Enhancement of Growth of Virulent Strains of
            <i>Escherichia coli</i>
            by Interleukin-1

Porat, Reuven; Clark, Burton D.; Wolff, Sheldon M.; Dinarello, Charles A.

doi:10.1126/science.1833820

Cited by 176 publications

(127 citation statements)

References 21 publications

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“…3a and b show the results of SDS-PAGE and immunoblot analyses, respectively, of the bound and subsequently eluted protein complex. It can be seen from It has been reported that some Gram-negative bacteria produce a protein with IL-l-like activities [16]. We found that in a search of the PIR protein sequence library, Cafl shared the highest level of homology with hIL-lra (28% identity between aa 62 89 of Cafl and aa 57-85 of hIL-lra) [15].…”

Section: Competition Between Cafl and Hll-l~ For Binding To Caflamentioning

confidence: 66%

“…Each of these operons encode an outer membrane usher protein which facilitates surface localisation and correct assembly of virulence-associated surface organelles (capsules, pili, fimbriae). Porat et al [16] have found that IL-1 displays reactivity with virulent E. coli strains and increases the number of colony-forming entities. It was proposed that human IL-1 may recognize a functional IL-l-like receptor structure on virulent E. coli and may be a virulence factor for bacterial pathogenicity.…”

Section: Identification Of Cafla As Hll-l[~ Receptormentioning

confidence: 99%

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Specific high affinity binding of human interleukin 1β by Caf1A usher protein of Yersinia pestis

et al. 1995

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Section: Competition Between Cafl and Hll-l~ For Binding To Caflamentioning

confidence: 66%

Section: Identification Of Cafla As Hll-l[~ Receptormentioning

confidence: 99%

Specific high affinity binding of human interleukin 1β by Caf1A usher protein of Yersinia pestis

et al. 1995

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“…Findings that relate to the ability of AAT to inhibit bacterial expansion include binding to the bacterialessential furin (135), as well as undergoing S-nitrosylation in the presence of nitric oxide (136), both actions that are independent of protease inhibition. The observation that the virulence of E. coli is increased by IL-1 (137) suggests that blockade of IL-1 by AAT may interfere with bacterial growth, a finding corroborated by reduced numbers of live S. pneumoniae in infected mouse lungs (EC Lewis, unpublished observations). In this context, notably, the role of AAT in reducing bacterial load involves tissue modulation, that is, reducing the levels of tissue-derived bioactive IL-1.…”

Section: Aat Is An Antibacterialmentioning

confidence: 83%

Expanding the Clinical Indications for α1-Antitrypsin Therapy

Lewis

2012

Mol Med

147

115

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α 1 -Antitrypsin (AAT) is a 52-kDa circulating serine protease inhibitor. Production of AAT by the liver maintains 0.9-1.75 mg/mL circulating levels. During acute-phase responses, circulating AAT levels increase more than fourfold. In individuals with one of several inherited mutations in AAT, low circulating levels increase the risk for lung, liver and pancreatic destructive diseases, particularly emphysema. These individuals are treated with lifelong weekly infusions of human plasma-derived AAT. An increasing amount of evidence appears to suggest that AAT possesses not only the ability to inhibit serine proteases, such as elastase and proteinase-3 (PR-3), but also to exert antiinflammatory and tissue-protective effects independent of protease inhibition. AAT modifies dendritic cell maturation and promotes T regulatory cell differentiation, induces interleukin (IL)-1 receptor antagonist and IL-10 release, protects various cell types from cell death, inhibits caspases-1 and -3 activity and inhibits IL-1 production and activity. Importantly, unlike classic immunosuppressants, AAT allows undeterred isolated T-lymphocyte responses. On the basis of preclinical and clinical studies, AAT therapy for nondeficient individuals may interfere with disease progression in type 1 and type 2 diabetes, acute myocardial infarction, rheumatoid arthritis, inflammatory bowel disease, cystic fibrosis, transplant rejection, graft versus host disease and multiple sclerosis. AAT also appears to be antibacterial and an inhibitor of viral infections, such as influenza and human immunodeficiency virus (HIV), and is currently evaluated in clinical trials for type 1 diabetes, cystic fibrosis and graft versus host disease. Thus, AAT therapy appears to have advanced from replacement therapy, to a safe and potential treatment for a broad spectrum of inflammatory and immune-mediated diseases.

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“…The authors proposed that monocytes in CD14-deficient mice were not activated by bacteria due to lack of mCD14, and this in turn reduced production of inflammatory cytokines, such as TNF-a and IL-1, which accelerate growth of bacteria [25,32]. The authors postulated that reagents capable of blocking or neutralizing mCD14 on monocytes might also inhibit growth of Gram-negative bacteria.…”

Section: Discussionmentioning

confidence: 99%

Recombinant bovine soluble CD14 reduces severity of experimental Escherichia coli mastitis in mice

Lee

Paape²,

Zhao

2003

Vet. Res.

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-Endotoxin, or lipopolysaccharide (LPS), is responsible for pathogenesis of infections induced by Gram-negative bacteria, such as E. coli. The cellular response to LPS is modulated by interactions among LPS, LPS-binding protein (LBP) and CD14. Accumulated evidence shows that the soluble form of CD14 (sCD14) competes with membrane-bound CD14 (mCD14) for LPS and plays a pivotal role in regulating bacterial infection and septic shock caused by Gram-negative bacteria. Recombinant bovine sCD14 (rbosCD14) was produced by transfected insect sf/9 cells and its biological function was evaluated in mice. Eighty-one 8-week old BALB/cj female mice were randomly assigned to two groups, and injected intraperitoneally with either LPS (8 mg/g of body weight, n = 41) or LPS plus rbosCD14 (6.8 mg/g of body weight, n = 40). Survival rate at 24 h after injection for mice injected with either LPS or LPS plus rbosCD14 was 30 and 72%, respectively (P < 0.01). At 48 h survival rate was 7 and 37%, respectively (P < 0.01). To investigate the protective effect of rbosCD14 on experimentally induced mastitis in mice, two abdominal contralateral mammary glands of 7 lactating BALB/cj mice were injected through the teat canal with 10-20 colony-forming units (CFU) of Escherichia coli. One gland simultaneously received rbosCD14 (6 mg) and the other saline. At 24 h after challenge, glands that received rbosCD14 had less swelling and hemorrhaging, significantly lower bacterial counts (P < 0.05) and lower concentrations of TNF-a (P < 0.05). Results indicate that rbosCD14 is biologically functional and reduces mortality in mice from endotoxin shock and severity of intramammary infection by E. coli. mastitis / CD14 / LPS / Escherichia coli / TNF-a

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Enhancement of Growth of Virulent Strains of Escherichia coli by Interleukin-1

Cited by 176 publications

References 21 publications

Specific high affinity binding of human interleukin 1β by Caf1A usher protein of Yersinia pestis

Specific high affinity binding of human interleukin 1β by Caf1A usher protein of Yersinia pestis

Expanding the Clinical Indications for α1-Antitrypsin Therapy

Recombinant bovine soluble CD14 reduces severity of experimental Escherichia coli mastitis in mice

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