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Using a chimera to study the role of Galectin‐1 in immunological responses and tumor progression (LB91)
Author(s) -
Bradford Nora,
Jin Cho Yong,
Bailey Lily,
Gustafson Jack,
Huang Tianyi,
Iyer Hansika,
Lu Hancheng,
MagliochettiCammarata Tessabella,
Nee William,
Park Jasmin,
Park Jin Young,
Sherrin McLean,
Sugarman Eli,
Tejeda Jeanny,
Zhan Bowen,
Rokous Judy,
Dimitroff Charles
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.lb91
Subject(s) - galectin , glycoconjugate , chemistry , chimera (genetics) , immune system , microbiology and biotechnology , lectin , galactose , biochemistry , biology , immunology , gene
Galectin‐1 (Gal‐1), a protein that impacts the fate and function of immune cells known to fight infection, eliminates cancer, and promotes inflammation, is found in most mammalian tissues at low levels. A small 130 amino acid “jelly‐roll” shaped ß‐galactoside‐binding lectin with a hydrophobic core, Gal‐1 plays a role in controlling intracellular processes, such as cell cycle progression and cell proliferation. Gal‐1 binds with high affinity to glycoconjugates galactose (Gal) and N‐acetylglucosamine (GlcNAc) by van der Waals forces and hydrogen bonding via a highly conserved carbohydrate recognition domain. Because native Gal‐1 oxidizes rapidly and loses its carbohydrate‐binding activity, studying the effect of Gal‐1 has been difficult. The Dimitroff laboratory engineered a Gal‐1 – human immunoglobulin Fc chimeric molecule (Gal‐1hFc), which facilitates dimerization while preventing oxidation‐induced multimerization. Experimental evidence has demonstrated that Gal‐1hFc behaves like native Gal‐1, enabling the use of the chimera to study Gal‐1’s effect on immune responses. The Governor’s Academy SMART (Students Modeling A Research Topic) Team designed a model using 3D printing technology to provide further evidence of Gal‐1hFc’s structure and binding function.Grant Funding Source : Supported by grants from NIH‐CTSA UL1RR031973 and NIH/NCI RO1CA118124