ArticleBiophysical journal2021
Correlating the Structure and Activity of Y. pestis Ail in a Bacterial Cell Envelope.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Structure-activity of outer membrane proteins in native bacterial membrane vesicles by solid-state NMR.bioRxiv : the preprint server for biology · 2026Article
- Nuclear magnetic resonance of membrane proteins-Advances and opportunities.Current opinion in structural biology · 2026Review
- Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025Review
- In situ NMR reveals a pH sensor motif in an outer membrane protein that drives bacterial vesicle production.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite.Journal of structural biology · 2024Article
- Dynamic Nuclear Polarization Illuminates Key Protein-Lipid Interactions in the Native Bacterial Cell Envelope.Biochemistry · 2023Article
- Dynamic nuclear polarization illuminates key protein-lipid interactions in the native bacterial cell envelope.bioRxiv : the preprint server for biology · 2023Article
- Interplays of mutations inFrontiers in cellular and infection microbiology · 2023Article
- A Comparative Study of Nitroxide-Based Biradicals for Dynamic Nuclear Polarization in Cellular Environments.Chembiochem : a European journal of chemical biology · 2022Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Understanding microbe-host interactions at the molecular level is a major goal of fundamental biology and therapeutic drug development. Structural biology strives to capture biomolecular structures in action, but the samples are often highly simplified versions of the complex native environment. Here, we present an Escherichia coli model system that allows us to probe the structure and function of Ail, the major surface protein of the deadly pathogen Yersinia pestis. We show that cell surface expression of Ail produces Y. pestis virulence phenotypes in E. coli, including resistance to human serum, cosedimentation of human vitronectin, and pellicle formation. Moreover, isolated bacterial cell envelopes, encompassing inner and outer membranes, yield high-resolution solid-state NMR spectra that reflect the structure of Ail and reveal Ail sites that are sensitive to the bacterial membrane environment and involved in the interactions with human serum components. The data capture the structure and function of Ail in a bacterial outer membrane and set the stage for probing its interactions with the complex milieu of immune response proteins present in human serum.
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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.