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

• Published in: Journal of structural biology Vol. 177; no. 2; pp. 583 - 588
• Main Authors: Kawai, Fumihiro, Paek, Seonghee, Choi, Kyoung-Jae, Prouty, Michael, Kanipes, Margaret I., Guerry, Patricia, Yeo, Hye-Jeong
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.02.2012
• Subjects: Adhesins, Bacterial - chemistry; Amino Acid Sequence; Bacterial lipoprotein; Campylobacter jejuni; Conserved Sequence; Crystal structure; Crystallography, X-Ray; Glycosylation; JlpA; Lipoproteins - chemistry; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Protein Structure, Tertiary; Structural Homology, Protein; Surface Properties; JlpA; Bacterial lipoprotein; Crystal structure; Campylobacter jejuni
• ISSN: 1047-8477; 1095-8657
• DOI: 10.1016/j.jsb.2012.01.001

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 unusually large hydrophobic basin with a localized acidic pocket, suggesting a possibility that JlpA may accommodate multiple ligands. Therefore, the structure provides framework for determining the molecular function of JlpA and new strategies for the rational design of small molecule inhibitors efficiently targeting JlpA.