ArticleProceedings of the National Academy of Sciences of the United States of America2009
Elucidation of a pH-folding switch in the Pseudomonas syringae effector protein AvrPto.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 35 citations in OpenAlex.
- From gut colonization to recurrence:Gut microbes · 2026Review
- Noncanonical calcium binding motif controls folding of HopQ1, a Pseudomonas syringae type III secretion effector, in a pH-dependent manner.Scientific reports · 2024Article
- Environmental alkalization suppresses deployment of virulence strategies inJournal of bacteriology · 2024Article
- Recruitment of heterologous substrates by bacterial secretion systems for transkingdom translocation.Frontiers in cellular and infection microbiology · 2023Review
- Dynamic relocalization of cytosolic type III secretion system components prevents premature protein secretion at low external pH.Nature communications · 2021Article
- Structure and Function in Antimicrobial Piscidins: Histidine Position, Directionality of Membrane Insertion, and pH-Dependent Permeabilization.Journal of the American Chemical Society · 2019Article
- Nuclease activity gives an edge to host-defense peptide piscidin 3 over piscidin 1, rendering it more effective against persisters and biofilms.The FEBS journal · 2017Article
- Acidic pH and divalent cation sensing by PhoQ are dispensable for systemic salmonellae virulence.eLife · 2015Article
- Ion-mediated conformational switches.Chemical science · 2015Article
- A non-catalytic histidine residue influences the function of the metalloprotease of Listeria monocytogenes.Microbiology (Reading, England) · 2014Article
- Intrinsic disorder in pathogen effectors: protein flexibility as an evolutionary hallmark in a molecular arms race.The Plant cell · 2013Article
- Article
- Structural instability tuning as a regulatory mechanism in protein-protein interactions.Molecular cell · 2011Article
- New insights into the signaling mechanism of the pH-responsive, membrane-integrated transcriptional activator CadC of Escherichia coli.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Pathogenic bacteria have developed extraordinary strategies for invading host cells. The highly conserved type III secretion system (T3SS) provides a regulated conduit between the bacterial and host cytoplasm for delivery of a specific set of bacterial effector proteins that serve to disrupt host signaling and metabolism for the benefit of the bacterium. Remarkably, the inner diameter of the T3SS apparatus requires that effector proteins pass through in at least a partially unfolded form. AvrPto, an effector protein of the plant pathogen Pseudomonas syringae, adopts a helical bundle fold of low stability (DeltaG(F-->U) = 2 kcal/mol at pH 7, 26.6 degrees C) and offers a model system for chaperone-independent secretion. P. syringae effector proteins encounter a pH gradient as they translocate from the bacterial cytoplasm (mildly acidic) into the host cell (neutral). Here, we demonstrate that AvrPto possesses a pH-sensitive folding switch controlled by conserved residue H87 that operates precisely in the pH range expected between the bacterial and host cytoplasm environments. These results provide a mechanism for how a bacterial effector protein employs an intrinsic pH sensor to unfold for translocation via the T3SS and refold once in the host cytoplasm and provide fundamental insights for developing strategies for delivery of engineered therapeutic proteins to target tissues.
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