Galectins - newly identified danger receptors for invading bacteria
March, 2012
Damaged or unwanted cellular components are normally broken down into basic molecules within the lysosomes of cells for recycling. This process, known as 'autophagy', has many functions, one of which is to rid cells of bacterial infection. The efficient uptake of pathogens is mediated by unidentified recognition factors that help to identify bacteria for destruction.
Galectins are carbohydrate-binding proteins that normally have a role in binding extracellular glycans. They accumulate in the cell cytosol (normally devoid of complex carbohydrates) before being secreted. Thurston et al demonstrate that galectins within the cytosol may have a role in the detection and autophagy of vesicle-damaging pathogens. They show that galectin 8, in particular, has a versatile role in monitoring endosomal and lysosomal integrity. Rupture of bacteria containing vesicles exposes the cytosol to host glycans and microbe-derived carbohydrates, either of which may cause galactin-8 accumulation. Galectin 8 restricts bacterial proliferation by binding host glycans on damaged bacteria-containing vacuoles and activating autophagy through the recruitment of NDP52. The authors suggest that galectin 8 is a versatile danger receptor for combatting bacterial infection. Live imaging was performed on a Nikon Eclipse Ti inverted microscope equipped with an Andor Revolution XD system and a Yokogawa CSU-X1 spinning disk unit.