A5101531425- Glycosylation and Glycoproteins Research
- Carbohydrate Chemistry and Synthesis
- Monoclonal and Polyclonal Antibodies Research
- Mast cells and histamine
- Allergic Rhinitis and Sensitization
- Food Allergy and Anaphylaxis Research
- Proteoglycans and glycosaminoglycans research
- Immunotherapy and Immune Responses
- HIV Research and Treatment
- Eosinophilic Esophagitis
- Immune Cell Function and Interaction
- Hepatitis B Virus Studies
- Cancer Immunotherapy and Biomarkers
- Eosinophilic Disorders and Syndromes
- Sinusitis and nasal conditions
- Hepatocellular Carcinoma Treatment and Prognosis
- Asthma and respiratory diseases
- T-cell and B-cell Immunology
- Natural product bioactivities and synthesis
- Cell Adhesion Molecules Research
- Biofuel production and bioconversion
- Polysaccharides and Plant Cell Walls
- IL-33, ST2, and ILC Pathways
- Interstitial Lung Diseases and Idiopathic Pulmonary Fibrosis
Yale University
2018-2021
Johns Hopkins Medicine
2015-2021
Johns Hopkins University
2015-2021
University of Maryland, Baltimore
2008-2010
Siglecs are transmembrane sialoglycan binding proteins, most of which expressed on leukocyte subsets and have inhibitory motifs that translate cell surface ligation into immune suppression. In humans, Siglec-8 eosinophils, mast cells basophils Siglec-9 neutrophils, monocytes some T-cells, mediate death, inhibition mediator release and/or enhancement anti-inflammatory release. Endogenous ligands in tissues, mostly uncharacterized, engage siglecs leukocytes to inhibit inflammation. Glycan...
Sialic acid-binding Ig-like lectin 8 (Siglec-8) is expressed on the surface of human eosinophils, mast cells, and basophils-cells that participate in allergic other diseases. Ligation Siglec-8 by specific glycan ligands or antibodies triggers eosinophil death inhibits cell degranulation; consequences could be leveraged as treatment. However, not murine most species, thus limiting preclinical studies vivo. Based a ROSA26 knock-in vector, construct was generated contains CAG promoter,...
Abstract Siglec-8 is an inhibitory receptor expressed on eosinophils and mast cells. In this study, we took advantage of a novel transgenic mouse model to assess the impact modulating IgE-dependent cell degranulation anaphylaxis using liposomal platform display allergen with or without synthetic glycan ligand for (Sig8L). The hypothesis that recruitment IgE–FcεRI complex will inhibit allergen-induced degranulation. Codisplay both Sig8L liposomes profoundly suppresses IgE-mediated bone...
The presence and precise structures of the glycans attached at Fc domain monoclonal antibodies play an important role in determining antibodies' effector functions such as antibody-dependent cell cytotoxicity (ADCC), complement activation, anti-inflammatory activity. This paper describes a novel approach for glycoengineering human IgG1-Fc that combines high-yield expression yeast subsequent vitro enzymatic glycosylation, using endoglycosidase-catalyzed transglycosylation key reaction. Human...
Human siglecs are a family of 14 sialic acid-binding proteins, most which expressed on subsets immune cells where they regulate responses. Siglec-8 is selectively human allergic inflammatory cells-primarily eosinophils and mast cells-where engagement causes eosinophil apoptosis inhibits cell mediator release. Evidence supports model in bind to sialoglycan ligands target tissues resolve inflammation limit tissue damage. To identify Siglec-8-binding sialoglycans from airways, proteins...
The Siglec family of cell surface receptors have emerged as attractive targets for cell-directed therapies due to their restricted expression on immune cells, endocytic properties, and ability modulate receptor signaling. Human Siglec-8, instance, has been identified a therapeutic target the treatment eosinophil mast disorders. A promising strategy Siglecs involves use liposomal nanoparticles with multivalent display ligands. key challenge this approach is identification high affinity ligand...
Abstract Sialic acid-binding immunoglobulin-like lectin (Siglec)-8 is a human cell surface protein expressed exclusively on eosinophils, mast cells, and basophils that, when engaged, induces eosinophil apoptosis inhibits mediator release. This makes Siglec-8 promising therapeutic target to treat diseases involving these types. However, preclinical studies of targeting in vivo are lacking because this only found humans, apes, some monkeys. Therefore, we have developed mouse strain which...
The third variable (V3) domain of HIV-1 gp120 envelope glycoprotein is critical for entry and represents an attractive target vaccine design. There are three conserved N-glycans within or around the V3 loop. N295 N332 glycans at base usually characterized as high-mannose type in gp120, N301 glycan a complex type. We report this paper expression characterization glycosylated, full-size derived from HIV-1Bal strain IgG1-Fc fusion protein, including its binding to two broadly HIV-neutralizing...
Abstract Src homology 2 domain–containing inositol 5-phosphatase 1 (SHIP-1) regulates the intracellular levels of phosphotidylinositol-3, 4, 5-trisphosphate, a phosphoinositide 3–kinase (PI3K) product. Emerging evidence suggests that PI3K pathway is involved in allergic inflammation lung. Germline or induced whole-body deletion SHIP-1 mice led to spontaneous type 2-dominated pulmonary inflammation, demonstrating essential for lung homeostasis. However, mechanisms by which and responsible...