Press releases

Whether it is new and groundbreaking research results, university topics or events – in our press releases you can find everything you need to know about the happenings at Goethe University. To subscribe, just send an email to ott@pvw.uni-frankfurt.de

Goethe University PR & Communication Department 

Theodor-W.-Adorno Platz 1
60323 Frankfurt 
presse@uni-frankfurt.de

 

Aug 11 2023
08:21

New study by Goethe University Frankfurt shows: Effluents from wastewater treatment plants change the invertebrate communities in Hesse’s waters

Even treated wastewater affects our rivers

Wastewater treatment plants are undoubtedly a great achievement. After all, they have made a significant contribution to improving the quality of natural waters. A study published in the journal “Water Research" shows, however, that substances still manage to enter the water cycle that have an impact on the composition of the organisms living in it. 

Effluents from wastewater treatment plants have a dual effect: Some species disappear, while others benefit. Especially certain insect orders, such as stonefly and caddisfly larvae, are decimated. Certain worms and crustaceans, by contrast, can increase in number. A team from Goethe University Frankfurt led by Daniel Enns and Dr. Jonas Jourdan has corroborated this in a comprehensive study, which has now been published in the journal “Water Research". They examined 170 wastewater treatment plants in Hesse in relation to species composition. 

Wastewater treatment plants are an indispensable part of our modern infrastructure; they have made a significant contribution to improving the quality of our surface waters. However, their ability to completely remove what are known as micropollutants from wastewater is mostly limited. These substances include, for example, active ingredients from pharmaceuticals and personal care products, pesticides and other synthetic substances enter waterbodies via the treated wastewater, placing an additional burden on rivers and streams. This exacerbates the challenges faced by already vulnerable insect communities and aquatic fauna. Previous studies – which have primarily focused on single wastewater treatment plants – have already shown that invertebrate communities downstream of such effluents are generally dominated by pollution-tolerant taxa. 

Until now, however, it was unclear how ubiquitous these changes are. That is why a team of biologists from Goethe University Frankfurt has now studied extensively how wastewater from 170 wastewater treatment plants in Hesse has an impact on the species composition of invertebrates. This has prompted a change in the common conception that human-induced stressors reduce the number of species in a habitat and thus their diversity: Rather, the findings indicate that a shift in species composition can be observed. The researchers were able to identify significant shifts in the composition of the species community between sites located upstream and downstream of wastewater treatment plants. Some species were particularly affected by effluents from wastewater treatment plants – such as stonefly and caddisfly larvae, which disappear entirely in some places. Other taxa, such as certain worms and crustaceans, by contrast, benefit and are found in greater numbers. This change can be observed especially in streams and smaller rivers. Overall, wastewater treatment plants alter conditions downstream to the advantage of pollution-tolerant taxa and to the disadvantage of sensitive ones. 

How can we reduce water pollution?
Modern treatment techniques such as ozonation or activated charcoal filtering can make water treatment in wastewater treatment plants more efficient, allowing a wider range of pollutants, including many trace substances, to be removed from the wastewater before it is released into the environment. Merging smaller wastewater treatment plants can also contribute to reducing the burden on the environment. Whatever measures are taken, it is important to make sure that upstream sections are not already degraded and are in a good chemical and structural condition. 

Publication: Enns D, Cunze S, Baker NJ, Oehlmann J, Jourdan J (2023) Flushing away the future: The effects of wastewater treatment plants on aquatic invertebrates. Water Research, 120388. doi.org/10.1016/j.watres.2023.120388 

Picture download: https://www.uni-frankfurt.de/141365425

Caption:
Images 1+2: Treated wastewater is discharged into a nearby stream. In this way, numerous trace substances enter our waters. (Photos: Jourdan)
Image 3: The photograph shows a typical wastewater treatment plant. The wastewater passes through various treatment stages to remove pollutants before the treated water is discharged into the environment. (Photo: Jourdan) 

Further Information
Dr. Jonas Jourdan
Senior Scientist
Institute of Ecology, Diversity and Evolution
Goethe University Frankfurt
Tel.: +49(0)69-798-42149
Email: jourdan@bio.uni-frankfurt.de
Twitter: @Jourdan_Jonas


Editor: Dr. Anke Sauter, Science Editor, PR & Communication Office, Tel: +49 (0)69 798-13066, Fax: +49 (0) 69 798-763 12531, sauter@pvw.uni-frankfurt.de

 

Aug 9 2023
14:25

Institute for Social Research [Institut für Sozialforschung, IfS] hosts three-day international conference on “Futuring Critical Theory”, September 13-15, 2023

Current standing and reorientation of Critical Theory 

To mark its 100th anniversary, the IfS Institute for Social Research is organizing an international conference, titled "Futuring Critical Theory", which will take place on Goethe University Frankfurt's Westend Campus from September 13-15, 2023. The conference sets out to determine where Critical Theory stands, and to reorient it in light of the existential challenges of our times. 

Several of the supposed certainties of Frankfurt School Critical Theory have in part been fundamentally challenged in the course of recent academic and political debates on, for example, post- and de-colonialism, queer feminism, as well as new materialism. Specifically, there are two fronts where the theory has been put to the test: On the one hand, the explanatory power of an approach that in its interpretation of crises has so far neither focused on the global interconnectedness of social phenomena nor on the material dimension of social reproduction has been called into question. On the other hand, it is debatable whether classical Critical Theory's normative tools are still appropriate for theorizing contemporary social relations. 

The "Futuring Critical Theory" conference marking IfS' centennial will be the place where the process of developing a new research program for the Institute comes to a preliminary conclusion, and the results presented to a broader public for the first time. The three conference days are divided into four sections: I Dissecting Critical Theory; II Globalizing Critical Theory; III Materializing Critical Theory; IV Recomposing Critical Theory. 

For further information and to register, visit: https://fct2023.ifs.uni-frankfurt.de 

Contact: Mirko Broll, Research Associate and PR advisor, Institute for Social Research, broll@em.uni-frankfurt.de


Editor: Dr. Dirk Frank, Press Officer / Deputy Head of PR and Communication, Goethe University Frankfurt, Theodor-W.-Adorno-Platz 1, 60323 Frankfurt am Main, Phone +49 (0)69 798–13753, frank@pvw.uni-frankfurt.de

 

Aug 4 2023
10:58

Research team from Frankfurt shows how the pathogen can achieve significant functional modifications in protein complexes over short evolutionary time spans

How the hospital pathogen Acinetobacter baumannii quickly adapts to new environmental conditions

Hospital-acquired infections are often hard to treat because the corresponding pathogens become increasingly resistant against antibiotics. Here, the bacterium Acinetobacter baumannii is particularly feared, and there is great pressure to devise novel therapeutic approaches to combat it. Bioinformaticians from Goethe University Frankfurt and Research Unit FOR2251 of the German Research Foundation have now detected an unexpectedly wide diversity of certain cell appendages in A. baumannii that are associated with pathogenicity. This could lead to treatment strategies that are specifically tailored to a particular pathogen. 

Each year, over 670,000 people in Europe fall ill because of antibiotic-resistant pathogens, and 33,000 die from the infections. Especially feared are pathogens with resistances against multiple, or even all, known antibiotics. One of these is the bacterium Acinetobacter baumannii, feared today above all as the “hospital superbug": According to estimates, up to five percent of all hospital-acquired and one tenth of all bacterial infections resulting in death can be attributed to this pathogen alone. This puts A. baumannii right at the top of a list of pathogens for which – according to the World Health Organization (WHO) – there is an urgent need to develop new therapies. 

Understanding which characteristics make A. baumannii a pathogen is one of the prerequisites for this. To this end, bioinformaticians led by Professor Ingo Ebersberger of Goethe University Frankfurt and the LOEWE Center for Translational Biodiversity Genomics (LOEWE-TBG) are comparing the genomes and the proteins encoded therein across a wide range of different Acinetobacter strains. Conclusions about which genes contribute to pathogenicity can be drawn above all from the differences between dangerous and harmless strains. 

Due to a lack of suitable methods, corresponding studies have so far concentrated on whether a gene is present in a bacterial strain or not. However, this neglects the fact that bacteria can acquire new characteristics by modifying existing genes and thus also the proteins encoded by them. That is why Ebersberger's team has developed a bioinformatics method to track the modification of proteins along an evolutionary lineage and has now applied this method for the first time to Acinetobacter in collaboration with microbiologists from the Institute for Molecular Biosciences and the Institute of Medical Microbiology and Infection Control at Goethe University Frankfurt. 

In the process, the researchers concentrated on hair-like cell appendages, known as type IVa (T4A) pili, which are prevalent in bacteria and that they use to interact with their environment. The fact that they are present in harmless bacteria on the one hand and have even been identified as a key factor for the virulence of some pathogens on the other suggests that the T4A pili have repeatedly acquired new characteristics associated with pathogenicity during evolution. 

The research team could show that the protein ComC, which sits on the tip of the T4A pili and is essential for their function, shows conspicuous changes within the group of pathogenic Acinetobacter strains. Even different strains of A. baumannii have different variants of this protein. This leads bioinformatician Ebersberger to compare the T4A pili to a multifunctional garden tool, where the handle is always the same, but the attachments are interchangeable. “In this way, drastic functional modifications can be achieved over short evolutionary time spans," Ebersberger is convinced. “We assume that bacterial strains that differ in terms of their T4A pili also interact differently with their environment. This might determine, for example, in which corner of the human body the pathogen settles." 

The aim is to use this knowledge of the unexpectedly high diversity within the pathogen to improve the treatment of A. baumannii infections, as Ebersberger explains: “Building on our results, it might be possible to develop personalized therapies that are tailored to a specific strain of the pathogen." However, the study by Ebersberger and his colleagues also reveals something else: Previous studies on the comparative genomics of A. baumannii have presumably only unveiled the tip of the iceberg. “Our approach has gone a long way towards resolving the search for possible components that characterize pathogens," says Ebersberger. 

Publication: Ruben Iruegas, Katharina Pfefferle, Stephan Götting, Beate Averhoff, Ingo Ebersberger: Feature-architecture aware phylogenetic profiling indicates a functional diversification of type IVa pili in the nosocomial pathogen Acinetobacter baumannii. PLOS Genetics (2023) https://doi.org/10.1371/journal.pgen.1010646 

Picture download: https://www.uni-frankfurt.de/141211330 

Caption: Like a multifunctional gardening tool, the T4A pili of different Acinetobacter strains have evolutionarily modified the ComC protein at their tip (oval, in different colors) to settle in different niches within humans. Gray bars: cell envelope. Graphic: Katharina Pfefferle, Goethe University 

Further Information:
Professor Ingo Ebersberger
Institute of Cell Biology and Neuroscience
Goethe University Frankfurt, Germany
Tel.: +49 (0)69 798 42112
ebersberger@bio.uni-frankfurt.de
Website: http://www.bio.uni-frankfurt.de/43045195/ak-ebersberger
https://www.bio.uni-frankfurt.de/51172482/Forschergruppe_FOR2251 

Twitter: @goetheuni


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

 

Aug 3 2023
10:05

An international research team from Frankfurt and New York has successfully demonstrated the structure of a biomolecule used by Caenorhabditis elegans to detect danger

An escape signal for the nematode: Artificial intelligence helps elucidate structure of a novel light sensor 

The small Caenorhabditis elegans nematode avoids light. While it does not have eyes, some of its cells contain a protein called LITE-1, which warns it of the sun, whose rays are dangerous for the animal. A team of scientists from Goethe University Frankfurt, the Max Planck Institute of Biophysics, and the Simons Foundation's Flatiron Institute in New York has now elucidated the structure of LITE-1 – a completely new type of light-controlled ion channel. Instead of biochemical experiments, the researchers used artificial intelligence to elucidate the structure, and verified their structural model using biological experiments

In a compost heap, the nematode Caenorhabditis elegans finds a richly laid table: at a length of just one millimeter, the worm feeds on bacteria that decompose organic material. It is essential that the animal avoids sunlight – and not just to ensure its body remains at an optimal temperature and does not dry out. Energy-rich blue and UV light can result in great damage to the cells of the transparent worm, causing the hereditary molecule DNA to mutate, or resulting in the formation of reactive oxygen species such as hydrogen peroxide (H2O2). The latter can, for example, prevent the correct production of proteins and drive cells to death. Laboratory observations show that Caenorhabditis elegans reflexively withdraws from a beam of light. 

The nematode does not have eyes, but some of its sensory neurons contain the protein LITE-1, which converts light sensation into biochemical signals in a hitherto unknown manner, ultimately triggering the withdrawal reflex. A group of scientists led by Prof. Alexander Gottschalk of Goethe University Frankfurt, Prof. Gerhard Hummer of the Max Planck Institute of Biophysics and Goethe University, and Dr. Sonya Hanson of the Flatiron Institute has now elucidated the structure and function of LITE-1. To do so, they used the "AlphaFold2-Multimer" software, an artificial intelligence capable of predicting the structure of proteins and protein complexes based on the sequence of their amino acid building blocks. Their finding: LITE-1 is a so-called channel protein, which is located in the cell membrane and forms a kind of pore through which charged particles – i.e. ions – can pass to cross the membrane. 

"The AI worked really well and suggested a plausible structure for LITE-1," says Alexander Gottschalk. "In ensuing genetic experiments, we went on to check whether predictions based on this structure could also be verified in the live nematode and its response to light." To do so, the researchers specifically mutated individual amino acids in LITE-1 and observed the consequences on the light-evoked behavior. They found that, among other things, the replacement of amino acids that form the channel resulted in a complete loss of function of LITE-1. Additional mutation experiments revealed sites where the protein could interact with H2O2 and also uncovered a central amino acid that appears to be responsible for absorbing the energy generated by UV light. 

Gerhard Hummer explains: "It appears as if LITE-1 contains a whole network of amino acids, aligned like antennas, to capture the energy of the UV photons and pass it on to a central position in the protein. Here, a cavity is located which in turn could serve as a binding pocket for a chromophore – i.e., a molecule that can absorb photons or their energy." The researchers' model posits that this as yet unknown chromophore is additionally stimulated directly by blue light, and then transfers all the energy to the LITE-1 protein, leading to the opening of the ion channel and the influx of ions into the cell. The higher ion concentration becomes the starting point for a biochemical-electrical signal that eventually triggers the recoil reflex. 

Alexander Gottschalk adds that it apparently plays a role whether H2O2 induced by light exposure in the cells is also present: "The additional activation of LITE-1 by H2O2 ensures that the recoil reflex is not triggered by weak light, only by very intense, tissue-damaging light, such as direct sunlight." 

LITE-1 constitutes a very simple form of light perception. Gottschalk says comparisons with insect olfactory receptors suggest that LITE-1 is derived from such an olfactory receptor, which may have coincidentally bound a molecule that could also absorb light and thus transmit a warning signal of harmful light to the animal. 

Gottschalk emphasizes the importance of this receptor for the research field of optogenetics, which was co-founded in Frankfurt following the discovery and specification of the first light-dependent ion channel, termed “channelrhodopsin". The field of optogenetics provides the possibility of using light-controlled switches in cells to study cellular functions. "Both LITE-1 and similar proteins we analyzed may be used as new optogenetic tools, allowing us to extend the spectrum into the UV range." Computational biophysicist Sonya Hanson sees great potential for the future in the research methodology: "The AI we used is now so good that without laborious biochemical work we can still get an idea of how a particular protein works." 

Publication: Sonya M. Hanson, Jan Scholüke, Jana Liewald, Rachita Sharma, Christiane Ruse, Marcial Engel, Christina Schüler, Annabel Klaus, Serena Arghittu, Franziska Baumbach, Marius Seidenthal, Holger Dill, Gerhard Hummer, Alexander Gottschalk: Structure-function analysis suggests that the photoreceptor LITE-1 is a light-activated ion channel. Current Biology (2023), https://doi.org/10.1016/j.cub.2023.07.008 

Images for download: www.uni-frankfurt.de/141166470 

Caption: The novel LITE-1 photosensor protein of the Caenorhabditis elegans nematode responds as a danger sensor to UV and blue light. LITE-1 is a light-gated ion channel and the second form of light-gated ion channel discovered to date, after the long-known rhodopsin channel of algae.
LITE-1-multicolored: Alexander Gottschalk, Goethe University Frankfurt
LITE-1-bronze: Lucy Reading-Ikkanda/Simons Foundation 

Further information
Alexander Gottschalk
Professor of Molecular Membrane Biology and Neurobiology
Institute for Biophysical Chemistry and Buchmann Institute for Molecular Life Sciences
Goethe University Frankfurt
Tel. +49 (0)69 798-42518
a.gottschalk@em.uni-frankfurt.de
https://www.bmls.de/Cellular_and_Molecular_Neurobiology/aboutus.html
https://www.uni-frankfurt.de/69793125/Molecular_Membrane_Biology_and_Neurobiology 

Professor Gerhard Hummer
Max Planck Institute of Biophysics and
Institute of Biophysics at Goethe University Frankfurt
Tel. +49 (0)69 6303 2501
gerhard.hummer@biophys.mpg.de
https://www.biophys.mpg.de/theoretical-biophysics 

Sonya M. Hanson, Ph.D.
Center for Computational Biology
Center for Computational Mathematics
Flatiron Institute
New York, USA
shanson@flatironinstitute.org
https://www.simonsfoundation.org/structural-and-molecular-biophysics-collaboration/ 

Twitter: @GWormlab @sonyahans @goetheuni @SimonsFdn @MPIbp


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

 

Jul 28 2023
12:59

Researchers from Goethe University Frankfurt discover central switch point in mitochondrial signaling chain under misfolding stress 

Cell biology: How cellular powerhouses call for help when under stress

Originally, the powerhouses of higher cells, the mitochondria, were independent organisms. Researchers at Goethe University Frankfurt have investigated to what extent their metabolism has blended with that of their host cells in the course of evolution, using the example of a mitochondrial stress response. They have discovered that mitochondria send two different biochemical signals. These are processed together in the cell and trigger a support mechanism to restore cellular balance (homeostasis). The work was partly done within the ENABLE cluster initiative (now EMTHERA) at Goethe University Frankfurt. 

As life propagated across Earth in the form of the widest variety of single-celled organisms, sometime between 3.5 and a billion years ago one such organism managed an evolutionary coup: Instead of devouring and digesting bacteria, it encapsulated its prey and used it as a source of energy. As a host cell, it offered protection and nutrition in return. This is referred to as the endosymbiotic theory, according to which that single-celled organism was the primordial mother of all higher cells, out of which all animals, fungi and plants developed. Over the course of billions of years, the encapsulated bacterium became the cell's powerhouse, the mitochondrion, which supplies it with the cellular energy currency ATP. It lost a large part of its genetic material – its DNA – and exchanged smaller DNA segments with the mother cell. However, now as in the past, mitochondria divide independently of the cell and possess some genes of their own. 

How closely the cell and the mitochondrion work together in human cells today is what a team of researchers led by Dr. Christian Münch of Goethe University Frankfurt is investigating. They have now discovered how the mitochondrion calls for help from the cell when it is under stress. Triggers for such stress can be infections, inflammatory diseases or genetic disorders, for example, but also nutrient deficiencies or cell toxins. 

A certain type of mitochondrial stress is caused by misfolded proteins that are not quickly degraded and accumulate in the mitochondrion. The consequences for both the mitochondrion and the cell are dramatic: Misfolded proteins can, for example, disrupt energy production or lead to the formation of larger amounts of reactive oxygen compounds, which attack the mitochondrial DNA and generate further misfolded proteins. In addition, misfolded proteins can destabilize the mitochondrial membranes, releasing signal substances from the mitochondrion that activate apoptosis, the cell's self-destruction program. 

The mitochondrion responds to the stress by producing more chaperones (folding assistants) to fold the proteins in order to reduce the misfolding, as well as protein shredding units that degrade the misfolded proteins. Until now, how cells trigger this protective mechanism was unknown. 

The researchers from Goethe University Frankfurt artificially triggered misfolding stress in the mitochondria of cultured human cells and analyzed the result. “What makes it difficult to unravel such signaling processes," explains Münch, himself a biochemist, “is that an incredibly large number take place simultaneously and at high speed in the cell." The research team therefore availed itself of methods (transcriptome analyses) that can be used to measure over time to what extent genes are transcribed. In addition, the researchers observed, among other things, which proteins bind to each other at which point in time, at which intervals the concentrations of intracellular substances change, and what effects there are when individual proteins are systematically deactivated. 

The result is that the mitochondria send two chemical signals to the cell when protein misfolding stress occurs: They release reactive oxygen compounds and block the import of protein precursors, which are produced in the cell and are only folded into their functional shape inside the mitochondrion, causing these precursors to accumulate in the cell. Among other things, the reactive oxygen compounds lead to chemical changes in a protein called DNAJA1. Normally, DNAJA1 supports a specific chaperone (folding assistant) in the cell, which molds the cell's newly formed proteins into the correct shape. 

As a consequence of the chemical change, DNAJA1 now increasingly forces itself on the folding assistant HSP70 as its helper. HSP70 then takes special care of the misfolded protein precursors that accumulate around the mitochondrion because of the blocked protein import. By doing so, HSP70 reduces its interaction with its regular partner HSF1. HSF1 is now released and can migrate into the cell nucleus, where it can trigger the anti-stress mechanism for the mitochondrion. 

As biochemist Münch explains, “It was very exciting to discover how the two mitochondrial stress signals are combined into one signal in the cell, which then triggers the cell's response to mitochondrial stress. Moreover, in this complex process, which is essentially driven by tiny local changes in concentration, the stress signaling pathways of the cell and the mitochondrion dovetail very elegantly with each other – like the cogs in a clockwork." 

Publication: F. X. Reymond Sutandy, Ines Gößner, Georg Tascher, Christian Münch: A cytosolic surveillance mechanism activates the mitochondrial UPR. Nature (2023) https://doi.org/10.1038/s41586-023-06142-0 

Background information:
Misfolding in mitochondria: Emmy Noether grant of the German Research Foundation for Christian Münch
https://aktuelles.uni-frankfurt.de/english/misfolding-in-mitochondria-how-does-the-cell-react/?highlight=M%C3%BCnch 

The EMTHERA (Emerging Therapies) research cluster is seeking new approaches to study infections and inflammatory diseases as well as immune system disorders and to develop innovative therapies. EMTHERA is an initiative of the Rhine-Main Universities (RMU). https://www.emthera.de/ 

Picture download: http://www.uni-frankfurt.de/93374838 

Caption: Dr. Christian Münch, Institute of Biochemistry II, Goethe University Frankfurt. Photo: Uwe Dettmar for Goethe University 

Further information:
Dr. Christian Münch
Emmy Noether Group Leader – Protein Quality Control & Quantitative Proteomics
Institute of Biochemistry II
Faculty of Medicine
Goethe University Frankfurt
Tel.: +49 (0)69 6301-3715
Web: https://pqc.biochem2.de
Twitter: @MuenchLab @goetheuni


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.