Academic Profile

Academic Profile

Assoc Prof Jaume Torres

Associate Professor, School of Biological Sciences

Assoc Prof Jaume Torres

Date of joining NTU: November 2001
Associate Professor
BSc, MSc and PhD, Universitat Autònoma de Barcelona (Catalonia, Spain)
Office: 04s-32
Telephone: 6316 2857

Professional Experience
Postdoctoral. University of Essx, UK
Postdoctoral. University of Cambridge,UK
Research Interests
Our work is focused on structural and functional aspects of membrane proteins, leading to understanding of their function and to development of drugs that will modify their activity.

One type of protein we explore is the aquaporins, the 'water channels' of the cell. Aquaporins selectively transport water and this makes them very useful for biotechnological applications such as water purification. In a medical context, aquaporins are found in most human cells and are involved in a vast array of pathological conditions, but no drugs are available for inhibition or activation. Therefore discovery of aquaporin inhibitors is one of our main interests.

Another system we study are small membrane proteins from enveloped viruses, which tend to oligomerize and form channels of different selectivities. Some examples are M2 from influenza A virus, p7 from hepatitis C virus, SH from respiratory syncytial virus and coronavirus envelope proteins. No structural data exists for the full length version of these proteins despite their small size (typically less than 100 amino acids). Further, their flexibility likely contributes to their multiple reported functions.
Current Projects
  • Biophysical characterization of membrane proteins
  • Can Zika virus helical amphipathic domains in non structural 4A (NS4A) protein mediate membrane binding and aggregation? A potential target for drug screening.
  • Feasibility study to fabricate biomimetic hollow fiber membranes incorporating human aquaporins, bacterial porins and viral ion channels for biotechnological applications.
  • Membrane protein sciences - Tools for rational discovery of novel therapeutics and diagnostics targeting integral membrane proteins
  • Optimisation of a Mimic Transmembrane Peptide Delivery System, Consisting of a Chimeric Bacterial-Hairpin-Like Construct, for Specific Labelling of Membrane Proteins. In Vitro & in Vivo Appln to Structure & Function of the SARS CoV E Protein
  • Rapid selection of functional stabilized mutants of water channel aquaporins: Applications to water purification and drug discovery
  • Scale-up the Fabrication of High Performance Aquaporin (AQP)-based Biomimetic Flat-Sheet Membranes for Seawater Desalination
  • Scale-up the Fabrication of High Performance Aquaporin (AQP)-based Biomimetic Hollow Fiber Membranes for Water Reuse and Desalination
  • Structural-activity relationships of envelope proteins in coronaviruses : Structural determination and specific contributions of protein domains to channel activity and membrane fusion during the virus life cycle
  • Synthesis, structure and inhibition of p7, a viroporin found in the hepatitis C virus.
Selected Publications
  • Li, Y., Surya, W., Claudine, S., and Torres, J. (2014). Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins. Journal of Biological Chemistry, 289(18), 12535-12549.
  • Nieto-Torres, J.L., DeDiego, M.L., Verdiá-Báguena, C., Jimenez-Guardeño, J.M., Regla-Nava, J.A., Fernandez-Delgado, R., Castaño-Rodriguez, C., Alcaraz, A., Torres, J. Aguilella, V., Enjuanes, L. (2014). Severe acute respiratory syndrome coronavirus envelope protein ion channel activity promotes virus fitness and pathogenesis. PLoS Pathogens, , (in press).
  • Gan, S.W., Surya, W., Vararattanavech, A., and Torres, J. (2014). Two different conformations in hepatitis C virus p7 protein account for proton transport and dye release. PLoS ONE, 9(1), e78494. doi:10.1371/journal.pone.0078494.
  • Gan, S.W., Tan, E., Lin, X., Yu, D., Wang, J., Tan, G., Vararattanavech, A., Yeo, C.Y., Soon, C.H., Soong, T.W., Pervushin, K., and Torres, J. (2012). The small hydrophobic protein of the human respiratory syncytial virus forms pentameric ion channels. Journal of Biological Chemistry, 287, 24671-24689.
  • Pervushin, K., Tan, E., Parthasarathy, K., Lin, X., Jiang, F.L., Yu,, D., Vararatannavech, A., Soong, T.W., Liu, D.X., and Torres, J. (2009). Structure and inhibition of the SARS Coronavirus Envelope Protein Ion Channel. PLoS Pathogens, 5(7), e1000511.

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