Self-associating autotransporters, SAATs: functional and structural similarities
Abstract
The autotransporter family of translocated proteins in Gram-negative bacteria all contain three structural motifs, a signal sequence, a passenger domain and a translocator domain. The autotransporters constitute a highly versatile group of proteins with respect to function, which accords with the widespread presence of these proteins. The group encompasses many important virulence factors. In Escherichia coli, a subgroup of autotransporter proteins consists of the TibA adhesin/invasin associated with some enterotoxigenic E. coli, the AIDA adhesin from diarrhea-causing E. coli and finally, the Ag43 autoaggregation factor found in the majority of E. coli strains. The three proteins exhibit approximately 25% identity at the sequence level, and are quite different with respect to size, glycosylation and processing. Nevertheless, they share some important properties: all are self-associating proteins that cause bacterial aggregation. They can also interact with each other via heterologous interactions to cause formation of mixed bacterial aggregates. Furthermore, these proteins enhance biofilm formation. Based on these properties we propose to classify them together in a group termed SAATs: self-associating autotransporters.
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Self-associating autotransporters (SAATs) of the Enterobacteriaceae and many type Vc secreted proteins promote strong autoaggregation.
“Among these, particularly the self-associating autotransporters (SAATs) of the Enterobacteriaceae (representing type Va) [69] and many type Vc secreted-proteins, such as the Yersinia adhesin YadA, BadA from Bartonella henselae and AtaA from certain strains of Acinetobacter baumannii [20],[23],[70], promote strong autoaggregation.”
From Bacterial autoaggregation (2018) · cites this paper as [69]
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- Authors
- Klemm, P., Vejborg, R. M., & Sherlock, O.
- Affiliations
- Technical University of Denmark (DK)
- Corresponding author
- Klemm, Per
- Venue
- International Journal of Medical Microbiology
- Publisher
- Elsevier BV
- Published
- 2006-08
- Volume
- 296
- Issue
- 4-5
- Pages
- 187-195
- ISSN
- 1438-4221 (ISSN-L)
- OpenAlex
- W1982077771
- Cited by
- 109
- References
- 43
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 1 · 2023: 6 · 2022: 2 · 2021: 4 · 2020: 3 · 2019: 6 · 2018: 9 · 2017: 5 · 2016: 4 · 2015: 4 · 2014: 7 · 2013: 12 · 2012: 8
- FWCI
- 0.61
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- International Journal of Medical Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU) (submittedVersion)
- Funders
- Teknologi og Produktion, Det Frie Forskningsråd
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- autotransporters, Escherichia coli, bacterial adhesins, virulence factors, bacterial aggregation, biofilm formation, enterotoxigenic Escherichia coli, signal peptide, passenger domain, protein glycosylation, protein processing
- MeSH terms
- Bacterial Adhesion, Bacterial Outer Membrane Proteins, Biological Transport, Carrier Proteins, Escherichia coli, Gram-Negative Bacteria, Hydrogen-Ion Concentration, Fimbriae, Bacterial, Bacterial Capsules, Biofilms, Adhesins, Bacterial, Adhesins, Escherichia coli
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