Investigation of the translocation process of effector proteins from Oomycetes

Investigation of the translocation process of effector proteins from Oomycetes

Biotechnology and Biological Sciences Research Council logo - bioscience for the futurePrincipal Investigator:

Research Co-Investigator:

Research fellow :

  • Dr. Franziska Trusch

The United Nations predict that by 2050 about 9-10 billion people will populate the world. To provide enough food for the growing world population, aquaculture is one area which will be exploited more rigorously in the future but also that losses due to diseases need to be reduced.

S. parasitica cells under microscopeMy project is focussed on the molecular functions of effector proteins, secreted by Saprolegnia parasitica during infection of fish, mainly salmon and trout. S. parasitica is an oomycete, which are fungal-like organisms inhabiting fresh water areas. Research on this pathogen is important since S. parasitica infects several millions of fish causing devastating losses in the aquaculture industry every year. Therefore the overall aim is to understand host pathogen interactions to reduce their heavy impact on food production.

During infection S. parasitica secretes effector proteins, some of which are able to self-translocate into host cells to manipulate the host for a successful infection and propagation. 

Phyre2-Model of a self-translocation domain from an effector proteinThe detailed analysis of the translocation mechanism of those effector molecules is required for the development of drugs to control infection of fish by S. parasitica.

To analyse self-translocation processes of effector proteins we are using a multidisciplinary approach including cell-based assays, molecular biology, proteomics, bioinformatics as well as structural biology.

Individual and overlay of two different fluorescence protein-tagged effector proteins in fish cells


Heterodimers of Tyrosylprotein Sulfotransferases Suggest Existence of a Higher Organization Level of Transferases in the Membrane of the trans-Golgi Apparatus'. Journal of Molecular Biology, vol 427, no. 6 Part B, pp. 1404-1412.

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