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

E Ficko-Blean (1) , Gerald Hart (2)

1 LBI2M - Laboratoire de Biologie Intégrative des Modèles Marins
2 LBI2M - Laboratoire de Biologie Intégrative des Modèles Marins

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 CRD4, 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 CRD4 to elucidate the molecular mechanisms driving binding specificity. These data contribute to our molecular understanding of Ca2+ ion-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.

Mots clés: Mannose receptor; CRD4; lectin; glycan array; carbohydrate; protein-carbohydrate interactions; affinity; avidity; multivalent binding

Domaines: Sciences du Vivant [q-bio]

E Ficko-Blean, Gerald Hart. A fresh trim provides a new look at the human mannose receptor. Journal of Biological Chemistry, 2021, 297, ⟨10.1016/j.jbc.2021.100922⟩. ⟨hal-03350142v1⟩