期刊
EMBO JOURNAL
卷 23, 期 6, 页码 1245-1256出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.emboj.7600142
关键词
adhesion; autotransporter; crystal structure; homotrimer; microbial pathogenesis
资金
- NHLBI NIH HHS [T32 HL007873, T32-HL07873] Funding Source: Medline
- NIAID NIH HHS [R01-AI49950, R01 AI049950, R01-AI44167, R01 AI044167] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
Haemophilus influenzae is an important human pathogen that initiates infection by colonizing the upper respiratory tract. The H. influenzae Hia autotransporter is an adhesive protein that promotes adherence to respiratory epithelial cells. Hia adhesive activity resides in two homologous binding domains, called HiaBD1 and HiaBD2. These domains interact with the same host cell receptor, but bind with different affinities. In this report, we describe the crystal structure of the high-affinity HiaBD1 binding domain, which has a novel trimeric architecture with three-fold symmetry and a mushroom shape. The subunit constituents of the trimer are extensively intertwined. The receptor-binding pocket is formed by an acidic patch that is present on all three faces of the trimer, providing potential for a multivalent interaction with the host cell surface, analogous to observations with the trimeric tumor necrosis factor superfamily of proteins. Hia is a novel example of a bacterial trimeric adhesin and may be the prototype member of a large family of bacterial virulence proteins with a similar architecture.
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