Professor Shie-Liang Edmond Hsieh is a Professor of Institute of Microbiology and Immunology, National Yang-Ming University and jointly appointed Investigator of Genomics Research Center, Academia Sinica and Vaccine Research and Development Center, National Health Research Institutes. He received his MD from School of Medicine, National Yang-Ming University and PhD in 1992 from University of Oxford. He received Johnson & Johnson fellowship and worked with professor Hugh McDevitt in Stanford University before he joined National Yang-Ming University as a faculty in 1994, and was appointed as Directors of Immunology Research Center (2001-president) and Department of Microbiology and Immunology (2005-2007), respectively. His research interests focus on the immunobiology of antigen presenting cells, immunomodulation of dendritic cells and macrophages, and host-pathogen interaction.

　　C-type lectin comprises numerous membranour and soluble proteins which are involved in pathogen-recognition, cell-cell adhesion, migration, and play important roles in innate immunity against various pathogens. In contrast to TOLL-like receptors, which trigger both proinflammatory cytokines and interfersons, downstream signaling of C-type lectins are not involved directly in intefersons secretion. This unique feature raises the possibility to attenuate inflammatory reactions without damping anti-viral immunity.

　　Dengue infections cause r mild inflammatory disease known as dengue fever in most of victims. However, 5~10% patients are suffered from severe symptoms known as dengue hemorrhagic fever. Like other viral hemorrhagic fever, the molecular mechanism is still unknown, neither specific treatment is available.

　　We found that CLEC5A (MDL-1), a C-type lectin-like membrane protein with a natural-killer T-cell C-type lectin domain, associates with a 12 kDa DNAX-activating protein (DAP12) on myeloid cells. We showed that dengue virus (DV) activate CLEC5A and induce DAP12 phosphorylation, thereby trigger downstream signaling cascades and induce proinflammatory cytokine release. Antagonistic anti-CLEC5A mAb protect STAT1-deficient mice from DV-induced subcutaneous hemorrhaging, vascular permeability change, and lethality. Recently, we further find CLEC5A also interacts with Japanese encephalitis virus (JEV) and West Nile Virus (WNV) directly, and anti-CLEC5A mAb suppress proinflammatory cytokine release from JEV- or WNV-infected macrophages. This indicates CLEC5A is a pattern recognition receptor, and anti-CLEC5A mAb is a potential therapeutic agent for patients infected with members of flaviviruses.