ArticlePLoS pathogens2008
Structure of the head of the Bartonella adhesin BadA.
Article in PLoS pathogens, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 83 citations in OpenAlex.
- Cooperation between Adh and OR5M11 contributes to the lung pathogenicity of Actinobacillus pleuropneumoniae by facilitating the NLRP3-mediated inflammatory response.Veterinary research · 2026Article
- Structural basis for immune cell binding ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Virulence-linked adhesin drives mutualist colonization of the bee gut via biofilm formation.bioRxiv : the preprint server for biology · 2024Article
- AmSystems · 2024Article
- Adhesion of Bartonella henselae to Fibronectin Is Mediated via Repetitive Motifs Present in the Stalk ofMicrobiology spectrum · 2022Article
- The C-terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network.Molecular microbiology · 2022Article
- Interaction of Bartonella henselae with Fibronectin Represents the Molecular Basis for Adhesion to Host Cells.Microbiology spectrum · 2022Article
- Long-Read Sequencing Reveals Genetic Adaptation ofFrontiers in microbiology · 2022Article
- What Is in a Cat Scratch? Growth ofMicroorganisms · 2021Review
- CEACAM1 Activation by CbpF-ExpressingFrontiers in cellular and infection microbiology · 2021Article
- New Insights on the Feature and Function of Tail Tubular Protein B and Tail Fiber Protein of the Lytic Bacteriophage φYeO3-12 Specific forMolecules (Basel, Switzerland) · 2020Article
- The Bartonella autotransporter BafA activates the host VEGF pathway to drive angiogenesis.Nature communications · 2020Article
- Recent advances in the understanding of trimeric autotransporter adhesins.Medical microbiology and immunology · 2020Review
- Non-adaptive Evolution of Trimeric Autotransporters inFrontiers in microbiology · 2020Article
- Article
- Interactions between the Trimeric Autotransporter Adhesin EmaA and Collagen Revealed by Three-Dimensional Electron Tomography.Journal of bacteriology · 2019Article
- Mechanisms of Resistance to the Contact-Dependent Bacteriocin CdzC/D inJournal of bacteriology · 2019Article
- Ahnak-knockout mice show susceptibility to Bartonella henselae infection because of CD4+ T cell inactivation and decreased cytokine secretion.BMB reports · 2019Article
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
- Genomic changes associated with the evolutionary transition of an insect gut symbiont into a blood-borne pathogen.The ISME journal · 2017Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trimeric autotransporter adhesins (TAAs) are a major class of proteins by which pathogenic proteobacteria adhere to their hosts. Prominent examples include Yersinia YadA, Haemophilus Hia and Hsf, Moraxella UspA1 and A2, and Neisseria NadA. TAAs also occur in symbiotic and environmental species and presumably represent a general solution to the problem of adhesion in proteobacteria. The general structure of TAAs follows a head-stalk-anchor architecture, where the heads are the primary mediators of attachment and autoagglutination. In the major adhesin of Bartonella henselae, BadA, the head consists of three domains, the N-terminal of which shows strong sequence similarity to the head of Yersinia YadA. The two other domains were not recognizably similar to any protein of known structure. We therefore determined their crystal structure to a resolution of 1.1 A. Both domains are beta-prisms, the N-terminal one formed by interleaved, five-stranded beta-meanders parallel to the trimer axis and the C-terminal one by five-stranded beta-meanders orthogonal to the axis. Despite the absence of statistically significant sequence similarity, the two domains are structurally similar to domains from Haemophilus Hia, albeit in permuted order. Thus, the BadA head appears to be a chimera of domains seen in two other TAAs, YadA and Hia, highlighting the combinatorial evolutionary strategy taken by pathogens.
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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.