Chiguang Feng is an Assistant Professor at the Department of Microbiology and Immunology, University of Maryland School of Medicine. He graduated from the University of Science and Technology of China with a major in cellular biology, and obtained his PhD from the Ehime University School of Medicine in Japan. He received postdoctoral training in immunology and cancer immunotherapy at the National Institutes of Health, and vaccine development at the University of Maryland School of Medicine.

Dr. Feng’s research interest is the regulation of immune responses including T cell differentiation and activation, mucosal immunity and vaccine development. He currently focuses on the roles of desialylation (by endogenous/exogenous neuraminidase) in host-pathogen interactions as well as host innate and adaptive immune responses. Protein glycosylation is an important post-transcriptional modification process that increases a protein’s structural and functional complexity by attaching different sugar groups onto the peptide chains, including the terminal sialyl residuals. Dr. Feng’s studies demonstrate that 1) removal of the terminal sialyl residuals (desialylation) enhances ligand-receptor interaction, such as integrin/ICAM-1 binding, and downstream signaling, such as LPS mediated TLR4/ NFκB activation and cytokine production; 2) the expression of sialidases (which desialyate glycans) mediates the desialylation and activation of EGFR and MUC1 that affects bacterial adhesion onto human epithelia, and modulates endothelial wound healing in lung microvascular endothelia; and 3) galectin (also known as S-lectin, a family of lectins which bind beta-galactoside) mediates or regulates the host-pathogen interaction in murine influenza infection and Oyster-Perkinsus systems. Therefore, desialylation of key cell surface receptors is an important regulatory mechanism in immune responses. Dr. Feng’s continuing work aims to decipher the mechanisms involving the multiple interactions of sialic acids, sialidases, and galectins in host-pathogen interactions and immune responses. The new knowledge derived from these studies has the potential to broaden the spectrum of glycan targets for developing novel therapeutic agents and vaccines against clinically important diseases.