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
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
Journal title :
Journal of Molecular Biology