Article ID Journal Published Year Pages File Type
2184821 Journal of Molecular Biology 2013 8 Pages PDF
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.

Graphical AbstractFigure optionsDownload full-size imageDownload high-quality image (415 K)Download as PowerPoint slideHighlights► Crystal structure of an immunogenic protein BP26 from Brucella abortus. ► BP26 forms a homo-hexadecamer with an internal channel. ► The structure of BP26 represents the first structure of the SIMPL domains.

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Life Sciences Biochemistry, Genetics and Molecular Biology Cell Biology
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