ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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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
37 citing papers in PubMed, 65 citations in OpenAlex.
- Structure-based classification of bacterial chitooligosaccharide-specific outer membrane porins (ChiPs).The Journal of biological chemistry · 2026Article
- Inactivation of the porB gene reduces the virulence of Neisseria meningitidis in transgenic mice.BMC microbiology · 2025Article
- Isolation of human monoclonal antibodies from 4CMenB vaccinees reveals PorB and LOS as the main OMV components inducing cross-strain protection.Frontiers in immunology · 2025Article
- Evolutionary Engineering a Larger Porin Using a Loop-to-Hairpin Mechanism.Journal of molecular biology · 2023Article
- Evolutionary engineering a larger porin using a loop-to-hairpin mechanism.bioRxiv : the preprint server for biology · 2023Article
- PathogenicInfection and immunity · 2022Article
- Viral vectors expressing group B meningococcal outer membrane proteins induce strong antibody responses but fail to induce functional bactericidal activity.The Journal of infection · 2022Article
- An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding.Biochimica et biophysica acta. Biomembranes · 2021Article
- A fully automated crystallization apparatus for small protein quantities.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Single-channel properties, sugar specificity, and role of chitoporin in adaptive survival ofThe Journal of biological chemistry · 2020Article
- Immunogenicity profiling of protein antigens from capsular group B Neisseria meningitidis.Scientific reports · 2019Article
- High-resolution experimental and computational electrophysiology reveals weak β-lactam binding events in the porin PorB.Scientific reports · 2019Article
- Molecular characterization of Neisseria meningitidis isolates recovered from 11-19-year-old meningococcal carriers in Salvador, Brazil.PloS one · 2017Article
- Neisseriae internalization by epithelial cells is enhanced by TLR2 stimulation.Microbes and infection · 2016Article
- Neisseria meningitidis Lacking the Major Porins PorA and PorB Is Viable and Modulates Apoptosis and the Oxidative Burst of Neutrophils.Journal of proteome research · 2016Article
- Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane.The Journal of biological chemistry · 2016Article
- Article
- Oral administration of recombinant Neisseria meningitidis PorA genetically fused to H. pylori HpaA antigen increases antibody levels in mouse serum, suggesting that PorA behaves as a putative adjuvant.Human vaccines & immunotherapeutics · 2015Article
- Article
- Inhibition of the alternative pathway of nonhuman infant complement by porin B2 contributes to virulence of Neisseria meningitidis in the infant rat model.Infection and immunity · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
PorB is the second most prevalent outer membrane protein in Neisseria meningitidis. PorB is required for neisserial pathogenesis and can elicit a Toll-like receptor mediated host immune response. Here, the x-ray crystal structure of PorB has been determined to 2.3 A resolution. Structural analysis and cocrystallization studies identify three putative solute translocation pathways through the channel pore: One pathway transports anions nonselectively, one transports cations nonselectively, and one facilitates the specific uptake of sugars. During infection, PorB likely binds host mitochondrial ATP, and cocrystallization with the ATP analog AMP-PNP suggests that binding of nucleotides regulates these translocation pathways both by partial occlusion of the pore and by restricting the motion of a putative voltage gating loop. PorB is located on the surface of N. meningitidis and can be recognized by receptors of the host innate immune system. Features of PorB suggest that Toll-like receptor mediated recognition outer membrane proteins may be initiated with a nonspecific electrostatic attraction.
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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.