ArticleJournal of structural biology2014
Crystallographic analysis of Neisseria meningitidis PorB extracellular loops potentially implicated in TLR2 recognition.
Article in Journal of structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- Structural Assessment ofVaccines · 2024Article
- An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding.Biochimica et biophysica acta. Biomembranes · 2021Article
- Peptidoglycan mediates Leptospira outer membrane protein Loa22 to toll-like receptor 2 for inflammatory interaction: a novel innate immune recognition.Scientific reports · 2021Article
- Protection against a chlamydial respiratory challenge by a chimeric vaccine formulated with theNPJ vaccines · 2020Article
- High-resolution experimental and computational electrophysiology reveals weak β-lactam binding events in the porin PorB.Scientific reports · 2019Article
- S-Layer Protein ofFrontiers in microbiology · 2019Article
- The Pathogenic Neisseria Use a Streamlined Set of Peptidoglycan Degradation Proteins for Peptidoglycan Remodeling, Recycling, and Toxic Fragment Release.Frontiers in microbiology · 2019Review
- Properly folded and functional PorB fromThe Journal of biological chemistry · 2018Article
- Structural and Immunological Characterization of Novel Recombinant MOMP-Based Chlamydial Antigens.Vaccines · 2017Article
- Active Components of Leptospira Outer Membrane Protein LipL32 to Toll-Like Receptor 2.Scientific reports · 2017Article
- Article
- Neisseriae internalization by epithelial cells is enhanced by TLR2 stimulation.Microbes and infection · 2016Article
- Binding of complement factor H to PorB3 and NspA enhances resistance of Neisseria meningitidis to anti-factor H binding protein bactericidal activity.Infection and immunity · 2015Article
- The N terminus of type III secretion needle protein YscF from Yersinia pestis functions to modulate innate immune responses.Infection and immunity · 2015Article
- Review
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Among all Neisseriae species, Neisseria meningitidis and Neisseria gonorrhoeae are the only human pathogens, causative agents of bacterial meningitis and gonorrhoea, respectively. PorB, a pan-Neisseriae trimeric porin that mediates diffusive transport of essential molecules across the bacterial outer membrane, is also known to activate host innate immunity via Toll-like receptor 2 (TLR2)-mediated signaling. The molecular mechanism of PorB binding to TLR2 is not known, but it has been hypothesized that electrostatic interactions contribute to ligand/receptor binding. Strain-specific sequence variability in the surface-exposed loops of PorB which are potentially implicated in TLR2 binding, may explain the difference in TLR2-mediated cell activation in vitro by PorB homologs from the commensal Neisseriae lactamica and the pathogen N. meningitidis. Here, we report a comparative structural analysis of PorB from N. meningitidis serogroup B strain 8765 (63% sequence homology with PorB from N. meningitidis serogroup W135) and a mutant in which amino acid substitutions in the extracellular loop 7 lead to significantly reduced TLR2-dependent activity in vitro. We observe that this mutation both alters the loop conformation and causes dramatic changes of electrostatic surface charge, both of which may affect TLR2 recognition and signaling.
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