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Results for “STING Protein”

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PubMed2002

Value of the plasma protein and hemoglobin concentration in the diagnosis of pulmonary edema in scorpion sting patients.

OBJECTIVE: To investigate the value of measuring total plasma protein and hemoglobin concentrations for the diagnosis of pulmonary edema secondary to scorpion envenomation. DESIGN AND SETTING: Retrospective study over a 4-year period in the medical intensive care unit of a university hospital. PATIENTS: 67 patients older than 3 years admitted in the intensive care unit for scorpion envenomation and stratified into two groups according to the presence of pulmonary edema assessed by a medical committee that took into account clinical, radiological, and blood gas data at admission and after treatment. Total plasma protein and hemoglobin concentrations were analyzed separately. RESULTS: At admission all patients with and without pulmonary edema exhibited polypnea and tachycardia. The mean plasma protein and hemoglobin concentrations were higher in patients with pulmonary edema (74+/-6 and 14.2+/-2.0 g/dl, respectively) than in those without pulmonary edema (64+/-6 and 12.3+/-1.4 g/dl). After 24 h plasma protein and hemoglobin concentrations decreased in the pulmonary edema group (-11 and -1.9 g/dl) despite a negative fluid balance (-500 ml). A plasma protein concentration of 70 g/l or more predicted the presence of pulmonary edema with a sensitivity of 80% a specificity of 96%, a positive predictive value of 97%, and negative predictive value of 77%. CONCLUSIONS: In scorpion-envenomed patients with cardiorespiratory manifestations high plasma protein and hemoglobin concentrations suggest the presence of pulmonary edema.

Adolescent↗
PubMed1983

Antibodies to purified bee venom proteins and peptides. I. Development of a highly specific RAST for bee venom antigens and its application to bee sting allergy.

IgE antibodies to purified proteins and peptides from honeybee venom have been measured by the RAST. Trace amounts (less than 0.1%) of the major venom protein phospholipase A2 (PLA2) grossly distorted the measurement of IgE antibody to the other venom proteins, acid phosphatase (Acid P) and hyaluronidase (HYAL), and overemphasized their importance. Reduction of antigen coupled to the cellulose paper discs, which were used in the assay, diluted out the contaminating PLA2 without apparent loss in sensitivity. The reduction of disc-bound antigen increased the competition between IgE and IgG antibodies but did not affect measurement of IgE antibodies in sera taken from 35 untreated patients who had a history of general allergic reactions to bee stings. In 54% of sera from bee venom--allergic patients, the greatest IgE antibody response was to PLA2. In all, IgE antibodies to PLA2 were present in 91% of these sera. IgE antibodies to Acid P, HYAL, or melittin were present in 60%, 51%, and 31% of sera, respectively, and accounted for the highest level of binding in 17%, 17%, and 6% of these. Only 6% of sera were positive for whole venom but negative for the isolated antigens. A low level of IgE antibody was found to peptide 401 in 6% of sera. No IgE antibodies were found to apamin. While confirming the central role played by PLA2 in bee sting allergy, these results show that other venom components are also important in some patients.

Acid Phosphatase↗
PubMed1989

Isolation of immunoglobulin G by affinity chromatography using an IgG Fc receptor protein from Streptococcus dysgalactiae coupled to a solid phase.

A culture of Streptococcus dysgalactiae (C 26) was shown to bind only to 125I-IgG, whereas another S. dysgalactiae culture (C 12) bound both 125I-IgG and 125I-albumin. The IgG-binding proteins could be readily solubilized by lysozyme treatment of the bacteria and isolated by affinity chromatography on IgG Sepharose. The purified IgG-binding protein from S. dysgalactiae C 26, which lacked simultaneous albumin binding activity, precipitated with IgG preparations from man, cow, horse, pig and mouse but not with chicken IgG. This IgG-binding protein was coupled to CNBr-activated Sepharose and subsequently used for the purification of IgG from both bovine and human serum. SDS-PAGE and immunoelectrophoretic studies confirmed the purity of the eluted proteins.

Animals↗
PubMed2026

Mycobacterium tuberculosis Rv0158 negatively regulates the cGAS-STING pathway mediated type I IFN production and enhances intracellular survival.

BACKGROUND: Type I interferons (IFN) play an important role in the host defense against Mycobacterium tuberculosis (M. tb) infection and disease pathogenesis. Although M. tb has evolved several mechanisms to evade host immune surveillance, the mechanism used to regulate type I IFN expression remains unclear. METHODS: In this study, genome-wide high-throughput loss-of-function screening was performed to screen M. tb determinants that regulate the Type I IFN pathway, and the role for M. tb Rv0158 in inhibiting type I IFN responses was identified in vitro and in vivo. RESULTS: The M. tb coding protein Rv0158 was identified among many transposon (Tn) insertion mutants, which increased the expression of IFN-β and some pro-inflammatory cytokines. The results suggested that Rv0158 is associated with reduced STING protein levels and suppression of cGAS-STING-mediated innate immune responses, suggesting that Rv0158 may indirectly facilitate STING degradation or modulate its stability through host-interacting partners. Rv0158 also down-regulated the transcription of interferon-stimulated genes (ISGs) and increased the bacterial load in mice. CONCLUSION: Overall, our finding identified a new bacterial factor Rv0158, these results reveal an important role for M. tb Rv0158 in inhibiting Type I IFN responses, which improves our understanding of the immune evasion mechanisms of M. tb.

Immune escape↗
PubMed2026

Cell-type specific activation of the cGAS-STING pathway in tumor immunotherapy: mechanisms and therapeutic implications.

BACKGROUND: The cyclic GMP–AMP synthase–stimulator of interferon genes (cGAS–STING) pathway acts as a pivotal innate immune sensor that detects cytosolic DNA and links genomic instability to antitumor immune activation. Therapeutic activation of this pathway has garnered substantial interest as a strategy to enhance cancer immunotherapy by promoting dendritic cell maturation, augmenting antigen presentation, and facilitating cytotoxic lymphocyte infiltration. However, the functional outcomes of cGAS–STING signaling are highly context dependent and influenced by both cell type and tumor microenvironmental (TME) conditions. MAIN BODY: Recent advances in single-cell and spatial transcriptomic profiling have revealed profound heterogeneity in cGAS–STING activation across distinct cellular and regional compartments within tumors. Acute and spatially restricted activation of the pathway can elicit potent antitumor immune responses, whereas chronic or dysregulated signaling may promote immune tolerance and tumor progression. Moreover, metabolic stress, epigenetic silencing, and microenvironmental immunosuppressive factors such as TGF-β and IL-10 can further modulate STING activity, leading to resistance to immunotherapy. Current translational efforts focus on next-generation STING agonists, nanoparticle-based delivery systems, and rational combination strategies with immune checkpoint blockade and metabolic modulators to overcome tumor-intrinsic resistance and minimize systemic toxicity. CONCLUSIONS: Understanding the cell-type-specific and spatial dynamics of cGAS–STING signaling is crucial for the rational design of precision immunotherapies. Future research should emphasize context-dependent modulation of STING activity to maximize therapeutic benefit while limiting adverse effects. Integrating multi-omics technologies and spatially guided drug delivery may ultimately enable personalized modulation of the cGAS–STING axis, transforming it into a clinically effective and safe strategy for cancer immunotherapy.

Humans↗
PubMed2000

Signal transduction. N-WASP regulation--the sting in the tail.

Signaling proteins can be regulated by their interactions with other proteins and phospholipids. As Fawcett and Pawson discuss in their Perspective, activation of the N-WASP protein (which coordinates formation of actin filaments) is far more complex, depending on the interaction of N-WASP with both a protein and a phospholipid. The authors explain new results (Prehoda et al.) demonstrating that cooperative binding of the phospholipid PIP2 and the small GTPase Cdc42 to N-WASP results in its activation. The Arp2/3 complex is then able to bind to N-WASP and to proceed with its job of initiating the assembly of actin monomers into actin filaments.

Actin Cytoskeleton↗
PubMed2026

Typhoid Toxin of Salmonella enterica Induces ISG15 Responses Mediating Host Cell Survival and Counteracting Intracellular Infection.

The typhoid toxin is a secreted virulence factor of typhoidal serovars of the bacterial pathogen Salmonella enterica implicated in typhoid fever and chronic infections. The toxin causes a DNA damage response in human cells, characterised by cell-cycle arrest and cellular distension, resulting in cellular senescence and increased bacterial burden. To better understand host responses to typhoid toxin, we performed a transcriptomic analysis of intoxicated host cells and found that the toxin induced expression of genes relating to the type-I interferon response, including the ubiquitin-like protein ISG15. ISG15 was upregulated in a STING-dependent manner, reduced bacterial burden, and was found to be critical to host cell survival in response to the typhoid toxin and interferon. This highlights ISG15 as an important component of the host cell defence to the typhoid toxin.

Humans↗
PubMed2026

VHL synthetic lethality screens uncover CBF-β as a negative regulator of STING.

Clear cell renal cell carcinoma (ccRCC) represents the most common form of kidney cancer and is typified by biallelic inactivation of the von Hippel-Lindau (VHL) tumour suppressor gene. Here, we undertake genome-wide CRISPR/Cas9 screening to reveal synthetic lethal interactors of VHL, and uncover that loss of Core Binding Factor β (CBF-β) causes cell death in VHL-null ccRCC cell lines and impairs tumour establishment and growth in vivo. This synthetic relationship is independent of the elevated activity of hypoxia inducible factors (HIFs) in VHL-null cells, but does involve the RUNX transcription factors that are known binding partners of CBF-β. Mechanistically, CBF-β loss leads to upregulation of type I interferon signalling, and we uncover a direct inhibitory role for CBF-β at the STING locus controlling Interferon Stimulated Gene expression. Targeting CBF-β in kidney cancer both selectively induces tumour cell lethality and promotes activation of type I interferon signalling.

Humans↗
PubMed1996

Comparison of proteins, IgE, and IgG binding antigens, and skin reactivity in commercial and laboratory-made mosquito extracts.

BACKGROUND: Commercial extracts are available for the diagnosis and treatment of mosquito allergy, but their antigen content has never been analyzed. OBJECTIVE: We wanted to analyze commercially available mosquito extracts and to compare these extracts with different laboratory preparations. METHODS: Seven commercially available mosquito whole body extracts from six companies and four laboratory mosquito preparations including saliva extract were studied. Epicutaneous tests and measurement of protein concentration were performed. Protein components were identified by sodium sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and silver stain. IgE and IgG binding antigens were analyzed by SDS-PAGE and immunoblotting with sera from mosquito-allergic subjects. RESULTS: The seven commercial materials produced wheals and papules ranging from 0 to 36 mm2. Their protein concentrations varied from 0.1 to 4.9 mg/mL. There were significant differences in their protein and antigen components. Some extracts contained multiple highly immunoreactive proteins and IgE- and IgG-binding antigens that are not present in mosquito saliva, but few actual salivary antigens. In the four laboratory preparations, rank ordered from whole body, head and thorax, salivary gland to saliva extracts, the amount of salivary antigens significantly increased, while non-salivary proteins and antigens significantly decreased. CONCLUSIONS: Commercial mosquito extracts should be standardized. Purer mosquito extracts should be used in diagnosis and immunotherapy of mosquito allergy.

Aedes↗
PubMed2000

[The wasp-mosquito syndrome: extension of cross-allergenicity to the horsefly].

The crossed allergenicity between wasp venom and mosquito extract was shown during recent work based on clinical observations and correlation studies between different biological parameters, indicating an IgE-dependent biological mechanism. A common protein was identified by Immunoblot. From observation of one of our patients involved in this work, we examined the possibility of the extension of crossed reactivity between wasp, mosquito and horsefly. In effect, our patient presented an anaphylactic reaction with neurological complications from attack on the central grey nucleus, shown by IRM; the immunological study showed a common protein between wasp venom and the total extracts of mosquito and horsefly.

Adult↗
PubMedDate not supplied

Mosquito bite hypersensitivity.

We report a patient who experienced systemic anaphylaxis after several mosquito bites. The skin tests were positive, by prick and intradermal tests, with two species of common mosquito (Aedes communis and Culex pipiens) and also with red midge larvae (Chironomus). Specific IgE against Aedes communis was demonstrated. We carried out SDS-PAGE and immunoblotting with whole body extracts of Aedes communis and Culex pipiens and with red midge larvae. The immunoblotting results showed specific IgE against two proteins of approximately 30 kDa with the extract of Culex pipiens. We also found IgE against one protein of a slightly lower molecular weight with Aedes communis, and against several proteins (the most important with a molecular weight between 30 and 70 kDa) with the Chironomus extract. Cross-reactivity between these insect species was suspected.

Adult↗
PubMed2001

Identification, cloning, and recombinant expression of procalin, a major triatomine allergen.

Among the most frequent anaphylactic reactions to insects are those attributed to reduviid bugs. We report the purification and identification of the major salivary allergen of these insects. This 20-kDa protein (procalin) is a member of the lipocalin family, which includes salivary allergens from other invertebrates and mammals. An expression system capable of producing reagent quantities of recombinant allergen was developed in Saccharomyces cerevisiae. Antisera produced against recombinant protein cross-reacts with ELISA with salivary allergen. Recombinant Ag is also shown to react with sera from an allergic patient but not with control sera. By immunolocalization, the source of the salivary Ag is the salivary gland epithelium and its secretions.

Allergens↗
PubMed2006

Equine insect bite hypersensitivity: immunoblot analysis of IgE and IgG subclass responses to Culicoides nubeculosus salivary gland extract.

Insect bite hypersensitivity (IBH) is an allergic dermatitis of horses caused by IgE-mediated reactions to bites of Culicoides and sometimes Simulium spp. The allergens causing IBH are probably salivary gland proteins from these insects, but they have not yet been identified. The aim of our study was to identify the number and molecular weight of salivary gland extract (SGE) proteins derived from Culicoides nubeculosus which are able to bind IgE antibodies (ab) from the sera of IBH-affected horses. Additionally, we sought to investigate the IgG subclass (IgGa, IgGb and IgGT) reactivity to these proteins. Individual IgE and IgG subclass responses to proteins of C. nubeculosus SGE were evaluated by immunoblot in 42 IBH-affected and 26 healthy horses belonging to different groups (Icelandic horses born in Iceland, Icelandic horses and horses from different breeds born in mainland Europe). Additionally, the specific antibody response was studied before exposure to bites of Culicoides spp. and over a period of 3 years in a cohort of 10 Icelandic horses born in Iceland and imported to Switzerland. Ten IgE-binding protein bands with approximate molecular weights of 75, 66, 52, 48, 47, 32, 22/21, 19, 15, 13/12 kDa were found in the SGE. Five of these bands bound IgE from 50% or more of the horse sera. Thirty-nine of the 42 IBH-affected horses but only 2 of the 26 healthy horses showed IgE-binding to the SGE (p<0.000001). Similarly, more IBH-affected than healthy horses had IgGa ab binding to the Culicoides SGE (19/22 and 9/22, respectively, p<0.01). Sera of IBH-affected horses contained IgE, IgGa and IgGT but not IgGb ab against significantly more protein bands than the sera of the healthy horses. The cohort of 10 Icelandic horses confirmed these results and showed that Culicoides SGE specific IgE correlates with onset of IBH. IBH-affected horses that were born in Iceland had IgGa and IgGT ab (p< or =0.01) as well as IgE ab (p=0.06) against a significantly higher number of SGE proteins than IBH-affected horses born in mainland Europe. The present study shows that Culicoides SGE contains at least 10 potential allergens for IBH and that IBH-affected horses show a large variety of IgE-binding patterns in immunoblots. These findings are important for the future development of a specific immunotherapy with recombinant salivary gland allergens.

Animals↗
PubMed1988

Circulating antibody detection in human serum to mosquito salivary gland proteins by the avidin-biotin-peroxidase technique.

Serum was collected from individuals with little, average, or extensive exposure to mosquito bites for determination of the presence of circulating antibodies to mosquito salivary gland proteins. Intensity of exposure was determined by mosquito-bite and exposure history. Sections cut through the thorax of four different species of mosquitoes, locally prevalent in South Florida, were exposed to serum and developed for antibody binding with the use of the avidin-biotin-peroxidase immunohistochemical technique. In subjects with histories of little or average exposure to mosquitoes, binding was observed that appeared to be species-specific; in subjects with extensive exposures, little antibody binding to salivary gland was noted. We hypothesize that suppression of the humoral immune response is an adaptive mechanism in response to significant exposures of mosquito salivary gland antigens.

Animals↗
PubMed2004

Cloning and sequencing of a cDNA expressing a ribosomal P0 peptide from Culicoides nubeculosus (Diptera).

Insect bite dermal hypersensitivity (IBH) is an allergic dermatitis of horses caused by bites of Culicoides spp. and sometimes Simulium spp. The aim of the investigation presented here was to identify allergens causing IBH. A cDNA library expressing recombinant Culicoides nubeculosus proteins was screened using affinity-purified serum from an IBH-affected horse. Screening of the library resulted in identification of one immunoreactive clone. The sequence of the cDNA insert was determined and revealed a 600 bp insert with an open reading frame coding for a 78 amino acid long protein, called rCul n 1. Analysis of the deduced amino acid sequence revealed an identity of 67-78% to the C-terminal part of the 318 amino acid long ribosomal P0 protein from other Diptera. Furthermore, the 38 C-terminal amino acids displayed an identity of 57% with the C-terminal part of the acidic ribosomal protein P2 from Aspergillus fumigatus. The cDNA insert was subcloned and expressed as a [His]6-tagged protein in Escherichia coli and purified using Ni2(+)-chelate affinity chromatography. The 10kDa recombinant Cul n 1 protein bound the affinity-purified antibody fraction used for screening the expression library. Determination of IgE and IgG levels against rCul n 1 by ELISA in sera from 19 IBH-affected and 18 Swiss control horses and in sera from eight control horses living in Iceland showed no significant differences between the three groups of horses (median IgE levels = 60, 49 and 44 relative ELISA units, respectively). rCul n 1 did not induce sulfidoleukotriene (sLT) release from peripheral blood leukocytes of IBH-affected horses (N = 5), although sLT release was induced with the Culicoides whole body extract.

Allergens↗