Zhang Y

University of North Carolina at Chapel Hill

OpenAlex Profile
3
Publications
73
h-index
(15,267 citations, 295 total works)

Research Topics

Carbon dioxide utilization in catalysis (39)Crystallization and Solubility Studies (36)X-ray Diffraction in Crystallography (36)Catalysis for Biomass Conversion (34)Asymmetric Hydrogenation and Catalysis (32)

Alpha-gal Syndrome Publications

Alpha-gal-specific human IgE promotes both alpha-gal-induced and antigen-independent allergic effector cell activation.

Wang Y, Zhang Y, Dudley C, Fitzgerald K, Carson AS, et al.
The Journal of allergy and clinical immunology •

In alpha-gal syndrome (AGS), IgE antibodies form against the glycan galactose-α-1,3-galactose (alpha-gal) in mammal products rather than food proteins. Alpha-gal glycolipids and glycoproteins activate human basophils sensitized with AGS plasma in an IgE-dependent fashion. However, it is unknown whether alpha-gal specific IgE (sIgE), independent of other blood proteins, is sufficient for mediating basophil and mast cell activation. We sought to determine whether alpha-gal antigens could activate passively sensitized rat basophilic leukemia (RBL) SX-38 cells, which express human IgE receptors and are commonly used to model allergen/IgE-mediated mast cell activation in food protein allergy. Using the clustered regularly interspaced short palindromic repeats technology, we created a novel, alpha-gal-deficient RBL cell line, alpha-gal knockout RBL SX-38, passively sensitizing cells with sera from AGS donors or with novel alpha-gal sIgE clones, and then stimulated with alpha-gal glycoproteins. To assess effector cell activation, we measured cell surface expression of activation marker CD63 by flow cytometry and mediator release through β-hexosaminidase release assays. After alpha-gal antigen stimulation, the percentage of CD63 alpha-gal knockout RBL SX-38 cells sensitized with AGS sera increased 3-fold compared with cells sensitized with control serum. Select human AGS IgE clones facilitated alpha-gal antigen-dependent and antigen-independent CD63 upregulation. Cells sensitized with pooled AGS sera released β-hexosaminidase in an alpha-gal-independent fashion. We saw no β-hexosaminidase release above background in cells sensitized with alpha-gal sIgE clones. Certain alpha-gal-specific human IgE clones may partially activate allergic effector cells independent of antigen, potentially lowering thresholds for subsequent alpha-gal-induced or antigen-independent allergic effector cell degranulation. This may affect duration and severity of allergic symptoms in patients with AGS.

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Successful administration of cetuximab using dose escalation method: a case report.

Li S, Zhang Y, Zha J, Chen W
Journal of medical case reports •

Cetuximab, used to treat head and neck squamous cell carcinoma and metastatic colorectal cancer, can cause severe infusion reactions. We report an 87-year-old East Asian woman with stage IV ileocecal signet ring cell carcinoma who experienced severe allergic reactions to cetuximab despite pre-treatment. A dose escalation method, involving weekly incremental doses with comprehensive pre-treatment and close monitoring, was employed, successfully reducing allergic reactions and allowing safe administration. This approach demonstrates a viable alternative for patients with hypersensitivity to cetuximab, warranting further research for personalized treatment optimization.

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A glucomannogalactan from Pleurotus geesteranus: Structural characterization, chain conformation and immunological effect.

Liang Z, Yin Z, Liu X, Ma C, Wang J, et al.
Carbohydrate polymers •

A water-soluble glucomannogalactan was isolated from P. geesteranus fruit bodies by hot water extraction and column chromatography method. The structure, chain conformation and immune effect of PGP-1c (20.9 kDa) were investigated comprehensively based on high purity and neutral sugar content (94.7 ± 0.5%). Confirmed by monosaccharide composition, methylation and NMR analysis, PGP-1c was composed of unsubstituted (1,6-α-Gal and 1,6-α-3-OMe-Gal) and monosubstituted (1,2,6-α-Gal and 1,2,6-α-3-OMe-Gal) galactose units in the backbone through α-(1 → 6) glycosidic bonds and the possible branches that a long-branched chain composed of →3)-Glc-(1 → Man and a few fucoses were connected at the O-2 of galactose with a branching degree of 48%. Through the conformational behavior of the molecular chain, it was observed that PGP-1c might have a long-branched or stacked macromolecular network caused by O-CH groups. Moreover, PGP-1c could promote the secretion of NO and cytokines significantly in a dose-dependent manner, which indicated a good immune-enhancing effect.

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