• Title of article

    Brucella Immunogenic BP26 Forms a Channel-like Structure

  • Author/Authors

    Daegeun Kim، نويسنده , , Jihye Park، نويسنده , , Soo Jin Kim، نويسنده , , Young-Min Soh، نويسنده , , Ho Min Kim، نويسنده , , Byung-Ha Oh، نويسنده , , Ji-Joon Song، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2013
  • Pages
    8
  • From page
    1119
  • To page
    1126
  • Abstract
    An outer membrane protein BP26/OMP28 of Brucella, BP26, is identified as a major immunodominant antigen and widely used as a diagnostic marker and for vaccination against Brucellosis. BP26 belongs to the family of proteins that contains a SIMPL (signaling molecule that associates with the mouse pelle-like kinase) domain, whose structure and function have been unknown. Here, we present the crystal structure of BP26 revealing that 16 BP26 molecules form a novel channel-like assembly as also shown by electron microscopy analysis. Eight BP26 molecules forming a ring structure contain a hole at the center of the octamer, and another octamer interacts with each other to form a channel having a large internal cavity. BP26 is found to be structurally similar to a bacteriophage protein involved in infection, implicating that BP26 might function during Brucella infection. In addition, the BP26 structure suggests that the protein functions as a multimeric channel-like form and provides a canonical model for the SIMPL domains.
  • Keywords
    Infection , pilus-binding domain , SIMPL domain , Brucella abortus , multimerization
  • Journal title
    Journal of Molecular Biology
  • Serial Year
    2013
  • Journal title
    Journal of Molecular Biology
  • Record number

    1255220