhersteller e.V.) and by earmarked donations from the following companies, foundations and institutions: Else Kröner-Fresenius-Foundation, Sanofi-Aventis Deutschland GmbH, C.H. Boehringer Sohn AG & Co. KG, Biotest AG, Hans und Wolfgang Schleussner-Foundation, Fresenius SE & Co. KGaA, F. Hoffmann-LaRoche Ltd., Grünenthal Group, Janssen-Cilag GmbH, Merck KGaA, Bayer AG, Georg von Holtzbrinck GmbH & Co.KG, AbbVie Deutschland GmbH & Co. KG., B. Metzler seel. Sohn & Co KGaA. The award winners are selected by the Scientific Council of the Paul Ehrlich Foundation. A list of the members of the Scientific Council is available on the website of the Paul Ehrlich Foundation. 

The Paul Ehrlich Foundation is a legally dependent foundation administered in trust by the Association of Friends and Benefactors of Goethe University. Honorary President of the Foundation, which was established in 1929 by Hedwig Ehrlich, is Professor Dr Katja Becker, President of the German Research Foundation, who also appoints the elected members of the Foundation Council and the Board of Trustees. The Chairman of the Scientific Council of the Paul Ehrlich Foundation is Professor Dr Thomas Boehm, Director at the Max Planck Institute for Immunobiology and Epigenetics in Freiburg, and the Chairman of the Board of Trustees is Professor Dr Jochen Maas, Managing Director Research & Development, Sanofi-Aventis Deutschland GmbH. In his function as Chairman of the Association of Friends and Benefactors of Goethe University, Prof. Dr Wilhelm Bender is also a member of the Scientific Council of the Paul Ehrlich Foundation. The President of Goethe University is in this capacity also a member of the Board of Trustees.