A fresh trim provides a new look at the human mannose receptor

J Biol Chem. 2021 Jul;297(1):100922. doi: 10.1016/j.jbc.2021.100922. Epub 2021 Jun 26.

Abstract

The human mannose receptor plays an important role in scavenging a variety of glycans and glycoconjugates, which contributes to both innate and adaptive immunity. However, the fine details of its ligand specificity, and specifically that of carbohydrate-recognition domain 4, the most functionally relevant C-type lectin domain within the receptor, are not completely understood. Feinberg et al. use glycan arrays, crystallography, and a newly trimmed version of carbohydrate-recognition domain 4 to elucidate the molecular mechanisms driving binding specificity. These data contribute to our molecular understanding of Ca2+-mediated binding promiscuity in the human mannose receptor and the scavenging role of the receptor itself and highlight unexpected interactions that should inspire further study.

Keywords: CRD4; affinity; avidity; carbohydrate; glycan array; lectin; mannose receptor; multivalent binding; protein–carbohydrate interactions.

Publication types

  • Comment

MeSH terms

  • Adaptive Immunity
  • Crystallography
  • Humans
  • Lectins, C-Type*
  • Mannose Receptor
  • Mannose-Binding Lectins
  • Receptors, Cell Surface*

Substances

  • Lectins, C-Type
  • Mannose Receptor
  • Mannose-Binding Lectins
  • Receptors, Cell Surface