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Chiguang Feng, PhD

Academic Title:

Assistant Professor

Primary Appointment:

Microbiology and Immunology

Location:

HSF II S314

Phone (Primary):

410-234-8827

Phone (Secondary):

410-706-5099

Fax:

410-706-6205

Education and Training

  • University of Science and Technology of China, BS, Cellular Biology, 1991
  • Ehime University School of Medicine, Japan, PhD, Immunology, 1999
  • National Institutes of Health, Fellow, Immunology, Cancer Therapy, 2004
  • University of Maryland School of Medicine, Fellow, Vaccine Development, 2008

Biosketch

Dr. Feng 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. He served as Research Associate since 2008 and recently was promoted to Assistant Professor. His research interest is the regulation of immune responses such as 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.

Research/Clinical Keywords

immune responses, host-pathogen interaction, glycobiology, neuraminidase/sialidase, galectins, vaccine development

Highlighted Publications

Feng C,  Li J, Snyder G,  Huang W, Goldblumd SE, Chen WH, Wang L, McClane BA,  Cross AS. Antibody against Microbial Neuraminidases Recognizes Human Sialidase 3 (NEU3): the Neuraminidase/Sialidase Superfamily Revisited. MBio. 2017 Jun 27;8(3). pii: e00078-17. doi: 10.1128/mBio.00078-17. PMID: 28655817

Vasta GR, Feng C, González-Montalbán N, Mancini J, Yang L, Abernathy K, Frost G, Palm C. Functions of Galectins as "Self/Non-Self" Recognition and Effector Factors. Pathog Dis. 2017 Jul 31;75(5). doi: 10.1093/femspd/ftx046. PMID: 28449072

Feng C, et al. Manipulating Galectin Expression in Zebrafish (Danio rerio). Methods Mol Biol. 2015;1207:327-41. doi: 10.1007/978-1-4939-1396-1_22. PMID: 25253151

Feng C, Ghosh A, Amin MN, Giomarelli B, Shridhar S, et al. The Galectin CvGal1 from the Eastern Oyster (Crassostrea virginica) Binds to Blood Group A Oligosaccharides on the Hemocyte Surface.J Biol Chem. 2013 Aug 23; 288(34): 24394-409.

Feng C, Zhang L, Nguyen C, Vogel S, Goldblum S, Blackwelder WC, Cross AS. Neuraminidase reprograms lung tissue and potentiates LPS-induced acute lung injury in mice. J. Immunol. 2013 Nov 1:191(9):4828-37. doi: 10.4049/jimmunol.1202673.

Complete

https://www.ncbi.nlm.nih.gov/sites/myncbi/chiguang.feng.1/bibliography/48029425/public/?sort=date&direction=ascending