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Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity

Authors Cantisani M, Vitiello M, Falanga A, Finamore E, Galdiero M, Galdiero S

Received 2 February 2012

Accepted for publication 3 March 2012

Published 11 May 2012 Volume 2012:7 Pages 2361—2371

DOI https://doi.org/10.2147/IJN.S30467

Review by Single-blind

Peer reviewer comments 2

Marco Cantisani,1 Mariateresa Vitiello,2 Annarita Falanga,1 Emiliana Finamore,2 Marilena Galdiero,2 Stefania Galdiero1

1Department of Biological Sciences, CIRPeB and IBB CNR, University of Naples "Federico II," Napoli, Italy; 2Department of Experimental Medicine, II University of Naples, Napoli, Italy

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.

Keywords: complementary-peptide, rational design, porin

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