The structure of a giant adhesin that binds its Antarctic bacterium Marinomonas primoryensis to ice has been fully mapped in a large collaboration project between researchers from Eindhoven University of Technology, Queen’s University (Kingston, ON, Canada) and the Hebrew University of Jeruzalem (Rehovot, Israel). The 1.5 MDa protein comprises of over 130 domains and contains protein, sugar and most notably ice binding sites, used in combination to bind the bacteria to each other, ice surfaces and diatoms in the cold waters of an Antarctic lake. The entire story concerning this intriguing discovery can be read in Science Advances.
