Postgraduate research opportunities Protein kinases as drug target against the infectious disease Human Leishmaniasis
ApplyKey facts
- Opens: Tuesday 1 February 2022
- Number of places: 3
- Duration: 3 years
Overview
Protein kinases are central regulators in vital processes of the human parasite Leishmania. In this project we want to identify activators of Leishmania protein kinases and their substrates. This will allow to identify specific inhibitors for parasite protein kinases as novel drugs to treat human leishmaniasis.Eligibility
Degree in a biology, medicine or chemistry-related subject.

Project Details
Protein kinases regulate vital processes like differentiation, proliferation, adaptation and motility in all cells. The human parasite Leishmania like other eukaryotes relies on signal transduction via reversible phosphorylation. As such parasite protein kinases are potential drug targets to be used to treat leishmaniasis, a human disease, which dependent on the parasite species and the immunological background of the host can be fatal. The project is comprised of a variety of different methods including CRISPR-Cas9, molecular biology, protein biochemistry, cell biology and screening. Genes will be cloned using modern cloning technologies. Recombinant proteins will be expressed using bacterial expression systems followed by purification and enzyme assays. Interactions of protein kinases with their interaction partners will be analysed in vivo using genetically modified parasites for proximity labelling (BioID) and mass spectrometry.
Further information
Wiese, M.. A mitogen-activated (MAP) protein kinase homologue of Leishmania mexicana is essential for parasite survival in the infected host. EMBO J., 17, 2619-2628 (1998)
Wiese, M. Leishmania MAP kinases – familiar proteins in an unusual context. Internat. J. Parasitol. 37(10), 1053-62 (2007)
John von Freyend S, Rosenqvist H, Fink A, Melzer IM, Clos J, Jensen ON, and Wiese M. LmxMPK4, an essential mitogen-activated protein kinase of Leishmania mexicana is phosphorylated and activated by the STE7-like protein kinase LmxMKK5. Int J Parasitol. 40(8), 969-78 (2010)
Funding details
A bench fee of £12,000 per year is required.
While there is no funding in place for opportunities marked "unfunded", there are lots of different options to help you fund postgraduate research. Visit funding your postgraduate research for links to government grants, research councils funding and more, that could be available.
Supervisors

Dr Martin Wiese
John Anderson Research Senior Lecturer
Strathclyde Institute of Pharmacy and Biomedical Sciences

Apply
Please apply via the PhD Pharmacy & Biomedical Sciences course page.
Number of places: 3
To read how we process personal data, applicants can review our 'Privacy Notice for Student Applicants and Potential Applicants' on our Privacy notices' web page.