ArticleJournal of the American Chemical Society2014
Structure of the Neisserial outer membrane protein Opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
36 citing papers in PubMed, 58 citations in OpenAlex.
- Investigation of Correlates of Protection Against Gonococcal Infection by Comparative Immunoprofiling of Responses in Experimental and Clinical Studies.The Journal of infectious diseases · 2026Article
- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Neutrophil CEACAMs and the Inflammatory Response toJournal of innate immunity · 2026Review
- Assessing Wolbachia circulation in wild populations of phlebotomine sand flies from Spain and Morocco: implications for control of leishmaniasis.Parasites & vectors · 2025Article
- Magic-angle spinning NMR structure of Opa60 in lipid bilayers.Journal of structural biology: X · 2024Article
- Identification and characterisation of a major outer membrane protein from Methylacidiphilum fumariolicum SolV.Antonie van Leeuwenhoek · 2023Article
- Distinct Wolbachia localization patterns in oocytes of diverse host species reveal multiple strategies of maternal transmission.Genetics · 2023Article
- A Germin-Like Protein GLP1 of Legumes Mediates Symbiotic Nodulation by Interacting with an Outer Membrane Protein of Rhizobia.Microbiology spectrum · 2023Article
- Temperature effects on cellular host-microbe interactions explain continent-wide endosymbiont prevalence.Current biology : CB · 2022Article
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- Molecular Docking Simulation Studies Identifies Potential Natural Product Derived-Antiwolbachial Compounds as Filaricides against Onchocerciasis.Biomedicines · 2021Article
- Proton Detected Solid-State NMR of Membrane Proteins at 28 Tesla (1.2 GHz) and 100 kHz Magic-Angle Spinning.Biomolecules · 2021Article
- Transferred-Rotational-Echo Double Resonance.The journal of physical chemistry. A · 2021Article
- Anti-Virulence Therapeutic Approaches forAntibiotics (Basel, Switzerland) · 2021Review
- Imaging Flow Cytometry Analysis of CEACAM Binding to Opa-Expressing Neisseria gonorrhoeae.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2020Article
- Epithelial Haven and Autophagy Breakout in Gonococci Infection.Frontiers in cell and developmental biology · 2020Review
- CEACAM1 structure and function in immunity and its therapeutic implications.Seminars in immunology · 2019Review
- Reconstitution and NMR Characterization of the Ion-Channel Accessory Subunit Barttin in Detergents and Lipid-Bilayer Nanodiscs.Frontiers in molecular biosciences · 2019Article
- Refinement of Highly Flexible Protein Structures using Simulation-Guided Spectroscopy.Angewandte Chemie (International ed. in English) · 2018Article
- Predicting allostery and microbial drug resistance with molecular simulations.Current opinion in structural biology · 2018Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The structure and dynamics of Opa proteins, which we report herein, are responsible for the receptor-mediated engulfment of Neisseria gonorrheae or Neisseria meningitidis by human cells and can offer deep understanding into the molecular recognition of pathogen-host receptor interactions. Such interactions are vital to understanding bacterial pathogenesis as well as the mechanism of foreign body entry to a human cell, which may provide insights for the development of targeted pharmaceutical delivery systems. The size and dynamics of the extracellular loops of Opa60 required a hybrid refinement approach wherein membrane and distance restraints were used to generate an initial NMR structural ensemble, which was then further refined using molecular dynamics in a DMPC bilayer. The resulting ensemble revealed that the extracellular loops, which bind host receptors, occupy compact conformations, interact with each other weakly, and are dynamic on the nanosecond time scale. We predict that this conformational sampling is critical for enabling diverse Opa loop sequences to engage a common set of receptors.
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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.