Bacterial protein domains with a novel Ig-like fold bind human CEACAM receptors

ABSTRACT: Streptococcus agalactiae, also known as group B Streptococcus (GBS), is the major cause of neonatal sepsis in humans. A critical step to infection is adhesion of bacteria to mucosal surfaces. GBS adhesins have been identified to bind extracellular matrix components and cellular receptors. However, several putative adhesins have no host binding partner characterized. We report here that surface-expressed B protein of GBS binds to human CEACAM1 and CEACAM5 receptors. A crystal structure of the complex showed that an IgSF domain in ? represents a novel Ig-fold subtype called IgI3, in which unique features allow binding to CEACAM1. Bioinformatic assessment revealed that this newly identified IgI3 fold is not exclusively present in GBS but is predicted to be present in adhesins from other clini

SUBMITTER: Dr. Nina, S van Sorge 

PROVIDER: S-SCDT-EMBOJ-2020-106103 | biostudies-other |

REPOSITORIES: biostudies-other