Septic Shock by Gram-Negative Infections: Role of Outer Membrane Proteins

Galdiero, Marilena; Cantisani, Marco; Tarallo, Rossella; Falanga, Annarita; Galdiero, Stefania

doi:10.5772/29110

Cited by 3 publications

(1 citation statement)

References 75 publications

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“…During their interaction with the host, porins from several Gram-negative bacteria have diverse biological activities on several eukaryotic cell types, in fact, porins can be considered important inducers of biological activity in host-cell interactions [52]. Several studies have been performed to analyze their immunobiological activities, showing that porins have important effects in several pathogenic mechanisms.…”

Section: Role Of Bacterial Porinsmentioning

confidence: 99%

Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins

Galdiero

Falanga²,

Cantisani³

et al. 2012

CPPS

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Gram negative bacteria have evolved many mechanisms of attaching to and invading host epithelial and immune cells. In particular, many outer membrane proteins (OMPs) are involved in this initial interaction between the pathogen and their host. The outer membrane (OM) of Gram-negative bacteria performs the crucial role of providing an extra layer of protection to the organism without compromising the exchange of material required for sustaining life. The OM, therefore, represents a sophisticated macromolecular assembly, whose complexity has yet to be fully elucidated. This review will summarize the structural information available for porins, a class of OMP, and highlight their role in bacterial pathogenesis and their potential as therapeutic targets.The functional role of porins in microbe-host interactions during various bacterial infections has emerged only during the last few decades, and their interaction with a variety of host tissues for adhesion to and invasion of the cell and for evasion of host-defense mechanisms have placed bacterial porins at the forefront of research in bacterial pathogenesis. This review will discuss the role that porins play in activating immunological responses, in inducing signaling pathways and their influence on antibiotic resistance mechanisms that involve modifications of the properties of the OM lipid barrier.

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Section: Role Of Bacterial Porinsmentioning

confidence: 99%

Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins

Galdiero

Falanga²,

Cantisani³

et al. 2012

CPPS

Self Cite

170

128

View full text Add to dashboard Cite

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Antibacterial and immunomodulatory effects of Pheromonicin-NM on Escherichia coli-challenged bovine mammary epithelial cells

Yang

Yuan

et al. 2020

International Immunopharmacology

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

Cantisani

Vitiello²,

Falanga³

et al. 2012

IJN

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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 mitogenactivated 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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Septic Shock by Gram-Negative Infections: Role of Outer Membrane Proteins

Cited by 3 publications

References 75 publications

Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins

Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins

Antibacterial and immunomodulatory effects of Pheromonicin-NM on Escherichia coli-challenged bovine mammary epithelial cells

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

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