Repetitive Architecture of the Haemophilus influenzae Hia Trimeric Autotransporter
2008
Structure of the Hia Trimeric Autotransporter
publication
Evidence: high
Author Information
Author(s): Meng Guoyu, St. Geme Joseph W. III, Waksman Gabriel
Primary Institution: Institute of Structural and Molecular Biology at UCL/Birkbeck
Hypothesis
The study investigates the structural characteristics of the Hia autotransporter and its adhesive function.
Conclusion
The study reveals that the Hia autotransporter has a modular architecture with distinct structural domains that are crucial for its adhesive activity.
Supporting Evidence
- The Hia autotransporter is essential for bacterial adherence to the respiratory epithelium.
- The study identified two homologous binding domains in Hia that interact with the same host cell receptor.
- The structure of Hia is characterized by a modular architecture containing repeats of structurally distinct domains.
Takeaway
The Hia protein helps bacteria stick to our respiratory system, and its structure is made up of repeating parts that work together to do this.
Methodology
The study used crystallography to determine the structures of various fragments of the Hia protein.
Digital Object Identifier (DOI)
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