Porins from Salmonella enterica serovar Typhimurium induce TNF-α, IL-6 and IL-8 release by CD14-independent and CD11a/CD18-dependent mechanisms

Galdiero, Marilena; D’Isanto, Marina; Vitiello, Mariateresa; Finamore, Emiliana; Peluso, Lucia; Galdiero, Massimiliano

doi:10.1099/00221287-147-10-2697

Cited by 24 publications

(22 citation statements)

References 52 publications

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“…21,23,28,41 Previous reports have demonstrated that porin-stimulated monocytic cell lines are activated with an evident phosphorylation of many cellular proteins. Some proteins were identified as MAPK and as nuclear transcription factors NF-κB, AP-1 and STAT-1/ STAT-3.…”

Section: Discussionmentioning

confidence: 99%

“…Among the different surface bacterial components, Hib porin is involved in the pathogenesis of bacterial meningitis. 28 The damage due to Gram-negative bacteria is a disorder thought to be caused by the excessive stimulation of mononuclear cells by active surface components of bacterial cells. Among those components, LPS has been studied most frequently, and several molecules have been analyzed for their antagonist activity against LPS.…”

Section: Discussionmentioning

confidence: 99%

“…27,28 The protein content of the porin preparation was determined by the method of Lowry et al 29 and checked by SDS-PAGE according to Laemmli. 30 All possible 32 Using the Limulus test, LPS contamination in the porin preparation was estimated to be about 0.001% w/w. The pore-forming ability of our preparation was checked by a functional assay (liposome swelling assay) after the incorporation into proteoliposome according to Nikaido and Rosenberg.…”

Section: Preparation Of Hib and Salmonella Ompc Porinsmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Preparation Of Hib and Salmonella Ompc Porinsmentioning

confidence: 99%

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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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“…Thus, LPS is known to be one of the most potent stimuli of the immune system. Furthermore, it was found that porins may also stimulate cytokines such as interleukins and tumour necrosis factor a (Galdiero et al 1993(Galdiero et al , 2001(Galdiero et al , 2002Alurkar and Kamat 1997;Massari et al 2002).…”

Section: Introductionmentioning

confidence: 99%

Investigation into the interaction of the bacterial protease OmpT with outer membrane lipids and biological activity of OmpT:lipopolysaccharide complexes

et al. 2004

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Outer-membrane proteases T (OmpT) are important defence molecules of Gram-negative bacteria such as Escherichia coli found in particular in clinical isolates. We studied the interaction of OmpT with the membrane-forming lipids phosphatidylethanolamine (PE) and phosphatidylglycerol (PG) from the inner leaflet and lipopolysaccharide (LPS) from the outer leaflet of the outer membrane. These investigations comprise functional aspects of the protein-lipid interaction mimicking the outer-membrane system as well as the bioactivity of LPS:OmpT complexes in the infected host after release from the bacterial surface. The molecular interaction of the lipids PE, PG, and LPS with OmpT was investigated by analysing molecular groups in the lipids originating from the apolar region (methylene groups), the interface region (ester), and the polar region (phosphates), and by analysing the acyl-chain melting-phase behaviour of the lipids. The activity of OmpT and LPS:OmpT complexes was investigated in biological test systems (human mononuclear cells and Limulus amoebocyte lysate assay) and with phospholipid model membranes. The results show a strong influence of OmpT on the mobility of the lipids leading to a considerable fluidization of the acyl chains of the phospholipids as well as LPS, and a rigidification of the phospholipid, but not LPS head groups. From this, a dominant role of the protein on the function of the outer membrane can be deduced. OmpT released from the outer membrane still contains slight contaminations of LPS, but its strong cytokine-inducing ability in mononuclear cells, which does not depend on the Toll-like receptors 2 and 4, indicates an LPS-independent mechanism of cell activation. This might be of general importance for infections induced by Gram-negative bacteria.

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“…The OmpU insertion mutant (OMPUN) showed 47% reduction in luciferase activity compared with wild-type. Several studies have reported that porins from Gram-negative bacteria stimulated cells to produce IL-8 [33,34]. Yersinia enterocolitica outer membrane protein invasin triggered IL-8 in intestinal epithelial cells [35].…”

Section: Activation Of Il-8 Promoter Is Associated With Motility and mentioning

confidence: 99%

Interleukin‐8 gene regulation in epithelial cells by Vibrio cholerae: role of multiple promoter elements, adherence and motility of bacteria and host MAPKs

et al. 2012

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Interleukin (IL)-8 is an important mediator in neutrophil-mediated acute inflammation. We previously demonstrated that incubation of intestinal epithelial cells with Vibrio cholerae O395 resulted in increased IL-8 mRNA expression and IL-8 secretion, which was associated with the adherence and motility of bacteria. However, the mechanisms responsible for transcriptional regulation of the IL-8 gene in epithelial cells during V. cholerae infections were not explored. Transient transfection analysis of 5¢ deletions and mutations of the IL-8 promoter driving expression of the luciferase reporter gene indicates that multiple binding sites contribute to IL-8 promoter induction in response to V. cholerae and that cooperation among these different sites is required for full activation of the promoter. Stimulation with V. cholerae O395 insertional mutants, defective in adherence and motility, significantly reduced IL-8 promoter activity compared with the wild-type strain. We further demonstrate maximal involvement of extracellular signal-regulated kinase 1 ⁄ 2 ⁄ mitogen-activated protein kinase pathways to regulate IL-8 gene transcription. This study will help to design agents which could reduce the V. cholerae-induced inflammatory response and in the generation of safe vaccines.

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Porins from Salmonella enterica serovar Typhimurium induce TNF-α, IL-6 and IL-8 release by CD14-independent and CD11a/CD18-dependent mechanisms

Cited by 24 publications

References 52 publications

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

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

Investigation into the interaction of the bacterial protease OmpT with outer membrane lipids and biological activity of OmpT:lipopolysaccharide complexes

Interleukin‐8 gene regulation in epithelial cells by Vibrio cholerae: role of multiple promoter elements, adherence and motility of bacteria and host MAPKs

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