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Zhang S , Moussodia RO , Vertesy S , Andre S , Klein ML , Gabius HJ , Percec V
Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface
Proc Natl Acad Sci U S A. 2015 May 5;112(18) :5585-90
PMID: 25902539    PMCID: PMC4426414   
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Abstract
Surface-presented glycans (complex carbohydrates) are docking sites for adhesion/growth-regulatory galectins within cell-cell/matrix interactions. Alteration of the linker length in human galectin-8 and single-site mutation (F19Y) are used herein to illustrate the potential of glycodendrimersomes with programmable glycan displays as a model system to reveal the functional impact of natural sequence variations in trans recognition. Extension of the linker length slightly reduces lectin capacity as agglutinin and slows down aggregate formation at low ligand surface density. The mutant protein is considerably less active as agglutinin and less sensitive to low-level ligand presentation. The present results suggest that mimicking glycan complexity and microdomain occurrence on the glycodendrimersome surface can provide key insights into mechanisms to accomplish natural selectivity and specificity of lectins in structural and topological terms.
Notes
Zhang, Shaodong Moussodia, Ralph-Olivier Vertesy, Sabine Andre, Sabine Klein, Michael L Gabius, Hans-Joachim Percec, Virgil Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. United States Proc Natl Acad Sci U S A. 2015 May 5;112(18):5585-90. doi: 10.1073/pnas.1506220112. Epub 2015 Apr 20.