ArticleInfection and immunity2003
Role of surface-exposed loops of Haemophilus influenzae protein P2 in the mitogen-activated protein kinase cascade.
Article in Infection and immunity, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It carries an expression of concern. Cited by 21 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
21 citing papers in PubMed, 40 citations in OpenAlex.
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- Diversification of OmpA and OmpF of Yersinia ruckeri is independent of the underlying species phylogeny and evidence of virulence-related selection.Scientific reports · 2021Article
- The Membranotropic PeptideJournal of fungi (Basel, Switzerland) · 2021Article
- OctoPartenopin: Identification and Preliminary Characterization of a Novel Antimicrobial Peptide from the Suckers ofMarine drugs · 2020Article
- Eradication of Candida albicans persister cell biofilm by the membranotropic peptide gH625.Scientific reports · 2020Article
- Surface-exposed loops L7 and L8 of Haemophilus (Glaesserella) parasuis OmpP2 contribute to the expression of proinflammatory cytokines in porcine alveolar macrophages.Veterinary research · 2019Article
- Differential Recognition ofInfection and immunity · 2019Article
- Melittin Inhibition and Eradication Activity for Resistant Polymicrobial Biofilm Isolated from a Dairy Industry after Disinfection.International journal of microbiology · 2019Article
- Efficiency of gold nanoparticles coated with the antimicrobial peptide indolicidin against biofilm formation and development ofInfection and drug resistance · 2018Article
- Marine Antimicrobial Peptides: Nature Provides Templates for the Design of Novel Compounds against Pathogenic Bacteria.International journal of molecular sciences · 2016Review
- Design and activity of a cyclic mini-β-defensin analog: a novel antimicrobial tool.International journal of nanomedicine · 2015Article
- Structural insights into and activity analysis of the antimicrobial peptide myxinidin.Antimicrobial agents and chemotherapy · 2014Article
- Peptide-lipid interactions: experiments and applications.International journal of molecular sciences · 2013Article
- Microbe-host interactions: structure and role of Gram-negative bacterial porins.Current protein & peptide science · 2012Review
- Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity.International journal of nanomedicine · 2012Article
- Mapping the laminin receptor binding domains of Neisseria meningitidis PorA and Haemophilus influenzae OmpP2.PloS one · 2012Article
- Cigarette smoke inhibits airway epithelial cell innate immune responses to bacteria.Infection and immunity · 2010Article
- Characterization and comparative analysis of the genes encoding Haemophilus parasuis outer membrane proteins P2 and P5.Journal of bacteriology · 2009Article
- Porin isolated from the outer membrane of Erwinia amylovora and its encoding gene.Current microbiology · 2007Article
Corrections and comments
- Expression of concern
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The outer membrane of gram-negative bacteria contains several proteins, and some of these proteins, the porins, have numerous biological functions in the interaction with the host; porins are involved in the activation of signal transduction pathways and, in particular, in the activation of the Raf/MEK1-MEK2/mitogen-activated protein kinase (MAPK) cascade. The P2 porin is the most abundant outer membrane protein of Haemophilus influenzae type b. A three-dimensional structural model for P2 was constructed based on the crystal structures of Klebsiella pneumoniae OmpK36 and Escherichia coli PhoE and OmpF. The protein was readily assembled into the beta-barrel fold characteristic of porins, despite the low sequence identity with the template proteins. The model provides information on the structural features of P2 and insights relevant for prediction of domains corresponding to surface-exposed loops, which could be involved in the activation of signal transduction pathways. To identify the role of surface-exposed loops, a set of synthetic peptides were synthesized according to the proposed model and were assayed for MEK1-MEK2/MAPK pathway activation. Our results show that synthetic peptides corresponding to surface loops of protein P2 are able to activate the MEK1-MEK2/MAPK pathways like the entire protein, while peptides modeled on internal beta strands are unable to induce significant phosphorylation of the MEK1-MEK2/MAPK pathways. In particular, the peptides corresponding to loops L5 (Lys206 to Gly219), L6B (Ser239 to Lys253), and L7 (Thr280 to Lys287) activate, as the whole protein, essentially JNK and p38.
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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.