ArticleThe Journal of biological chemistry2011
Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 78 citations in OpenAlex.
- Mutations affecting the β-sheet at the extracellular opening of the intimin β-barrel domain lead to reduced protein levels and inefficient passenger secretion.Bioscience reports · 2026Article
- Engineering non-pathogenic bacteria for auto-transporter-driven secretion of functional interferon.Gut microbes · 2025Article
- The crystal structure of the toxin EspC from enteropathogenicGut microbes · 2025Article
- Bacterial surface display of human lectins in Escherichia coli.Microbial biotechnology · 2024Article
- In Vivo Disulfide-Bond Crosslinking to Study β-Barrel Membrane Protein Interactions, Dynamicity, and Folding Intermediates.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Efficient Autotransporter-Mediated Extracellular Secretion of a Heterologous Recombinant Protein by Escherichia coli.Microbiology spectrum · 2023Article
- Cysteine-Dependent Conformational Heterogeneity of Shigella flexneri Autotransporter IcsA and Implications of Its Function.Microbiology spectrum · 2022Article
- BamA forms a translocation channel for polypeptide export across the bacterial outer membrane.Molecular cell · 2021Article
- BamA and BamD Are Essential for the Secretion of Trimeric Autotransporter Adhesins.Frontiers in microbiology · 2021Article
- Article
- Properties of protein unfolded states suggest broad selection for expanded conformational ensembles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
- Developing Gram-negative bacteria for the secretion of heterologous proteins.Microbial cell factories · 2018Review
- Molecular basis for the folding of β-helical autotransporter passenger domains.Nature communications · 2018Article
- Comparing autotransporter β-domain configurations for their capacity to secrete heterologous proteins to the cell surface.PloS one · 2018Article
- Fusion with the cold-active esterase facilitates autotransporter-based surface display of the 10th human fibronectin domain in Escherichia coli.Extremophiles : life under extreme conditions · 2018Article
- Antigen Localization Influences the Magnitude and Kinetics of Endogenous Adaptive Immune Response to Recombinant Salmonella Vaccines.Infection and immunity · 2017Article
- Article
- Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria.Microbiology spectrum · 2015Review
- Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.Molecular microbiology · 2015Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Autotransporters are a superfamily of virulence factors typified by a channel-forming C terminus that facilitates translocation of the functional N-terminal passenger domain across the outer membrane of Gram-negative bacteria. This final step in the secretion of autotransporters requires a translocation-competent conformation for the passenger domain that differs markedly from the structure of the fully folded secreted protein. The nature of the translocation-competent conformation remains controversial, in particular whether the passenger domain can adopt secondary structural motifs, such as disulfide-bonded segments, while maintaining a secretion-competent state. Here, we used the endogenous and closely spaced cysteine residues of the plasmid-encoded toxin (Pet) from enteroaggregative Escherichia coli to investigate the effect of disulfide bond-induced folding on translocation of an autotransporter passenger domain. We reveal that rigid structural elements within disulfide-bonded segments are resistant to autotransporter-mediated secretion. We define the size limit of disulfide-bonded segments tolerated by the autotransporter system demonstrating that, when present, cysteine pairs are intrinsically closely spaced to prevent congestion of the translocator pore by large disulfide-bonded regions. These latter data strongly support the hairpin mode of autotransporter biogenesis.
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Registered trials
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.