ArticleInternational journal of nanomedicine2012
Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity.
Article in International journal of nanomedicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 21 citations in OpenAlex.
- Prevalence, Resistance Patterns and Biofilm Production Ability of Bacterial Uropathogens from Cases of Community-Acquired Urinary Tract Infections in South Italy.Pathogens (Basel, Switzerland) · 2023Article
- Viral Infection and Antiviral Treatments in Ocular Pathologies.Microorganisms · 2022Review
- Characterization and Comparison of Ocular Surface Microbiome in Newborns.Microorganisms · 2022Article
- 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
- The C-terminal region of the major outer sheath protein of Treponema denticola inhibits neutrophil chemotaxis.Molecular oral microbiology · 2017Article
- Marine Antimicrobial Peptides: Nature Provides Templates for the Design of Novel Compounds against Pathogenic Bacteria.International journal of molecular sciences · 2016Review
- Microbe-host interactions: structure and role of Gram-negative bacterial porins.Current protein & peptide science · 2012Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Haemophilus influenzae type b (Hib) is one of the leading causes of invasive bacterial infection in young children. It is characterized by inflammation that is mainly mediated by cytokines and chemokines. One of the most abundant components of the Hib outer membrane is the P2 porin, which has been shown to induce the release of several inflammatory cytokines. A synthetic peptide corresponding to loop L7 of the porin activates JNK and p38 mitogen-activated protein kinase (MAPK) pathways. We report a novel use of the complementary peptide approach to design a peptide that is able to bind selectively to the protein P2, thereby reducing its activity. This work provides insights into essential molecular details of P2 that may affect the pathogenesis of Hib infections where interruption of the signaling cascade could represent an attractive therapeutic strategy.
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Registered trials
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