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Logo of jbcThe Journal of Biological Chemistry
 
J Biol Chem. 2013 December 27; 288(52): 36772.
PMCID: PMC3873536

Sugar-binding Specificity of the Receptor Langerin Affects Pathogen Entry into the Immune System♦

Common Polymorphisms in Human Langerin Change Specificity for Glycan Ligands

♦ See referenced article, J. Biol. Chem. 2013, 288, 36762–36771

A receptor called langerin lets pathogens enter the immune system as part of the body's adaptive immune response. The receptor, which is found on Langerhans cells, binds sugar molecules on the surfaces of pathogens such as HIV, the measles virus, and some species of yeast. In this Paper of the Week, a team led by Maureen Taylor at Imperial College London looked into how genetic variations in the human langerin gene affected the molecule's ability to bind to sugars. They demonstrated that two common and linked genetic variations altered langerin's sugar-binding specificity. For example, one genetic variation changed lysine to isoleucine in the sugar-binding site. Taylor and colleagues showed that “this amino acid change abolishes binding to oligosaccharides with terminal 6SO4-Gal and enhances binding to oligosaccharides with terminal GlcNAc residues.” The authors concluded that people with different forms of langerin may have different susceptibilities to pathogens.

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Mechanism of 6SO4-Gal binding by langerin. The langerin CRD bound to 6SO4-Galβ1–4GlcNAc. The protein is green, Ca2+ is orange, oxygen atoms are red, nitrogen atoms are blue, and the sulfur atom is gold.


Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology