ArticlePloS one2009
A possible role for metallic ions in the carbohydrate cluster recognition displayed by a Lewis Y specific antibody.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 18 citations in OpenAlex.
- Targeting the "Sweet Side" of Tumor with Glycan-Binding Molecules Conjugated-Nanoparticles: Implications in Cancer Therapy and Diagnosis.Nanomaterials (Basel, Switzerland) · 2021Review
- Altered glycosylation in cancer: A promising target for biomarkers and therapeutics.Biochimica et biophysica acta. Reviews on cancer · 2021Review
- Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysin reveals the basis for its lewis antigen specificity.Structure (London, England : 1993) · 2012Article
- Structural basis for Fc gammaRIIa recognition of human IgG and formation of inflammatory signaling complexes.Journal of immunology (Baltimore, Md. : 1950) · 2011Article
- A computational approach for exploring carbohydrate recognition by lectins in innate immunity.Frontiers in immunology · 2011Article
- Carbohydrates contribute to the interactions between cockroach allergen Bla g 2 and a monoclonal antibody.Journal of immunology (Baltimore, Md. : 1950) · 2011Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLewis Y (Le(y)) is a blood group-related carbohydrate that is expressed at high surface densities on the majority of epithelial carcinomas and is a promising target for antibody-based immunotherapy. A humanized Le(y)-specific antibody (hu3S193) has shown encouraging safety, pharmacokinetic and tumor-targeting properties in recently completed Phase I clinical trials. METHODOLOGY/PRINCIPAL
findingsWe report the three-dimensional structures for both the free (unliganded) and bound (Le(y) tetrasaccharide) hu3S193 Fab from the same crystal grown in the presence of divalent zinc ions. There is no evidence of significant conformational changes occurring in either the Le(y) carbohydrate antigen or the hu3S193 binding site, which suggests a rigid fit binding mechanism. In the crystal, the hu3S193 Fab molecules are coordinated at their protein-protein interface by two zinc ions and in solution aggregation of Fab can be initiated by zinc, but not magnesium ions. Dynamic light scattering revealed that zinc ions could initiate a sharp transition from hu3S193 Fab monomers to large multimeric aggregates in solution. CONCLUSIONS/SIGNIFICANCE: Zinc ions can mediate interactions between hu3S193 Fab in crystals and in solution. Whether metallic ion mediated aggregation of antibody occurs in vivo is not known, but the present results suggest that similar clustering mechanisms could occur when hu3S193 binds to Le(y) on cells, particularly given the high surface densities of antigen on the target tumor cells.
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