Institute of Immunology and Infection ResearchInstitute of Immunology and Infection Research
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Dr. Achim Schnaufer

Location: Room GA.55, Ashworth Laboratories
Telephone:+44 (0131) 650 5548
Email: achim.schnaufer@ed.ac.uk

Web-Site: http://schnauferlab.bio.ed.ac.uk

C.V.

Year Description
1991 - 1992 Diploma student, University of Giessen
1993 - 1997 PhD studentship (Research Assistant), University of Bern
1998 - 2002 Senior Research Fellow, Seattle Biomedical Research Institute (SBRI)
2002 - 2003 Research Associate, SBRI & University of Washington
2003 - 2006 Associate Scientist, SBRI
2007 - 2008 Senior Scientist, SBRI
2008 - Present Research Fellow, University of Edinburgh

Research interests

Our lab aims to understand mitochondrial biogenesis, metabolism and RNA processing in trypanosomatid protozoa, which are important parasites of man and livestock, and to utilize that knowledge to inform drug development.

In particular, our studies are concentrated on the following two areas:

Mitochondrial function in bloodstream stage trypanosomes
This project is aimed at shedding light on the essential - and currently quite elusive - role that the mitochondrion plays in the disease-causing (bloodstream) stage of trypanosomes. It also aims to identify the adaptations that allow so-called dyskinetoplastic trypanosomes to survive the loss of their mitochondrial genome.

Stained mitochondria of insect and bloodstream form Trypanosoma brucei Stained mitochondria of insect (green, on the left) and bloodstream form Trypanosoma brucei (red, on the right).


Evaluation of the trypanosome RNA editing complex as a drug target

RNA editing is an unusual form of post-transcriptional processing of mitochondrial mRNAs in these organisms. It is catalyzed by a macromolecular complex and of vital importance for the parasite. The goal of this project is to assess the potential of its essential components as drug targets. Of particular interest is RNA editing ligase 1 (REL1), the three-dimensional structure of which we recently determined.

Active site of TbREL1 with the ATP co-factor and a modelled inhibitor Active site of TbREL1 with the ATP co-factor (in grey) and a modelled inhibitor (in color) identified by virtual screening in collaboration with Dr. Rommie Amaro (UC San Diego).


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