ArticlePloS one2010
Structure of a Burkholderia pseudomallei trimeric autotransporter adhesin head.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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
19 citing papers in PubMed, 33 citations in OpenAlex.
- Recent advances in the understanding of trimeric autotransporter adhesins.Medical microbiology and immunology · 2020Review
- Structure of the UspA1 protein fragment from Moraxella catarrhalis responsible for C3d binding.Journal of structural biology · 2019Article
- Article
- Interactions between the Trimeric Autotransporter Adhesin EmaA and Collagen Revealed by Three-Dimensional Electron Tomography.Journal of bacteriology · 2019Article
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
- Structural Basis for Toughness and Flexibility in the C-terminal Passenger Domain of an Acinetobacter Trimeric Autotransporter Adhesin.The Journal of biological chemistry · 2016Article
- Mining locus tags in PubMed Central to improve microbial gene annotation.BMC bioinformatics · 2014Article
- Evidence for metaviromic islands in marine phages.Frontiers in microbiology · 2014Article
- Functional characterization of Burkholderia pseudomallei trimeric autotransporters.Infection and immunity · 2013Article
- 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
- Correlation of the amino-acid sequence and the 3D structure of the functional domain of EmaA from Aggregatibacter actinomycetemcomitans.Journal of structural biology · 2012Article
- Article
- Article
- Structural characterization of a ribose-5-phosphate isomerase B from the pathogenic fungus Coccidioides immitis.BMC structural biology · 2011Article
- Correlation of in situ mechanosensitive responses of the Moraxella catarrhalis adhesin UspA1 with fibronectin and receptor CEACAM1 binding.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Structural genomics of infectious disease drug targets: the SSGCID.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- SAD phasing using iodide ions in a high-throughput structural genomics environment.Journal of structural and functional genomics · 2011Article
- Trimeric autotransporter adhesins in members of the Burkholderia cepacia complex: a multifunctional family of proteins implicated in virulence.Frontiers in cellular and infection microbiology · 2011Review
- Autotransporters and Their Role in the Virulence of Burkholderia pseudomallei and Burkholderia mallei.Frontiers in microbiology · 2011Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundPathogenic bacteria adhere to the host cell surface using a family of outer membrane proteins called Trimeric Autotransporter Adhesins (TAAs). Although TAAs are highly divergent in sequence and domain structure, they are all conceptually comprised of a C-terminal membrane anchoring domain and an N-terminal passenger domain. Passenger domains consist of a secretion sequence, a head region that facilitates binding to the host cell surface, and a stalk region. METHODOLOGY/PRINCIPAL
findingsPathogenic species of Burkholderia contain an overabundance of TAAs, some of which have been shown to elicit an immune response in the host. To understand the structural basis for host cell adhesion, we solved a 1.35 A resolution crystal structure of a BpaA TAA head domain from Burkholderia pseudomallei, the pathogen that causes melioidosis. The structure reveals a novel fold of an intricately intertwined trimer. The BpaA head is composed of structural elements that have been observed in other TAA head structures as well as several elements of previously unknown structure predicted from low sequence homology between TAAs. These elements are typically up to 40 amino acids long and are not domains, but rather modular structural elements that may be duplicated or omitted through evolution, creating molecular diversity among TAAs. CONCLUSIONS/SIGNIFICANCE: The modular nature of BpaA, as demonstrated by its head domain crystal structure, and of TAAs in general provides insights into evolution of pathogen-host adhesion and may provide an avenue for diagnostics.
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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.