Goethe-Universität — Press releases

Jan 16 2026

09:38

One of Only a Few Devices Worldwide Enables Imaging of Living Cells

A View into the Innermost Workings of Life: First Scanning Electron Microscope with Nanomanipulator in Hesse Inaugurated at Goethe University

Goethe University Frankfurt (Germany) ceremonially commissioned a state-of-the-art cryo plasma-FIB scanning electron microscope with nanomanipulator worth more than 5 million euros on Thursday. The large-scale instrument, supported by the Dr. Rolf M. Schwiete Foundation, is the first of its kind in Hesse and one of only a few in Germany. It enables precise nanobiopsies of biological samples such as tissue or cell aggregates and is a key technology for the Cluster of Excellence SCALE, where researchers investigate the molecular foundations of cells.

FRANKFURT. With a so-called cryo plasma-FIB (Plasma Focused Ion Beam) scanning electron microscope with nanomanipulator, the Goethe University in Frankfurt (Germany) is expanding its research infrastructure with a powerful instrument. The microscope was inaugurated today at the Buchmann Institute for Molecular Life Sciences on the Riedberg Campus – as the first of its kind in Hesse and one of only a few in all of Germany.

The large-scale instrument works with a focused plasma ion beam, which can be used to prepare tiny sections from biological cells – so-called nanobiopsies with dimensions in the nanometer range. The decisive advantage over conventional ion beam microscopes: the plasma beam works more gently and faster, which is particularly important for sensitive biological samples such as water-containing cells. These ultra-thin sections can then be examined using both scanning electron microscopy and transmission electron microscopy. This makes it possible to visualize protein structures in their natural environment or to trace cellular changes in diseases such as Alzheimer's or cancer at the molecular level.

"This microscope bridges medicine and structural cell biology, opening up completely new possibilities for our research," emphasizes Prof. Achilleas Frangakis, who secured the large-scale instrument worth 5.6 million euros. "We can now visualize biological processes under the microscope that were previously hidden – such as how proteins work together in cells in the still unknown physiological context or even how diseases develop at the nanoscale."

The non-profit Dr. Rolf M. Schwiete Foundation provided substantial funding for the microscope, for which it was honored with a plaque on the device. For the Foundation, supporting high-quality medical research projects is a central concern in order to contribute to improving research conditions and advancing medical knowledge.

Prof. Bernhard Brüne, Vice President for Research at Goethe University, emphasized: "Without this generous funding, this acquisition would not have been possible. The device is indispensable for work in the Cluster of Excellence SCALE – it allows researchers to examine the architecture of cells in previously unattainable detail."

SCALE (Subcellular Architecture of Life) is a joint research project of Goethe University and Johannes Gutenberg University Mainz within the Rhine-Main Universities (RMU) alliance, the Max Planck Institutes for Biophysics and Brain Research, and other partners. Researchers there investigate how cellular structures are built and how errors in this molecular blueprint lead to diseases. The new microscope makes it possible to three-dimensionally image and analyze precisely these defective structures in cancer cells or in neurodegenerative diseases.

Prof. Maike Windbergs, Research Dean at the Department of Biochemistry, Chemistry and Pharmacy, noted that the device makes the Frankfurt location significantly more attractive for international collaborations. Prof. Martin Pos, Dean of Studies at the department, also emphasized that students and doctoral candidates here gain access to a technology that is only available at a few locations worldwide – an important building block for their scientific training and later careers.
Prof. Inga Hänelt, spokesperson for the Cluster of Excellence SCALE, stressed that the microscope will be used by researchers from both RMU partner universities as well as the other partners and allows new insights into the subcellular architecture of life.

Initial images have already deciphered a cellular structure that is crucial for human kidney function. The microscope is now available for a wide range of research projects.

Picture download:
https://www.uni-frankfurt.de/182148333

Caption: Prof. Dr. Achilleas Frangakis presents the scanning electron microscope with nanomanipulator supported by the Dr. Rolf M. Schwiete Foundation (image: Uwe Dettmar/Goethe University).

Further Information:
Prof. Dr. Achilleas Frangakis
Institute for Biophysics
Buchmann Institute for Molecular Life Sciences
Goethe-University Frankfurt, Germany
+49 69 / 798 46462
achilleas.frangakis@biophysik.uni-frankfurt.de
https://frangakis.biophysik.org/

Editor: Dr. Phyllis Mania, Science Editor, PR & Communications Office, Theodor-W.-Adorno-Platz 1, 60323 Frankfurt, Tel: +49 (0) 69 798-13001, mania@physik.uni-frankfurt.de

Jan 15 2026

13:12

Research team at Goethe University Frankfurt classifies all human E3 ligases – New opportunities for targeted protein degradation therapies

The “broker” family helps tidy up the cell

Cells must continually adjust their protein composition, which includes protein synthesis as well as degradation. Most regulated protein degradation is executed by the ubiquitin–proteasome system (UPS), in which proteins are tagged with ubiquitin and routed to a protein-shredder called proteasome. The enzyme E3 ligase plays a key role here by acting as a “broker” that mediates the labeling of the proteins to be degraded. A research team at Goethe University Frankfurt has now made the first systematic catalog and relationship map of all human E3 ligases and identified 40 of them as potential key players in emerging drug classes such as PROTACs, which are used, for example, to treat cancer.

FRANKFURT. Maintaining cellular order is a major logistical challenge: Individual mammalian cells contain billions of protein molecules, which must be synthesized, deployed, and removed with precision. In the ubiquitin-proteasome system (UPS), proteins destined for degradation are tagged with chains of several ubiquitin proteins and then degraded by the proteasome. The crucial step is the target selection: E3 ligases are enzymes that act as molecular “broker” by binding specific target proteins and coordinating the transfer of ubiquitin from an E2 enzyme.

As an E3 ligase recognizes only a restricted set of target proteins, cells maintain a large and diverse E3 ligase repertoire. A research team at Goethe University Frankfurt, led by Dr. Ramachandra M. Bhaskara from the Institute of Biochemistry II, has now compiled all members of the “broker family” in a catalog and mapped for the first time how human E3 ligases relate to one another, and what that implies for function, substrate recognition, and drug discovery.

A data-driven map of the “E3 ligome”

To describe the broker family – the so-called “E3 ligome” – the researchers performed AI-supported computational comparisons of E3 ligase features and then validated key functional inferences in cell culture experiments. In this way, the Frankfurt researchers defined 13 major families, as well as subfamilies, which capture more similarities between E3 ligase family members than shared amino acid sequences and structural characteristics. Bhaskara explains: “Our data-driven machine-learning approach reveals family-specific functions. For example, members of one family are important for DNA repair programs and for preventing unplanned cell death, while those of another are involved in antiviral defense.”

Beyond their role in protein degradation, E3 ligases are also implicated in ubiquitin signaling, which is not used for protein degradation, broadening their relevance across cellular pathways and disease mechanisms.

Implications for next-generation therapeutics

The new E3 ligase map is particularly relevant for targeted protein degradation strategies used in novel types of active pharmaceutical substances such as PROTACs. PROTACs (Proteolysis Targeting Chimeras) are bifunctional molecules that bring an E3 ligase into proximity with a disease-relevant protein, triggering ubiquitin tagging and proteasomal destruction of the disease-relevant protein. Although the field has advanced rapidly, most existing PROTAC programs rely on only a small number of well-characterized E3 ligases.

By systematically analyzing the full E3 ligome, the team identified 40 additional E3 ligases that may be suitable for PROTAC development—and, importantly, the family relationships may help researchers repurpose or adapt ligands and design principles across related E3 ligases. This could widen the range of tissues, cellular contexts, and diseases that targeted degradation can reach.

Open resource for the research community

Because many groups worldwide are developing targeted degradation approaches, the Goethe University team has made the complete E3 ligome publicly available via a dedicated database, enabling other researchers to build on the classification and functional insights.

Publication: Arghya Dutta, Alberto Cristiani, Siddhanta V. Nikte, Jonathan Eisert, Yves Matthess, Borna Markusic, Cosmin Tudose, Chiara Becht, Varun Jayeshkumar Shah, Thorsten Mosler, Koraljka Husnjak, Ivan Dikic, Manuel Kaulich, Ramachandra M. Bhaskara: Multi-scale classification decodes the complexity of the human E3 ligome. Nature Communications (2025) https://doi.org/10.1038/s41467-025-67450-9

Picture download:
https://www.uni-frankfurt.de/181983680

Captions:
1.Sun of families: Researchers at Goethe University have elucidated the relationships among all 462 catalytic human E3 ligases; E3 ligases also support non-degradative functions. Image: Ramachandra M. Bhaskara, Goethe University Frankfurt

2. PROTACs and E3 ligases: PROTACs link a target protein (protein of interest, POI) with an E3 ligase, which mediates the ubiquitin labeling (yellow) of the POI via an E2 enzyme. The POI is then degraded in the proteasome shredder (blue). Image: Institute of Biochemistry II, Goethe University Frankfurt

Contact:
Dr. Ramachandra M. Bhaskara
Team Leader Computational Cell Biology
Institute of Biochemistry II
Goethe University Frankfurt, Germany
Tel. +49 (0)69 7984-2526
Bhaskara@med.uni-frankfurt.de
https://biochem2.com/people/bhaskara-ramachandra-m

Jan 12 2026

11:53

Protein Engineering Enables Sustainable Production of Industrially Important Fatty Acids

From Palm Oil to Designer Enzymes: Frankfurt Researchers Reprogram Yeast Cells

Fatty acids derived from palm oil and coconut oil are found in countless everyday products, but their extraction drives deforestation. Researchers at Goethe University Frankfurt (Germany) have now reprogrammed the enzyme fatty acid synthase to produce custom fatty acids of any chain length. With just two targeted modifications, the enzyme can be redirected from producing the usual 16-carbon fatty acids to generating shorter chains. In collaboration with a partner laboratory in China, the engineered fatty acid synthase was implemented in yeast strains to enable sustainable bioreactor-based production of industrially relevant fatty acids.

FRANKFURT. Whether laundry detergents, mascara, or Christmas chocolate – many everyday products contain fatty acids from palm oil or coconut oil. However, the extraction of these raw materials is associated with massive environmental issues: rainforests are cleared, habitats for endangered species are destroyed, and traditional farmers lose their livelihoods. The team led by Prof. Martin Grininger at Goethe University in Frankfurt, Germany, has now developed a biotechnological approach that could enable a more environmentally friendly production method.

A Molecular Assembly Line with Precise Control
At the heart of this research is an enzyme called fatty acid synthase (FAS) – a type of molecular assembly line that builds fatty acids in all living organisms. “FAS is one of the most important enzymes in a cell's metabolism and has been fine-tuned by evolution over millions of years," explains Grininger.

The enzyme typically produces palmitic acid, a 16-carbon fatty acid that serves as a building block for cell membranes and energy storage. Industry, however, primarily requires shorter variants with 6 to 14 carbon atoms, which today are sourced from plant oils produced on large-scale oil palm plantations linked to deforestation and biodiversity loss. The decisive advantage of the new, FAS-based method: “Fundamentally, our advantage lies in the very precise control of chain length. We can theoretically make any chain length, and we're demonstrating this with the example of C12 fatty acid, which otherwise can only be obtained from palm kernels or coconut," says Grininger.

Understanding Through Modification
Grininger and his team have significantly contributed to understanding the molecular foundations of FAS over the past 20 years. They discovered that chain length is regulated by the interplay between two subunits: ketosynthase repeatedly elongates the chain by two carbon atoms while thioesterase cleaves off the finished chain as a fatty acid. “We then asked ourselves whether we could go beyond analysis and build FAS with new chain length regulation," says Grininger. “True understanding begins when you can change or customize a phenomenon."

Two Targeted Interventions Lead to Success
Grininger's doctoral student Damian Ludig took up this idea. “We asked what would happen if we specifically intervened in the interaction between these two subunits," Ludig explains. “Could we then control the chain length of the fatty acids that are produced?"

Ludig employed protein engineering methods where individual amino acids can be exchanged or entire protein regions modified. “Two changes to FAS through protein engineering ultimately led us to our goal," says Ludig. “In the ketosynthase subunit, I first exchanged one amino acid which resulted in chains being extended only with low efficiency beyond a certain length. Additionally, I replaced the thioesterase subunit with a similar protein from bacteria that shows activity in cleaving short chains." Depending on further adjustments, Ludig was able to produce short- and medium-length fatty acids.

From Frankfurt to Dalian
Collaboration with Prof. Yongjin Zhou's research group at Dalian Institute of Chemical Physics, Chinese Academy of Sciences, ultimately achieved breakthrough results. Supported by the German Research Foundation (DFG) and the National Natural Science Foundation of China (NSFC), Zhou and his lab succeeded in developing yeast strains that produce fatty acids containing only 12 carbon atoms instead of 16. Various designer FAS from Grininger's lab were integrated into these yeasts for optimization.
Both laboratories have already filed patents for their technologies. “On the Chinese side, Unilever was involved in this project. Our development has thus far taken place without industrial participation. However, we are striving for a collaboration with an industry partner in order to bring the technology into application," says Grininger.

Thinking Ahead: From Fatty Acids to Pharmaceuticals
In a second project, Felix Lehmann from Grininger's lab took the research even further by investigating how universally applicable FAS are for tailored biosyntheses: “This question is also driven by necessity – to continually develop chemical processes towards more sustainable green chemistry," explains Grininger.

The specific question was: Can FAS be redirected to make not only fatty acids, but also entirely different compounds, such as styrylpyrones? These molecules are precursors to substances derived from kava plants that attract medical interest due to their potential anxiolytic properties. Here, too, Lehmann achieved success with relatively few modifications: “First we cut away part of FAS that we didn't need for our target products; then we altered ketosynthase so that cinnamic acid could be used as starting material," he explains. The team even integrated another protein into the FAS structure so it became part of multi-enzyme complex.

“In this project we systematically examined how entire biosynthetic pathways can be constructed with FAS from readily available building blocks," Grininger explains. While the results do not yet have immediate practical applications, they provide important guidance for the future design of novel synthases.

At the Intersection of Chemistry and Biology
“Our lab has made significant strides towards biocatalysis and biotechnological applications over recent years, driven by the contributions of many projects and collaborations. We will continue down this path", Grininger summarizes. “Within the Cluster of Excellence SCALE, we will also use this enzyme to generate tailored biomembranes, whose analysis will help deepen our understanding of key organelles such as the endoplasmic reticulum and mitochondria."

Whether technology can indeed alleviate palm oil issues now depends on successful scaling up alongside industry partners. The scientific foundation has certainly been laid and the lab still has many ideas to explore.

Publications:
Damian L. Ludig, Xiaoxin Zhai, Alexander Rittner, Christian Gusenda, Maximilian Heinz, Svenja Berlage, Ning Gao, Adrian J. Jervis, Yongjin J. Zhou & Martin Grininger. Engineering metazoan fatty acid synthase to control chain length applied in yeast. Nature Chemical Biology (2026) https://doi.org/10.1038/s41589-025-02105-w

Felix Lehmann, Nadja Joachim, Carolin Parthun, Martin Grininger. Design of a Multienzyme Derived from Mouse Fatty Acid Synthase for the Compartmentalized Production of 2-Pyrone Polyketides. Angewandte Chemie International Edition (2025). https://doi.org/10.1002/anie.202511726

Picture download:
https://www.uni-frankfurt.de/181986496

Caption:
File “Palmoil_Shutterstock": Palm oil plantations often stretch for kilometers and pose a problem for humans and animals alike (Image: Shutterstock).
File “Biosynthesis_LehmannGrininger_EN": Schematic representation of biosynthesis in a cell (top) and in the laboratory (bottom). The designer enzyme shortens the chain length of the fatty acid (Image: Felix Lehmann & Martin Grininger/Goethe University).

Further Information:
Prof. Dr. Martin Grininger
Institute for Organic Chemistry and Chemical Biology
Buchmann Institute for Molecular Life Sciences
Goethe University Frankfurt
Max-von-Laue-Str. 15
60438 Frankfurt am Main, Germany
+49 (0)69 798 42705
grininger@chemie.uni-frankfurt.de
https://www.greeninger-chemistry.com/

Editor: Dr. Phyllis Mania, Science Editor, PR & Communications Office, Theodor-W.-Adorno-Platz 1, 60323 Frankfurt, Tel: +49 (0) 69 798-13001, mania@physik.uni-frankfurt.de

Dec 19 2025

10:12

Frankfurt research team presents first comprehensive analysis on the distribution of the human-pathogenic parasite in Europe

Continuous spread: Raccoon roundworm detected in nine European countries

The raccoon roundworm Baylisascaris procyonis can cause severe diseases in humans, including fatal brain damage. A research team from the ZOWIAC collaborative project at Goethe University Frankfurt has now presented the first comprehensive analysis for Europe: The parasite is already established in nine countries and continues to spread. The study combines new investigations of 146 raccoons from Germany with a comprehensive evaluation of all available European data and has been published in the journal Parasitology Research.

FRANKFURT. While the spread of raccoons in Europe is often discussed, their companion tends to remain unnoticed: The raccoon roundworm Baylisascaris procyonis arrived in Europe at the beginning of the 20th century with the first raccoons from North America. Since their release or escape from fur farms, raccoons have spread uncontrollably across large parts of Central Europe – and their parasite with them. Germany is now considered the main distribution area for both species in Europe.

Dangerous companion of the raccoon
"This parasite can also infect humans and cause so-called larva migrans, in which migrating larvae damage tissues and organs," explains Prof. Dr. Sven Klimpel from Goethe University Frankfurt and the Senckenberg Biodiversity and Climate Research Centre. Humans become infected by accidentally ingesting infectious eggs found in soil, water, or on objects contaminated with raccoon feces.
A research team from the collaborative research project ZOWIAC (Zoonotic and Wildlife Ecological Impacts of Invasive Carnivores) has now investigated how far the parasite has already spread in Europe.

Insidious life cycle
The parasite's life cycle is complex: Adult roundworms live in the small intestine of raccoons. Females produce up to 180,000 eggs daily, which enter the environment via feces. At so-called raccoon latrines – preferred defecation sites – the resistant eggs accumulate. In the environment, they develop into infectious larvae within two weeks under adequate temperature and humidity conditions, and can survive for several years.

Children particularly at risk
Human infection with the raccoon roundworm is called baylisascariasis. Anne Steinhoff from Goethe University Frankfurt and first author of the study explains: "If the larvae enter the central nervous system, the disease can have severe consequences. Due to frequent hand-to-mouth contact, young children are primarily affected." Most known cases occur in North America, the natural distribution area of raccoons and the roundworm. There, in most documented cases, the disease led to permanent neurological damage or even death.
"Furthermore, it is assumed that many cases remain undetected or are misdiagnosed due to non-specific symptoms," Klimpel adds. "In Europe, diagnosis in humans is further complicated by the lack of specific diagnostic testing options." Definitive diagnosis is currently only possible at the Centers for Disease Control and Prevention (CDC) in the USA and Canada.

First comprehensive Europe-wide analysis
The aim of the study was to provide a current overview of the parasite's distribution in Europe and to identify research needs. To this end, the team led by Klimpel and Steinhoff examined raccoons from Germany by necropsy and supplemented these new data with a comprehensive analysis of available scientific studies and infection data from Europe.
Of the 146 raccoons examined, 66.4 percent were infected with Baylisascaris procyonis: 77.4 percent in Hesse, 51.1 percent in Thuringia, and 52.9 percent in North Rhine-Westphalia. The study provided prevalence data for Thuringia for the first time. "The results show both an expansion of the roundworm's distribution area and stable infection occurrence at high levels in German raccoon populations," Klimpel explains. The analysis revealed that the roundworm occurs in wild raccoons in nine European countries, primarily in Central Europe – in some cases with extremely high infection rates. In three additional countries, infections were detected in raccoons or other animal species in captivity.

Spread coupled to raccoon populations
"The studies show a steady expansion of the distribution area in Europe. The distribution of the roundworm is linked to the steady spread of its definitive host, the raccoon, which now occurs throughout Europe," Klimpel continues. "The actual distribution of the roundworm is likely significantly underestimated due to insufficient or absent data collection."
Particularly concerning: The urbanization of raccoon populations increases the likelihood of contact between humans and contaminated areas. Three documented cases of baylisascariasis in Europe are known – all resulted in permanent visual impairment.

"The results of this study make it clear that further research on the raccoon roundworm in Europe is urgently needed – particularly in light of growing raccoon populations and their increasing adaptation to urban habitats," Klimpel concludes.

Publication: Anne Steinhoff, Robin Stutz, Anna Viktoria Schantz, Norbert Peter, Dorian D. Dörge & Sven Klimpel. Baylisascaris procyonis on the rise in Europe: a comprehensive review and analysis of occurrence data. Parasitology Research (2025). https://doi.org/10.1007/s00436-025-08611-z

Picture download:
https://www.uni-frankfurt.de/181720394

Caption:
[Collage] Raccoons, which are invasive in Europe, are often infected with the parasitic raccoon roundworm Baylisascaris procyonis (circle) (photos: ZOWIAC/Goethe-Universität).

[Intestine] During dissection in the laboratory, it becomes clear how severely the intestine of a single raccoon is infected with Baylisascaris procyonis (photo: ZOWIAC/Goethe-Universität)

Contact
Prof. Dr. Sven Klimpel
Institute for Ecology, Evolution and Diversity
Goethe University Frankfurt, Germany
Senckenberg Biodiversity and Climate Research Centre
+49 69 798-42237
klimpel@bio.uni-frankfurt.de
https://zowiac.eu/

Editor: Dr. Phyllis Mania, Science Editor, PR & Communications Office, Theodor-W.-Adorno-Platz 1, 60323 Frankfurt, Tel: +49 (0) 69 798-13001, Fax 069 798-763-12531, mania@physik.uni-frankfurt.de

Dec 15 2025

15:25

Researchers at Universitaetsmedizin Frankfurt and Goethe University Identify Achilles’ Heel of the Oroya Pathogen Bartonella bacilliformis

Tropical Disease Oroya Fever: Elucidation of Disease Mechanism Opens Possibility for Novel Therapy

The bacterial pathogen Bartonella bacilliformis causes in South America one of the most dangerous infectious diseases known: the so-called “Oroya fever." Without antibiotic treatment, 90 percent of the infected patients will die, as the pathogen destroys red blood cells. Researchers at University Medicine Frankfurt have now clarified how the pathogen triggers this hemolytic disease. In laboratory experiments, they were even able to inhibit the destruction of red blood cells. The results open up a possible avenue for developing a novel therapy against this often fatal infectious disease.

FRANKFURT. The so-called “Oroya fever" is an extremely severe infectious disease, yet it is classified among the so-called neglected tropical diseases. This is because the infection occurs – so far – exclusively in high-altitude valleys of the South American Andes, primarily in Peru, but also in Ecuador and Colombia. As a result, it has received little attention from research and pharmaceutical development. Oroya fever is caused by the bacterium Bartonella bacilliformis, which is transmitted through the bite of infected sandflies of the genus Lutzomyia. The disease typically begins with high fever and massive destruction of red blood cells (erythrocytes), resulting in a severe hemolytic anemia. Without antibiotic treatment, Oroya fever is fatal in up to 90 percent of cases. Already 26 percent of the pathogens are resistant to the standard antibiotic ciprofloxacin, making antibiotic treatment significantly more difficult.

Lutzomyia sandflies are so far found only in South America. However, due to global warming and increasing travel, experts expect that the habitat of these sandflies could expand to other continents and even into Europe.

An international research team led by Professor Volkhard Kempf from Universitaetsmedizin Frankfurt and Goethe University has now generated and analyzed more than 1,700 genetic variants of the pathogen, identifying two proteins that Bartonella requires for the destruction of red blood cells: a so-called porin, which enables the exchange of substances such as ions with the environment, and an enzyme called α/β-hydrolase. Together, these two proteins are responsible for hemolysis. Structural analyses and targeted point mutations showed that the hemolytic activity of Bartonella bacilliformis strictly depends on the enzymatic integrity of the α/β-hydrolase. “Both proteins work together to destroy human erythrocytes and thereby provide an explanation for the characteristic clinical presentation of Oroya fever," explains Dr. Alexander Dichter, first author of the study. “This makes the α/β-hydrolase a suitable target protein for therapeutic agents."

In laboratory experiments, the researchers also identified an inhibitor – a phospholipase inhibitor – that blocks the activity of the α/β-hydrolase and can also prevent the hemolysis of erythrocytes. “If we succeed in selectively disabling the disease-causing effect of the bacterium in the human body in this way, we may have a therapy against which resistance is unlikely to develop," Dichter is convinced.

“Oroya fever is a serious public health problem in Peru and South America, killing hundreds of people every year without drawing attention from the rest of the world. The disease is poverty-related and belongs to the neglected tropical diseases, which receive far too little attention says Professor Volkhard Kempf, Director of the Institute of Medical Microbiology and Hospital Hygiene, which also hosts the German Consiliary Laboratory for Bartonella Infections (appointed by Robert Koch Institute, Berlin). “We are therefore all the more pleased that we have laid the foundation for developing novel therapeutic approaches for Oroya fever and thus made an important contribution to the fight against this deadly neglected tropical disease."

With the project's funding period now ended, efforts are underway to secure further financial support to continue the research, Kempf explains. “Now that we have elucidated the mechanisms of hemolysis, our next goal is to understand how the pathogen binds to erythrocytes, since adhesion of pathogens to host cells is always the first step in any infection. We were able to elucidate the adhesion mechanisms of a related pathogen, the bacterium Bartonella henselae, several years ago."

Background information

Detection of Bartonella bacilliformis: Tracing a Dangerous Infectious Disease (2023)
https://aktuelles.uni-frankfurt.de/unireport/auf-den-spuren-einer-gefaehrlichen-infektionskrankheit/

Frankfurt–Lima Research Axis
The publication represents another success of a cooperation that has existed since 2019 between Universitätsmedizin Frankfurt and the Universidad Peruana Cayetano Heredia in Lima. It is part of a series of publications within the German-Peruvian scientific network, in which several researchers from Lima have already worked in Frankfurt, and the Frankfurt team collected diagnostic samples in the endemic region during an expedition in 2022. As part of a follow-up project, Peruvian young scientist Luis Solis-Cayo analyzed new Bartonella bacilliformis patient isolates from Peru in 2024 and 2025 for their pathogenic properties.

The research was funded by the State of Hesse through the LOEWE Center DRUID (2018–2024), which aimed to advance research by universities in Hesse in the fight against neglected tropical diseases.

Publication: Alexander A. Dichter, Florian Winklmeier, Diana Munteh, Wibke Ballhorn, Sabrina A. Becker, Beate Averhoff, Halvard Bonig, Adrian Goldman, Meritxell García-Quintanilla, Luis Solis Cayo, Pablo Tsukayama, Volkhard A. J. Kempf: Porin A and α/β-hydrolase are necessary and sufficient for hemolysis induced by Bartonella bacilliformis. Nature Communications (2025). DOI: https://doi.org/10.1038/s41467-025-66781-x

Picture download: https://www.uni-frankfurt.de/181481095

Caption: Bartonella bacilliformis (blue) infecting human erythrocytes. Image: Juergen Berger, Max Planck Institute for Biology, Tübingen, Germany, CC-BY 4.0: https://creativecommons.org/licenses/by/4.0/

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

Bluesky: @goetheuni.bsky.social #BeatNTDs #TropicalDiseases
Linkedin: @Goethe-Universität Frankfurt

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

Press releases

Goethe University PR & Communication Department

A View into the Innermost Workings of Life: First Scanning Electron Microscope with Nanomanipulator in Hesse Inaugurated at Goethe University

The “broker” family helps tidy up the cell

From Palm Oil to Designer Enzymes: Frankfurt Researchers Reprogram Yeast Cells

Continuous spread: Raccoon roundworm detected in nine European countries

Tropical Disease Oroya Fever: Elucidation of Disease Mechanism Opens Possibility for Novel Therapy