Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Typing and surface charges of the variable loop regions of PorB from Neisseria meningitidis.

IUBMB life - 1 Jun 2016

Stefanelli Paola, Neri Arianna, Tanabe Mikio, Fazio Cecilia, Massari Paola

Abstract excerpt

PorB is a pan-Neisserial major outer membrane protein with a trimeric β-barrel structure. Each monomer presents eight periplasmic turns and eight surface exposed loop regions with sequence variability. PorB induces activation of host cell responses via a TLR2-dependent mechanism likely mediated by electrostatic interactions between TLR2 and PorB surface exposed loops. Variability in the loop amino acid sequence...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alleles
Share to TLR2 gene
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Neisseria meningitidis

Share to Porins

Share to Protein Conformation

Share to Serogroup

Source

Identifiers

PMID: 27156582
DOI: 10.1002/iub.1508

Genes

TLR2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Typing and surface charges of the variable loop regions of PorB from Neisseria meningitidis.PMID 27156582Read ↗

The amino acid sequence of Neisseria lactamica PorB surface-exposed loops influences Toll-like receptor 2-dependent cell activation.Semantic proximity Read ↗

Structural and evolutionary inference from molecular variation in Neisseria porins.Semantic proximity Read ↗

Investigating genetic, antigenic, and structural diversity in the Neisseria gonorrhoeae outer membrane protein, PorB: implications for vaccine design.Semantic proximity Read ↗

Multiple facets of bacterial porinsSemantic proximity Read ↗

PorA types in Neisseria meningitidis serogroup B isolated in Argentina from 2001 to 2003: implications for the design of an outer membrane protein-based vaccine.Semantic proximity Read ↗

Distribution of surface protein variants among hyperinvasive meningococci: implications for vaccine design.Semantic proximity Read ↗

Bioinformatic analysis of meningococcal Msf and Opc to inform vaccine antigen design.Semantic proximity Read ↗

Sequence analysis and relationships between meningococcal class 3 serotype proteins and other porins from pathogenic and non-pathogenic Neisseria species.Semantic proximity Read ↗

Prevalence and phase variable expression status of two autotransporters, NalP and MspA, in carriage and disease isolates of Neisseria meningitidis.Semantic proximity Read ↗

Antigenic and/or phase variation of PorA protein in non-subtypable Neisseria meningitidis strains isolated in Spain.Semantic proximity Read ↗

Variation within serovars of Neisseria gonorrhoeae detected by structural analysis of outer-membrane protein PIB and by pulsed-field gel electrophoresis.Semantic proximity Read ↗

Deletion of major porins from meningococcal outer membrane vesicle vaccines enhances reactivity against heterologous serogroup B Neisseria meningitidis strainsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.