Endosialidase NF Appears To Bind PolySia DP5 in a Helical Conformation

Abstract

Phages infecting the polySia-encapsulated human pathogen E. coli K1 are equipped with capsule-degrading tail spikes known as endosialidases, which are the only identified enzymes that specifically degrade polySia. The X-ray crystallographic structure of endosialidase has been reported but it remains unclear how polySia interacts with the active site. Here we report STD and trNOE NMR experiments that investigate the binding mode of polySia DP5 at a molecular level.