Lectins articles from across Nature Portfolio

ERGIC-53 engages in the ER-to-Golgi transport of secretory and membrane proteins by unknown mechanisms. Here authors report a long flexible tetrameric structure of full-length ERGIC-53 complexed with its functional partner MCFD2 by cryo-EM.

A metagenomic phage display library from healthy human fecal samples with carbohydrate binding screens identifies protein sequences of novel carbohydrate binding domains and their folds with AlphaFold2 predictions.

Antimicrobial protein REG3A improved insulin sensitivity by combating oxidative stress and activating AMPK in skeletal muscle in HFD-induced obese mice overexpressing human REG3A in the liver.

Streptococcal siglec-like binding regions (SLBRs) selectively bind cell surface glycans, but the basis for this selectivity is not understood. Here, the authors identify selectivity-modulating SLBR regions and study how changes in SLBR glycan selectivity affect interactions with human glycoprotein receptors.

Trefoil factors (TFFs) protect the mucosa and have various reported binding activities, but whether they share a common interaction mechanism has remained unclear. Here, the authors provide structural and biochemical evidence that all three human TFFs are divalent lectins that recognise the same disaccharide.

A cluster of three rice lectin receptor kinases confers resistance to planthopper insects.

Galectins are carbohydrate-binding proteins with diverse activities, but there is no unifying picture of their primary physiological role. Galectins now emerge as autonomous bacteria-killing agents (pages 295–301), unexpected findings that may point to a principal role of these proteins in innate immunity.