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Contact Details

Phone
64 3 479 5290
Email
erwin.lamping@otago.ac.nz
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.

Publications

Krishnan, C., Li, K. C., Lyons, K., Lamping, E., Tompkins, G., & Cannon, R. (2022). Evaluating the suitability of Electrolysed Oxidising Water as a denture disinfectant. New Zealand Dental Journal, 118(4), (pp. 169). [Abstract] Conference Contribution - Published proceedings: Abstract

Alhumaidi, M., Nentwig, L.-M., Rahman, H., Schmitt, L., Rudrow, A., Harris, A., … Lamping, E., … Golin, J. (2022). Residues forming the gating regions of asymmetric multidrug transporter Pdr5 also play roles in conformational switching and protein folding. Journal of Biological Chemistry, 298(12), 102689. doi: 10.1016/j.jbc.2022.102689 Journal - Research Article

James, J. E., Santhanam, J., Cannon, R. D., & Lamping, E. (2022). Voriconazole treatment induces a conserved sterol/pleiotropic drug resistance regulatory network, including an alternative ergosterol biosynthesis pathway, in the clinically important FSSC species, Fusarium keratoplasticum. Journal of Fungi, 8(10), 1070. doi: 10.3390/jof8101070 Journal - Research Article

James, J. E., Santhanam, J., Zakaria, L., Mamat Rusli, N., Abu Bakar, M., Suetrong, S., … Lamping, E., & Cannon, R. D. (2022). Morphology, phenotype, and molecular identification of clinical and environmental Fusarium solani species complex isolates from Malaysia. Journal of Fungi, 8(8), 845. doi: 10.3390/jof8080845 Journal - Research Article

Niimi, M., Niimi, K., Tanabe, K., Cannon, R. D., & Lamping, E. (2022). Inhibitor resistant mutants give important insights into Candida albicans ABC transporter Cdr1 substrate specificity and help elucidate efflux pump inhibition. Antimicrobial Agents & Chemotherapy, 66(1), e01748-21. doi: 10.1128/aac.01748-21 Journal - Research Article

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