Medical Biochemistry and Biophysics Seminar Series, spring 2012

Jacques Le Pendu, INSERM, Universite de Nantes, Nantes, France

"Adaptation of Caliciviruses to histo-blood group antigens diversity and potential involvement in host-pathogens co-evolution"

Place: KB3A9, Lilla hörsalen, KBC

Host: Thomas Borén

Extra Seminar - Department of Molecular Biology

Thomas Geissman, Bacterial pathogenesis and innate immunity Faculté de Médecine Laennec, Lyon, France

"RNAIII of Staphylococcus aureus and its role in cell wall homeostasis"

Place: room Thymine, Department of Molecular Biology, NUS Area, bldg 6L

Host: Jörgen Johansson

Thesis Defence

Jonas Gripenland, Department of Molecular Biology

"Regulatory roles of two small RNAs in the human pathogen Listeria monocytogenes and Evaluation of an alternative infection model"

Place: Major Groove, bldg. 6L, NUS

Opponent: Thomas Geissmann, Associate Professor, Université de Lyon, Frankrike.

Supervisor: Jörgen Johansson, Department of Molecular Biology

KBC-Seminar

Kazuya Kikuchi, Osaka University, Graduate School of Engineering, WPI-Immunology Frontier Research Center, Osaka, Japan

"Design, synthesis and biological application of in vivo imaging probes with tunable chemical switches"

Place: KB3B1, Stora hörsalen, KBC

Host: Gunnar Öquist, Department of Plant Physiology

Abstract:
One of the great challenges in the post-genome era is to clarify the biological significance of intracellular molecules directly in living cells. If we can image a molecule in action, it is possible to acquire biological information, which is unavailable if we deal with cell homogenates. One possible approach is to design and synthesize chemical probes that can convert biological information to chemical output. Protein fluorescent labeling provides an attractive approach to study the localization and function of proteins in living cells. Recently, a specific pair of a protein tag and its ligand has been utilized to visualize a protein of interest (POI). In this method, a POI is fused with a protein tag and the tag is labeled with the ligand connected to a fluorescent molecule. The advantage of this protein labeling system is that a variety of fluorescent molecules are potentially available as labeling reagents, and that the protein tag is conditionally labeled with its fluorescent ligand. I have designed a protein labeling system that allows fluorophores to be linked to POI. The protein tag (BL-tag) is a mutant class A ?-lactamase (TEM-1) modified to be covalently bound to the designed specific labeling probes and the labeling probes is consisted with a ?-lactam ring (ampicillin, cephalosporin) attached to various fluorophores. A fluorogenetic labeling system can be designed using the unique property of cephalosporin, which release leaving group by subsequent reaction after opening the lactam ring. For further sophisticated application, multicolor imaging was done by adopting the colorful fluorophores.

Umeå Plant Science Centre Seminar

Janne Lehtiö, Karolinska Institute, Stockholm

"Defining human proteome using high resolution peptide isoelectric focusing coupled to mass spectrometry (HiRIEF-LC-MS) and the application of this method to improve cancer treatment "

Place: Lilla hörsalen, KB3A9

Host: Anders Nordström, Department of Molecular Biology