• Coordinating the R&D efforts for antibody-drug conjugates.• Coordinating the protein engineering R&D.• Leading the protein engineering group.

• Corporate Strategy• SBIR/STTR• IP• Business Development• Talent Recruiting

• Leading the development of site-specific antibody-drug conjugates through chemoenzymatic glycoengineering• Leading the glycoengineering of protein therapeutics• Responsible for application and management of SBIR funding, awardee (PI) of 7 SBIR grants, totally $6 million• Managment of technology out-licensing of the company, including successful licensing of GlycoT's technology for Daiichi Sankyo to develop its next generation ADC• Managment of routine R&D operation of the company

• Clycoengineering of protein therapeutics• Development of glycopeptide vaccine for HIV/AIDS

• Developing cutting-edge genetic editing tools• Customized lentiviral packaging, stable cell line generation, and cloning service

• Leading the liver cancer research team in successful development of a series of lentiviral vectors (multiple tumor suppressor/shRNAs/miRNAs at different levels of expression control) for hepatocellular carcinoma treatment; • Leading the HIV project team to develop lentiviral gene therapy based therapeutics (supported by Phase I SBIR Contract funding from NIH) for the treatment of HIV/AIDS; • Leading the Hepatitis C Virus (HCV) project team to develop viral gene therapy based therapeutics (supported by Phase I SBIR Grant funding from NIH) for the treatment of HCV infection;

• Leading the liver cancer research team in successful development of a lentiviral vector (multiple tumor suppressor/shRNAs in single vector) for hepatocellular carcinoma treatment • Developing cancer-specific viral envelope by attaching ScFv towards tumor-specific antigen to viral envelope protein

• Developing lentiviral vector based cancer therapeutics (tumor suppressor gene and shRNAs) • Establishing proof-of-concept of tumor microenvironment-activated fusion protein therapeutics by protein engineering.• Developed protocol for large scale expression of lentiviral vectors

Major contribution: developed a protein vaccine candidate for HIV-1; glycol-engineered erythropoietin (EPO) and antibody Fc domain 1. Glycoengineering of human Erythropoietin (EPO): cloned and expressed both complex glycan and high-mannose type EPO in HEK293T cells, for the first time developed purification protocols for high mannose type EPO (DEAE anion exhange following Ni-NTA affinity chromatography), developed analytic method to analyze its complex N-glycan (both neutral and sialylated), finally performed chemoenzymatic transglycosylation followed by click chemistry to attach alkyne-PEG onto EPO2. Mammalian cell expression and characterization of glycosylated HIV-1 V3 domain fused to Fc domain of human IgG antibody (V3-Fc) as a HIV vaccine candidate: designed, expressed, and purified the fusion protein; engineered its various glycoform with glycosidase inhibitor; developed novel bio-analytic method to characterized its glycoforms; evaluation of its antigenicity (interaction with antibodies by BIAcore analysis) indicates this fusion protein is a valuable vaccine candidate3. Glycoengineering of bacteria oligosaccharide to produce glycoprotein in E.coli: functionally transferred the bacteria N-glycosylation system of C. jejuli into E. coli; expressed and purified the glycoprotein with bacteria N-glycan in E. coli; finally chemoenzymatic engineering of the bacteria oligosaccharide to eukaryotic N-glycan 4. Glycogengineering of human antibody IgG-Fc: expressed and purified IgG-Fc from 293T cells; chemoenzymatic engineering the Fc domain with bisecting N-glycan5. Evaluation of rabbit antisera induced with a synthetic V3-glycopeptide: determine its titer and potency of the sera and purified IgG with

Cancer Immunology

Postdoctoral training in Cancer immunology1. Cell composition analysis of tumor-draining lymph nodes (LN) in human head and neck cancer patients by FACS: discovered altered lymphocytes composition in tumor LN compared to normal LN2. Determine the global methylation level of tumor cell line TC-1 by DNA Microarray analysis of immunoprecipitated methylated-DNAPostdoctoral training in membrane protein structure/function, 1. Construction and experimental validation of a theoretical structural model for OxlT, the oxlalate membrane transporter: successfully developed modeling method for membrane protein; utilized this method to create a high resolution structural model for OxlT, leading to the discovery of second critical residue in substrate-binding site; experimentally validated the discovery with reconstitutional functional assay (this research was published in high-profile journal: PNAS)2. Structural and functional study of UhpT (the uptake hexose transporter in Escherichia. coli) by homology modeling, mutagenesis, thiol cross-linking and reconstitutional functional assay: directed by the structural model, the substrate-binding site composed by two arginine and two tyrosine were successfully identified, one mutant that bears changed substrate selectivity was identified and kinetically validated3. Kinetic study of the membrane transport by GlpT, successfully provided evidence for the proposed rocker-switch mechanism of this protein4. Optimization of purification protocol for UhpT: optimized the protein, lipid and detergent ratio, improve the activity of purified protein• Supervised two rotation graduate students and one junior graduate student• Coordinated the research team of OxlT study