ArticleCell surface (Amsterdam, Netherlands)2025
Insights into the complex formation of a trimeric autotransporter adhesin with a peptidoglycan-binding periplasmic protein.
Article in Cell surface (Amsterdam, Netherlands), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Desiccation-tolerant Acinetobacter as a robust chassis candidate for gas-phase bioprocesses.Journal of biological engineering · 2026Article
- Advancements in Bio-Based Piezoelectric Composites for Antibacterial Applications.Bioengineering (Basel, Switzerland) · 2026Review
- Computational Analysis of Periplasmic Protein-Mediated Resistance to Membrane Extraction of a Trimeric Autotransporter Adhesin Transmembrane Domain.Computational and structural biotechnology journal · 2026Article
- Construction and characterization of a nanopore derived from the transmembrane domain of a trimeric autotransporter adhesin.Frontiers in bioengineering and biotechnology · 2026Article
- Phytochemical inhibition of quorum sensing and biofilm formation byVeterinary world · 2025Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trimeric autotransporter adhesins (TAAs) are outer membrane (OM) proteins that are widely distributed in gram-negative bacteria and are involved primarily in adhesion to biotic and abiotic surfaces, cell agglutination, and biofilm formation. TAAs consist of a passenger domain, which is secreted onto the cell surface, and a transmembrane domain, which forms a pore in the OM to secrete and anchor the passenger domain. Because the interactions between TAAs and chaperones or dedicated auxiliary proteins during secretion are short-lived, TAAs are thought to reside on the OM without forming complexes with other proteins after secretion. In this study, we aimed to clarify the interactions between an
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Registered trials
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