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

Cantisani, Marco; Vitiello, Mariateresa; Falanga, Annarita; Finamore, Emiliana; Galdiero, Marilena; Galdiero, Stefania

doi:10.2147/ijn.s30467

Cited by 13 publications

(5 citation statements)

References 47 publications

(64 reference statements)

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“…Accumulating evidence has suggested that the regulation of transcriptional factors and the subunit composition by porin stimulation may affect the adaptive immune mechanism to modulate the production of biologically active proteins or peptides. The engagement of multiple pathways during signal transmission makes the possible use of molecular inhibitors as therapeutic agents very difficult; although recent findings show that peptides complementary to loop regions have a certain ability to block the activity of the porin [86]. …”

Section: Porins Induced Signaling Pathwaysmentioning

confidence: 99%

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

Galdiero

Falanga²,

Cantisani³

et al. 2012

CPPS

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171

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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: Porins Induced Signaling Pathwaysmentioning

confidence: 99%

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

Galdiero

Falanga²,

Cantisani³

et al. 2012

CPPS

Self Cite

171

128

View full text Add to dashboard Cite

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“…Measurement of human hs-CRP in serum was performed using the nephelometric technique (Minineph TM, the Binding Site Ltd, PO Box 11712, Birmingham, B14 4ZB, U.K.) (Erlandsen & Randers, 2000). Human IL-6 was measured by AviBion Human ELISA kits (Orgenium Laboratories Business Unit, Vantaa, Finland) according to the manufacturer's recommendations (Cantisani et al, 2012).…”

Section: Methodsmentioning

confidence: 99%

“…Inflammatory biomarkers, including CRP and IL-6 are increased in various inflammatory conditions and are useful in studying thalassemia and other disease states, including heart disease (Cantisani et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

The relation between glutathione S-Transferase M1 null-genotype and cardiac problems in beta-thalassemia.

et al. 2016

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“…The roles of these surface-exposed loops are of considerable interest, and numerous studies have shown their importance in terms of hostpathogen interactions [3]. In particular, extracellular loops have been shown to bind specific cellular receptors, to mediate signalling, and to modulate the immune response [9][10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

G1 Cell Cycle Arrest Is Induced by the Fourth Extracellular Loop of Meningococcal PorA in Epithelial and Endothelial Cells

Vassey

Firdaus

Aslam

et al. 2023

Cellular Microbiology

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Neisseria meningitidis is the most frequent cause of bacterial meningitis and is one of the few bacterial pathogens that can breach the blood-brain barrier (BBB). The 37/67 kDa laminin receptor (LamR) was previously identified as a receptor mediating meningococcal binding to rodent and human brain microvascular endothelial cells, which form part of the BBB. The meningococcal surface proteins PorA and PilQ were identified as ligands for this receptor. Subsequently, the fourth extracellular loop of PorA (PorA-Loop4) was identified as the LamR-binding moiety. Here, we show that PorA-Loop4 targets the 37 kDa laminin receptor precursor (37LRP) on the cell surface by demonstrating that deletion of this loop abrogates the recruitment of 37LRP under meningococcal colonies. Using a circularized peptide corresponding to PorA-Loop4, as well as defined meningococcal mutants, we demonstrate that host cell interaction with PorA-Loop4 results in perturbation of p-CDK4 and Cyclin D1. These changes in cell cycle control proteins are coincident with cellular responses including inhibition of cell migration and a G1 cell cycle arrest. Modulation of the cell cycle of host cells is likely to contribute to the pathogenesis of meningococcal disease.

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

Cited by 13 publications

References 47 publications

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

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

The relation between glutathione S-Transferase M1 null-genotype and cardiac problems in beta-thalassemia.

G1 Cell Cycle Arrest Is Induced by the Fourth Extracellular Loop of Meningococcal PorA in Epithelial and Endothelial Cells

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