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05.03.2025 13:13

Cologne Research Team Identifies a Bacterial Trick for Survival within the Host Cell

Gabriele Meseg-Rutzen Kommunikation und Marketing
Universität zu Köln

    Bacteria produce specific proteins in order to protect themselves against being marked by a cell and then destroyed. A multidisciplinary team in Cologne has now discovered proteins which can provide permanent protection against this marking / publication in Molecular Cell

    Working in collaboration with colleagues at the University of Leiden in the Netherlands, scientists at the University of Cologne’s Institute for Genetics have discovered a strategy in bacteria by which they embed themselves permanently in host cells. The researchers have established that specific intracellular types of living bacteria possess special enzymes which allow them to permanently remove what is referred to as ubiquitin marking. This marking represents a key stage in defence against bacteria. In this process, bacteria are labelled as foreign bodies within cells, thereby signalling their destruction by the cellular recycling system. Under the title ‘A family of bacterial Josephin-like deubiquitinases with an irreversible cleavage mode’, the study conducted by the Cologne research team led by Professor Kay Hofmann has been published in the journal Molecular Cell.

    These bacterial enzymes, referred to as ubiquitin clippases, split the ubiquitin molecule into two parts in such a way that the released fragment is too short to be used again. At the same time, a small fragment remains on the bacterial substrate and thus blocks renewed ubiquitination. This trick allows the bacteria to make themselves at home in the host cell and avoid falling prey to the immune system.

    Working together with the University of Cologne structural biologists led by Professor Ulrich Baumann, the team was able to identify the molecular structures of several bacterial clippases along with a closely related deubiquitinase without clippase properties. The direct comparison of these structures reveals how, in the course of evolution, the cleavage position has been shifted, thus causing the change in activity.

    This discovery not only provides insights into the evolutionary arms race but also has practical applications for research into the human ubiquitin system. Thus, the treatment of cell or tissue samples with clippases allows to identify which proteins were originally modified with ubiquitin.

    Press and Communications Team:
    Dr Anna Euteneuer
    +49 221 470 1700
    a.euteneuer@verw.uni-koeln.de

    Press Spokesperson: Dr Elisabeth Hoffmann – e.hoffmann@verw.uni-koeln.de


    Wissenschaftliche Ansprechpartner:

    Professor Dr Kay Hofmann
    Institute for Genetics
    +49 221 470 1701
    kay.hofmann@uni-koeln.de


    Originalpublikation:

    Publication:
    https://www.cell.com/molecular-cell/fulltext/S1097-2765(25)00107-8


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