Crystal structure of JlpA, a surface-exposed lipoprotein adhesin of Campylobacter jejuni.

ABSTRACT: The Campylobacter jejuni JlpA protein is a surface-exposed lipoprotein that was discovered as an adhesin promoting interaction with host epithelium cells, an early critical step in the pathogenesis of C. jejuni disease. Increasing evidence ascertained that JlpA is antigenic, indicating a role of JlpA in immune response during the infectious process. Here, we report the crystal structure of JlpA at 2.7Å resolution, revealing a catcher's mitt shaped unclosed half β-barrel. Although the apparent architecture of JlpA is somewhat reminiscent of other bacterial lipoproteins such as LolB, the topology of JlpA is unique among the bacterial surface proteins reported to date and therefore JlpA represents a novel bacterial cell surface lipoprotein. The concave face of the structure results in an unus

SUBMITTER: Kawai F 

PROVIDER: S-EPMC3288704 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature