Molecular Interactions Of Tectonin Proteins In Host and Pathogen Recognition

Abstract

Beta-propeller proteins exhibit diverse functions in catalysis, protein-protein interaction, cell-cycle regulation, and immunity. Tectonins, a sub-class of beta-propeller family, have been implicated in bacterial binding. Our prediction revealed that the galactose-binding protein (GBP) in the horseshoe crab, Carcinoscorpius rotundicauda, is an all-beta sheet protein consisting of Tectonin domains. Studies have shown that upon binding to Gram-negative bacterial lipopolysaccharide (LPS), GBP interacts with C-reactive protein (CRP) and carcinolectin (CL5) to form a pathogen recognition complex. However, the molecular basis of interactions between GBP and LPS and how it interplays with CRP remains largely unknown. Here, we sought to unravel the mechanisms of interaction by examining the structure-function relationship, with a view to understanding the pathophysiological implications of the Tectonin domain-containing proteins and the possible conservation of this concept in the mammalian system.