ArticleScientific reports2016
An Acinetobacter trimeric autotransporter adhesin reaped from cells exhibits its nonspecific stickiness via a highly stable 3D structure.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Comparative genomics andFrontiers in microbiology · 2026Article
- Computational Analysis of Periplasmic Protein-Mediated Resistance to Membrane Extraction of a Trimeric Autotransporter Adhesin Transmembrane Domain.Computational and structural biotechnology journal · 2026Article
- Insights into the complex formation of a trimeric autotransporter adhesin with a peptidoglycan-binding periplasmic protein.Cell surface (Amsterdam, Netherlands) · 2025Article
- Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells.Nature communications · 2025Article
- Virulence-linked adhesin drives mutualist colonization of the bee gut via biofilm formation.bioRxiv : the preprint server for biology · 2024Article
- Adhesion preference of the sticky bacteriumFrontiers in bioengineering and biotechnology · 2024Article
- Development of a Biocontained Toluene-Degrading Bacterium for Environmental Protection.Microbiology spectrum · 2021Article
- A conserved region of Acinetobacter trimeric autotransporter adhesion, Ata, provokes suppression of Acinetobacter baumannii virulence.Archives of microbiology · 2021Article
- Cell behavior of the highly sticky bacterium Acinetobacter sp. Tol 5 during adhesion in laminar flows.Scientific reports · 2018Article
- Reversible bacterial immobilization based on the salt-dependent adhesion of the bacterionanofiber protein AtaA.Microbial cell factories · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trimeric autotransporter adhesins (TAAs), cell surface proteins of Gram-negative bacteria, mediate bacterial adhesion to host cells and extracellular matrix proteins. However, AtaA, a TAA in the nonpathogenic Acinetobacter sp. strain Tol 5, shows nonspecific, high adhesiveness to abiotic material surfaces as well as to biotic surfaces. AtaA is a homotrimer of polypeptides comprising 3,630 amino acids and forms long nanofibers; therefore, it is too large and structurally complex to be produced as a recombinant protein. In this study, we isolated AtaA's passenger domain (AtaA PSD), which is translocated to the cell surface through the C-terminal transmembrane domain and exhibits biological functions, using a new method. We introduced a protease recognition site and reaped AtaA nanofibers 225 nm in length from the cell surface through proteolytic cleavage with a specific protease. Biochemical and biophysical analyses of the purified native AtaA PSD revealed that it has a stable structure under alkaline and acidic conditions. Temperatures above 80 °C, which disrupted AtaA's higher-order structure but maintained the full-length AtaA polypeptide, inactivated AtaA's nonspecific adhesiveness, suggesting that the stickiness of AtaA requires its 3D structure. This finding refutes the widespread but vague speculation that large unfolded polypeptides readily stick to various surfaces.
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