Host glycan recognition by a pore forming toxin.
An exposed F-type lectin domain fused to the N-terminus of a cholesterol-dependent cytolysin scaffold allows Streptococcus mitis lectinolysin to cluster at fucose-rich sites on target cell membranes, thereby leading to increased pore-forming toxin activity. In this issue of Structure, Feil and coworkers define the structural basis for lectinolysin glycan-binding specificity.
Division of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
Samuel
S
Bouyain
Brian V
BV
Geisbrecht
D001426:Bacterial Proteins / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry*; D007983:Lewis Blood Group Antigens / Q000737:chemistry*; D052899:Pore Forming Cytotoxic Proteins / Q000737:chemistry*; D034361:Streptococcus mitis
D001426:Bacterial Proteins; D037102:Lectins; D007983:Lewis Blood Group Antigens; C094162:Lewis Y antigen; D052899:Pore Forming Cytotoxic Proteins