ArticleThe EMBO journal2004
Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter.
Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
47 citing papers in PubMed.
- Article
- Non-TypeableInternational journal of molecular sciences · 2020Article
- Immunogenicity of trimeric autotransporter adhesins and their potential as vaccine targets.Medical microbiology and immunology · 2020Review
- Non-adaptive Evolution of Trimeric Autotransporters inFrontiers in microbiology · 2020Article
- In vitro assembly of Haemophilus influenzae adhesin transmembrane domain and studies on the electrostatic repulsion at the interface.Biophysical reviews · 2019Review
- Bioinformatic analysis of meningococcal Msf and Opc to inform vaccine antigen design.PloS one · 2018Article
- Folding of a bacterial integral outer membrane protein is initiated in the periplasm.Nature communications · 2017Article
- The crystal structure of PD1, a Haemophilus surface fibril domain.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Structural Basis for Toughness and Flexibility in the C-terminal Passenger Domain of an Acinetobacter Trimeric Autotransporter Adhesin.The Journal of biological chemistry · 2016Article
- Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria.Microbiology spectrum · 2015Review
- Article
- Complete fiber structures of complex trimeric autotransporter adhesins conserved in enterobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Molecular characterization of the EhaG and UpaG trimeric autotransporter proteins from pathogenic Escherichia coli.Applied and environmental microbiology · 2012Article
- Correlation of the amino-acid sequence and the 3D structure of the functional domain of EmaA from Aggregatibacter actinomycetemcomitans.Journal of structural biology · 2012Article
- The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.Bacteriophage · 2012Article
- SadA, a trimeric autotransporter from Salmonella enterica serovar Typhimurium, can promote biofilm formation and provides limited protection against infection.Infection and immunity · 2011Article
- Structure and function of the Haemophilus influenzae autotransporters.Frontiers in cellular and infection microbiology · 2011Review
- Adhesive activity of the haemophilus cryptic genospecies cha autotransporter is modulated by variation in tandem Peptide repeats.Journal of bacteriology · 2011Article
- Construction and immunogenicity of recombinant adenovirus vaccines expressing the HMW1, HMW2, or Hia adhesion protein of nontypeable Haemophilus influenzae.Clinical and vaccine immunology : CVI · 2010Article
- Identification of Burkholderia mallei and Burkholderia pseudomallei adhesins for human respiratory epithelial cells.BMC microbiology · 2010Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.