ArticleJournal of bacteriology2006
Proteolytic processing is not essential for multiple functions of the Escherichia coli autotransporter adhesin involved in diffuse adherence (AIDA-I).
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 43 citations in OpenAlex.
- The Role ofInternational journal of molecular sciences · 2025Review
- Engineering Adhesion of the Probiotic StrainACS synthetic biology · 2024Article
- Characterization and antibiotic resistance pattern of diffusely adherentNew microbes and new infections · 2020Article
- The Bartonella autotransporter BafA activates the host VEGF pathway to drive angiogenesis.Nature communications · 2020Article
- The Serine Protease Autotransporters TagB, TagC, and Sha from Extraintestinal PathogenicInternational journal of molecular sciences · 2020Article
- The UDP-GalNAcA biosynthesis genes gna-gne2 are required to maintain cell envelope integrity and in vivo fitness in multi-drug resistant Acinetobacter baumannii.Molecular microbiology · 2020Article
- Three new serine-protease autotransporters ofVirulence · 2019Article
- Type V Secretion Systems: An Overview of Passenger Domain Functions.Frontiers in microbiology · 2019Review
- Global landscape of cell envelope protein complexes in Escherichia coli.Nature biotechnology · 2018Article
- Characterization of Shiga Toxin Subtypes and Virulence Genes in Porcine Shiga Toxin-Producing Escherichia coli.Frontiers in microbiology · 2016Article
- Multiple driving forces required for efficient secretion of autotransporter virulence proteins.The Journal of biological chemistry · 2015Article
- Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Molecular microbiology · 2015Review
- An alternative outer membrane secretion mechanism for an autotransporter protein lacking a C-terminal stable core.Molecular microbiology · 2013Article
- Acquisition of omptin reveals cryptic virulence function of autotransporter YapE in Yersinia pestis.Molecular microbiology · 2013Article
- Identification and mechanism of evolution of new alleles coding for the AIDA-I autotransporter of porcine pathogenic Escherichia coli.Applied and environmental microbiology · 2012Article
- XatA, an AT-1 autotransporter important for the virulence of Xylella fastidiosa Temecula1.MicrobiologyOpen · 2012Article
- In vitro assay of bacterial adhesion onto mammalian epithelial cells.Journal of visualized experiments : JoVE · 2011Article
- Structure-function analysis of the TibA self-associating autotransporter reveals a modular organization.Infection and immunity · 2011Article
- Article
- Conformation change in a self-recognizing autotransporter modulates bacterial cell-cell interaction.The Journal of biological chemistry · 2010Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli adhesin involved in diffuse adherence (AIDA-I), like many other autotransporter proteins, is released in the periplasm as a proprotein undergoing proteolytic processing after its translocation across the outer membrane. The proprotein is cleaved into a membrane-embedded fragment, AIDAc, and an extracellular fragment, the mature AIDA-I adhesin. The latter remains noncovalently associated with the outer membrane and can be released by heat treatment. The mechanism of cleavage of the proprotein and its role in the functionality of AIDA-I are not understood. Here, we show that cleavage is independent of the amount of AIDA-I in the outer membrane, suggesting an intramolecular autoproteolytic mechanism or a cleavage mediated by an unknown protease. We show that the two fragments, mature AIDA-I and AIDAc, can be cosolubilized and copurified in a folded and active conformation. We observed that the release by heat treatment results from the unfolding of AIDA-I and that the interaction of AIDA-I with AIDAc seems to be disturbed only by denaturation. We constructed an uncleavable point mutant of AIDA-I, where a serine of the cleavage site was changed into a leucine, and showed that adhesion, autoaggregation, and biofilm formation mediated by the mutant are indistinguishable from the wild-type levels. Lastly, we show that both proteins can mediate the invasion of cultured epithelial cells. Taken together, our experiments suggest that the proteolytic processing of AIDA-I plays a minor role in the functionality of this protein.
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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.