8/13/2023 0 Comments Cobalt 60 capsuleb, Genetic organization of region 2 of the capsule gene cluster of Hib. Supported by biochemical studies and comprehensive 2D nuclear magnetic resonance, our data explain how the ribofuranosyltransferase CriT, the phosphatase CrpP, the ribitol-phosphate transferase CroT and a polymer-binding domain function as a unique multi-enzyme assembly.Ī, Chemical structure and schematic representation of the Hib capsule polymer repeating unit. This architecture is commonly exploited for surface glycan synthesis by both Gram-negative and Gram-positive pathogens. The X-ray crystal structure of the capsule polymerase Bcs3 reveals a multi-enzyme machine adopting a basket-like shape that creates a protected environment for the synthesis of the complex Hib polymer. ![]() Reconstitution of this pathway enabled the fermentation-free production of Hib vaccine antigens starting from widely available precursors and detailed characterization of the enzymatic machinery. Here we define the capsule biosynthesis pathway of Haemophilus influenzae serotype b (Hib), a Gram-negative bacterium that causes severe infections in infants and children. They provide a protective envelope against host recognition, leading to immune evasion and bacterial survival. Timm Fiebig ORCID: /0000-0002-2021-7296 3īacterial capsules have critical roles in host-pathogen interactions.A multi-enzyme machine polymerizes the Haemophilus influenzae type b capsule
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