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New compounds discovered as possible candidates for new antimicrobial drugs against Listeria infection

Hep cells grown without and with 2 pyridones


Scientists at Umeå Centre for Microbial Research (UCMR) have discovered chemical compounds which are able to attenuate the virulence of the bacterial human pathogen Listeria monocytogenes. Their findings are published today in the high impact journal Cell Chemical Biology.

The dramatic increase of antibiotic resistance makes new antimicrobial strategies necessary. The researchers at Umeå University in Sweden are studying an alternative approach, to inhibit the disease capacity (virulence) of bacteria but not their viability. Compared with traditional antibiotics, which often kill the bacteria, the risk of resistance development in disarmed bacteria is lower, since their survival does not depend on resistance against the new drug.

A Listeria infection can be very severe, particularly among patients such as elderly, infants, immunocompromised or pregnant women. Although disease occurrence is relatively low, Listeria’s severe and sometimes fatal health consequences make it among the most serious foodborne infections, with a mortality of 30%. Listeria is found in unpasteurized dairy products and various ready-to-eat foods, and can grow at refrigeration temperatures. In Sweden, 60-90 people per year get infected and the statistics show that the number of outbreaks is increasing.

The study involved several different Umeå University research groups with diverse specialties: Microbiology, Chemistry and Structural Biology. The group of Jörgen Johansson, professor at the laboratory for Molecular Infection Medicine Sweden (MIMS) and the Department of Molecular Biology collaborated with the research groups of Elisabeth Sauer-Eriksson and Fredrik Almqvist, both professors at the Department of Chemistry.

Read more: New compounds discovered as possible candidates for new antimicrobial drugs against Listeria...

MIMS/UCMR Mini-Symposium, 29 May 2018

UCMR DAY 2018Welcome to the 3rd MIMS/UCMR-Mini-Symposium of the year!

29 May 2018, 9:00 - 11:50

Bergasalen, Umeå University Hospital (NUS), South Entrance
In the first session presentations by the Oliver Billker, appointed new Director of MIMS from 1st October, Barbara Sixt, new MIMS Group Leader,  Gemma Atkinson and Linda Sandblad, recipients of UCMR Gender Policy Support. In the second session five Postdoctoral Fellows from the MIMS/UCMR Postdoctoral Programme will present: Christian Pett, Hiraku Takada, Ravendra Nagampalli, Dharmedra Kumar Soni, Rajender Kumar.

Hosts: Bernt Eric Uhlin, Maria Fällman, Elisabeth Sauer-Eriksson, Åke Forsberg

Please register here latest on 27 May:

Contact for questions: Eva-Maria Diehl, This email address is being protected from spambots. You need JavaScript enabled to view it.

NOTE the programme is updated (Christian Pett's presentation has been cancelled)

pdfProgramme for download

Read more: MIMS/UCMR Mini-Symposium, 29 May 2018

MIMS UCMR Mini-Symposium 30 Sept 2013

Place: Betula, building 6M

Welcome to an interesting afternoon! Meet new post-docs and group leaders
The post-docs recruited through the first UCMR_MIMS call and the new MIMS group leaders will present their research. Bernt Eric Uhlin director of MIMS and UCMR will give an update over the newest developments at MIMS.

Read more: MIMS UCMR Mini-Symposium 30 Sept 2013

Make it or break it: how bacteria balance production and degradation of the ‘magic spot’ signaling alarmone

Picture Rel[2020-05-11] When stressed or starved, bacteria regulate their metabolism by producing signalling molecules called alarmones or ‘magic spots’. In the majority of bacteria, the magic spot compounds are both made and destroyed by a large, complex enzyme called Rel. The question of how Rel switches from making the alarmone to degrading it was finally resolved by an international team from Sweden – Vasili Hauryliuk (MIMS & UCMR) – and Belgium: Jelle Hendrix (Hasselt University) and Abel Garcia-Pino (Université Libre de Bruxelles). The results of this study were published in the high impact journal Nature Chemical Biology ("A nucleotide-switch mechanism mediates opposing catalytic activities of Rel enzymes", 11 May 2020).

The team have studied a Rel enzyme from a thermophilic bacterium Thermusthermophilus using a combination of structural (X-ray), biochemical (enzymology) and biophysical (single molecule FRET assays and Isothermal Titration Calorimetry). Since the T.thermophilus has an optimal growth temperature of about 65 °C, by solving the structures at room temperature the researchers could slow down the enzyme enough to ‘catch’ it in the act of synthesising or degrading the alarmone. It turned out that binding of the substrates to the active site region (domain) that is responsible for synthesis of the ‘magic spot’ allosterically inhibits the domain responsible for its degradation – and vice versa, binding of the substrates to the degradation domain inhibits the synthesis  domain. This simple but elegant mechanism ensures that bacteria avoid wasteful production and degradation of the magic spot signalling molecule. Biochemical characterisation of T.thermophilus was performed in Umeå by Dr. Hiraku Takada who is supported by a personal postdoctoral fellowship from the Umeå Centre for Microbial Research (UCMR).

Read more: Make it or break it: how bacteria balance production and degradation of the ‘magic spot’ signaling...

Inauguration of UCEM


Inauguration Umeå Core Facility Electron Microscopy (UCEM) Print E-mail

Welcome to the inauguration of UCEM!  The Umeå Core Facility Electron Microscopy will celebrate the inauguration of a new high resolution field emission SEM equipped with a cryo-stage. The new Field Emission SEM instrument has a unique lens and detector design that opens up new avenues for research in life science, plant biotechnology/wood science, and material science.

23 May 2013, 12:00 - 17:00
Stora hörsalen KB3B1, KBC
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