ArticleJournal of bacteriology2008
Contribution of trimeric autotransporter C-terminal domains of oligomeric coiled-coil adhesin (Oca) family members YadA, UspA1, EibA, and Hia to translocation of the YadA passenger domain and virulence of Yersinia enterocolitica.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 44 citations in OpenAlex.
- Effects of the type V secretion system eYadA on the biological properties and pathogenicity of avian pathogenic Escherichia coli.Veterinary research · 2026Article
- The Trimeric Autotransporter Adhesin EmaA and Infective Endocarditis.Pathogens (Basel, Switzerland) · 2024Review
- The serotype a-EmaA adhesin ofMicrobiology (Reading, England) · 2022Article
- Immunogenicity of trimeric autotransporter adhesins and their potential as vaccine targets.Medical microbiology and immunology · 2020Review
- Utilization of Variant and Fusion Proteins To Functionally Map the Aggregatibacter actinomycetemcomitans Trimeric Autotransporter Protein ApiA.Infection and immunity · 2018Article
- Plague Vaccines: Status and Future.Advances in experimental medicine and biology · 2016Review
- Evolutionary conservation in biogenesis of β-barrel proteins allows mitochondria to assemble a functional bacterial trimeric autotransporter protein.The Journal of biological chemistry · 2014Article
- Heterologous expression of Bartonella adhesin A in Escherichia coli by exchange of trimeric autotransporter adhesin domains results in enhanced adhesion properties and a pathogenic phenotype.Journal of bacteriology · 2014Article
- Evaluation of YadC protein delivered by live attenuated Salmonella as a vaccine against plague.Pathogens and disease · 2014Article
- Analysis of the proteome of intracellular Shigella flexneri reveals pathways important for intracellular growth.Infection and immunity · 2013Article
- Characterization and functional analysis of AatB, a novel autotransporter adhesin and virulence factor of avian pathogenic Escherichia coli.Infection and immunity · 2013Article
- Trimeric autotransporter adhesin-dependent adherence of Bartonella henselae, Bartonella quintana, and Yersinia enterocolitica to matrix components and endothelial cells under static and dynamic flow conditions.Infection and immunity · 2011Article
- Neisseria meningitidis adhesin NadA targets beta1 integrins: functional similarity to Yersinia invasin.The Journal of biological chemistry · 2011Article
- Mitochondria can recognize and assemble fragments of a beta-barrel structure.Molecular biology of the cell · 2011Article
- Autotransporters and Their Role in the Virulence of Burkholderia pseudomallei and Burkholderia mallei.Frontiers in microbiology · 2011Article
- Article
- Trimer stability of YadA is critical for virulence of Yersinia enterocolitica.Infection and immunity · 2010Article
- Molecular aspects of Moraxella catarrhalis pathogenesis.Microbiology and molecular biology reviews : MMBR · 2009Review
- Sab, a novel autotransporter of locus of enterocyte effacement-negative shiga-toxigenic Escherichia coli O113:H21, contributes to adherence and biofilm formation.Infection and immunity · 2009Article
- Identification, characterization, and molecular application of a virulence-associated autotransporter from a pathogenic Pseudomonas fluorescens strain.Applied and environmental microbiology · 2009Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Oca family is a novel class of autotransporter-adhesins with highest structural similarity in their C-terminal transmembrane region, which supposedly builds a beta-barrel pore in the outer membrane (OM). The prototype of the Oca family is YadA, an adhesin of Yersinia enterocolitica and Yersinia pseudotuberculosis. YadA forms a homotrimeric lollipop-like structure on the bacterial surface. The C-terminal regions of three YadA monomers form a barrel in the OM and translocate the trimeric N-terminal passenger domain, consisting of stalk, neck, and head region to the exterior. To elucidate the structural and functional role of the C-terminal translocator domain (TLD) and to assess its promiscuous capability with respect to transport of related passenger domains, we constructed chimeric YadA proteins, which consist of the N-terminal YadA passenger domain and C-terminal TLDs of Oca family members UspA1 (Moraxella catarrhalis), EibA (Escherichia coli), and Hia (Haemophilus influenzae). These constructs were expressed in Y. enterocolitica and compared for OM localization, surface exposure, oligomerization, adhesion properties, serum resistance, and mouse virulence. We demonstrate that all chimeric YadA proteins translocated the YadA passenger domain across the OM. Y. enterocolitica strains producing YadA chimeras or wild-type YadA showed comparable binding to collagen and epithelial cells. However, strains producing YadA chimeras were attenuated in serum resistance and mouse virulence. These results demonstrate for the first time that TLDs of Oca proteins of different origin are efficient translocators of the YadA passenger domain and that the cognate TLD of YadA is essential for bacterial survival in human serum and mouse virulence.
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