Contact Details
- Phone
- 64 3 479 5290
- erwin.lamping@otago.ac.nz
University Links
- Position
- Senior Research Fellow
- Department
- Department of Oral Sciences
- Qualifications
- PhD
- Research summary
- Membrane protein biology
- Teaching
Dr Lamping supervises undergraduate and postgraduate students, and enjoys sharing his skills and experience with like-minded individuals.
- Memberships
- Member of the American Society for Microbiology, the New Zealand Microbiological Society, the New Zealand Society for Biochemistry and Molecular Biology, as well as member of the Oral Microbiology and Dental Health Research Theme and the Webster Centre for Infectious Diseases of the University of Otago.
Research
Experienced in molecular biology with expertise in biochemistry, yeast genetics, and molecular biology, Dr Lamping is particularly interested in studying the structure and function of eukaryotic membrane proteins—especially integral membrane proteins associated with multidrug resistance of fungal pathogens and human cancer cells. The list of membrane proteins includes:
- The azole antifungal drug target ERG11, an essential enzyme of ergosterol biosynthesis
- Multidrug efflux pumps of the pleiotropic drug resistance (PDR) and the multidrug resistance (MDR) family of efflux transporters
A significant part of his studies are dedicated to the continuous improvement of the basic molecular biology toolkit that enables scientists to ever more efficiently, precisely, and predictably express heterologous membrane proteins in the eukaryotic model organism Saccharomyces cerevisiae.
In the past decade he helped create and optimise a patented yeast membrane protein expression system used worldwide by over 50 research teams. Dr Lamping used that patented technology to create a suit of yeast strains overexpressing the azole drug target ERG11, as well as many PDR and MDR efflux transporters from human and important fungal pathogens: Candida albicans, C. glabrata, C. krusei, Cryptococcus neoformans, and Aspergillus fumigatus.
These strains have been used successfully for many different research applications funded by national (Marsden, HRC, and FRST), and international funding agencies (NIH, USA; Japan Health Sciences Foundation; and Japan Society for the Promotion of Sciences), and they helped solve the first crystal structure for any full-length cytochrome P450 enzyme, S. cerevisiae Erg11p.