Biomedical subjects

S S Teuber

Publications and source records attributed to S S Teuber.

At least 19 recordsLinked to original sources

PubMed2005

Allergen immunotherapy with heat-killed Listeria monocytogenes alleviates peanut and food-induced anaphylaxis in dogs.

BACKGROUND: Heat-killed Listeria monocytogenes (HKL) potently stimulates interferon (IFN)-gamma production in CD4 T-lymphocytes, and when used as adjuvant for immunotherapy, reduces immunoglobulin (Ig)E production and reverses established allergen-induced airway hyperreactivity (AHR) in a murine model of asthma. We asked if such treatment could decrease established peanut-induced anaphylaxis or cow's milk-induced food allergy in highly food-allergic dogs. METHODS: We therefore studied four 4-year-old atopic colony dogs extremely allergic to peanut (Group I), as well as five 7-year-old dogs very allergic to wheat, milk and other foods (Group II). All dogs experienced marked allergic symptoms, including vomiting and diarrhea on oral challenge with the relevant foods. The dogs were then vaccinated once subcutaneously with peanut or milk and wheat with HKL emulsified in incomplete Freund's adjuvant. RESULTS: Following vaccination of the allergic dogs with HKL and allergen, oral challenges with peanut (Group I) or milk (Group II) elicited only minor or no symptoms. In addition, skin test end-point titrations showed marked reductions for >10 weeks after treatment, and levels of Ara h 1-specific IgE in serum of peanut sensitive dogs, as demonstrated by immunoblotting, were greatly reduced by treatment with HKL plus peanut allergen. CONCLUSIONS: Thus, HKL plus allergen treatment markedly improved established food allergic responses in dogs, suggesting that such an immunotherapy strategy in humans might greatly improve individuals with food allergy and anaphylaxis.

Allergens↗

PubMed2004

Extensive in vitro cross-reactivity to seed storage proteins is present among walnut (Juglans) cultivars and species.

BACKGROUND: Tree nuts, including English walnuts (Juglans regia), are sources of food allergens often associated with life-threatening allergic reactions. It is unknown if seed storage proteins from other Juglans species have IgE epitopes similar to those of the important English walnut allergens, Jug r 1 (2S albumin) and Jug r 2 (vicilin-like). OBJECTIVE: To screen for potential germplasm sources of hypoallergenic seed storage proteins of relevance in walnut food allergy. We sought to identify English walnut cultivars (cvs) or other Juglans species that showed decreased IgE binding to major seed storage proteins or an inability to cross-react with Jug r 1 or Jug r 2. METHODS: We determined if IgE in sera of patients who have had life-threatening systemic reactions to English walnut bound protein extracts from all tested walnut cvs (57 cvs total) or species (six) by Western immunoblot. Further, we used immunoblot inhibition to determine the in vitro cross-reactivity of Jug r 1 and Jug r 2, native and recombinant, with several walnut species. RESULTS: All walnut cvs and species contain allergenic proteins. Furthermore, as shown by in vitro immunoblot inhibition, the major walnut allergens in the species tested cross-reacted with those in J. regia cv. Chandler and J. nigra cv. Thomas extracts. CONCLUSIONS: Based on our findings, it is unlikely that a composite hypoallergenic walnut could be bred from available germplasm. In addition, patients with severe allergy to English walnut are likely to be clinically allergic to all commercial English walnut cvs and other closely related Juglans species.

2S Albumins, Plant↗

PubMed2002

Effects of roasting, blanching, autoclaving, and microwave heating on antigenicity of almond (Prunus dulcis L.) proteins.

Whole, unprocessed Nonpareil almonds were subjected to a variety of heat processing methods that included roasting (280, 300, and 320 degrees F for 20 and 30 min each; and 335 and 350 degrees F for 8, 10, and 12 min each), autoclaving (121 degrees C, 15 psi, for 5, 10, 15, 20, 25, and 30 min), blanching (100 degrees C for 1, 2, 3, 4, 5, and 10 min), and microwave heating (1, 2, and 3 min). Proteins were extracted from defatted almond flour in borate saline buffer, and immunoreactivity of the soluble proteins (normalized to 1 mg protein/mL for all samples) was determined using enzyme linked immunosorbent assay (ELISA). Antigenic stability of the almond major protein (amandin) in the heat-processed samples was determined by competitive inhibition ELISA using rabbit polyclonal antibodies raised against amandin. Processed samples were also assessed for heat stability of total antigenic proteins by sandwich ELISA using goat and rabbit polyclonal antibodies raised against unprocessed Nonpareil almond total protein extract. ELISA assays and Western blotting experiments that used both rabbit polyclonal antibodies and human IgE from pooled sera indicated antigenic stability of almond proteins when compared with that of the unprocessed counterpart.

Animals↗

PubMed2001

Electrophoretic and immunological analyses of almond (Prunusdulcis l.) genotypes and hybrids.

Aqueous extracts from sixty almond samples representing various genotypes and interspecies hybrids of almond, including almond-peach, were analyzed for protein and peptide content using electrophoresis, Western immunoblotting, and enzyme-linked immunosorbent assay (ELISA). Nondenaturing nondissociating polyacrylamide gel electrophoresis (NDND-PAGE) of the aqueous extracts indicated that a single major storage protein (almond major protein -- AMP or amandin) dominated the total soluble protein composition. Denaturing SDS--PAGE analyses of the aqueous extracts revealed that the AMP was mainly composed of two sets of polypeptides with estimated molecular masses in the ranges of 38--41 kDa and 20--22 kDa, regardless of the source; however, distinct variations in the intensity and electrophoretic mobility of some bands were noted between samples. In addition to AMP, several minor polypeptides were also present in all the genotypes, and variations were seen in these as well. Regardless of the genotype, AMP was recognized in Western blots by rabbit polyclonal anti-AMP antibodies, mouse monoclonal anti-AMP antibodies (mAbs), and serum IgE from patients displaying strong serum anti-almond IgE reactivity. As with protein staining results, antibody reactivity also revealed common patterns but displayed some variation between samples. An anti-AMP inhibition ELISA was used to quantify and compare aqueous extracts for various samples. All samples (n = 60) reacted in this assay with a mean +/- standard deviation (sigma n) = 0.82 +/- 0.18 when compared to reference aqueous extract from Nonpareil designated as 1.0.

Allergens↗

PubMed2001

Detection and stability of the major almond allergen in foods.

Almond major protein (AMP or amandin), the primary storage protein in almonds, is the major allergen recognized by almond-allergic patients. A rabbit antibody-based inhibition ELISA assay for detecting and quantifying AMP in commercial foods has been developed, and this assay, in conjunction with Western blotting analyses, has been applied to the investigation of the antigenic stability of AMP to harsh food-processing conditions. The ELISA assay detects purified AMP at levels as low as 87 +/-16 ng/mL and can detect almond at between 5 and 37 ppm in the tested foods. The assay was used to quantify AMP in aqueous extracts of various foods that were defatted and spiked with known amounts of purified AMP or almond flour. In addition, AMP was quantified in commercially prepared and processed almond-containing foods. Neither blanching, roasting, nor autoclaving of almonds markedly decreased the detectability of AMP in subsequent aqueous extracts of almonds. Western blots using both rabbit antisera and sera from human almond-allergic patients confirm a general stability of the various peptides that comprise this complex molecule and show that the rabbit antibody-based assay recognizes substantially the same set of peptides as does the IgE in sera from almond-allergic patients.

Allergens↗

PubMed2001

Walnut polyphenolics inhibit in vitro human plasma and LDL oxidation.

Recent epidemiologic studies have associated nut consumption with a reduced incidence of cardiovascular mortality. However, little is known about the contribution of nut polyphenols to antioxidant and cardiovascular protection. In this investigation, polyphenol-rich extracts from English walnuts (Juglans regia) were studied and compared with ellagic acid for their ability to inhibit in vitro plasma and LDL oxidation, as well as their effects on LDL alpha-tocopherol during oxidative stress. In addition, the Trolox equivalent antioxidant activity (TEAC) was determined and liquid chromatography electrospray detection mass spectrometry (LC-ELSD/MS) analyses of the walnut extracts were performed. 2,2'-Azobis'(2-amidino propane) hydrochloride (AAPH)-induced LDL oxidation was significantly inhibited by 87 and 38% with the highest concentration (1.0 micromol/L) of ellagic acid and walnut extract, respectively. In addition, copper-mediated LDL oxidation was inhibited by 14 and 84% in the presence of ellagic acid and walnut extract, respectively, with a modest, significant LDL alpha-tocopherol sparing effect observed. Plasma thiobarbituric acid reacting substance (TBARS) formation was significantly inhibited by walnut extracts and ellagic acid in a dose-dependent manner, and the extracts exhibited a TEAC value greater than that of alpha-tocopherol. LC-ELSD/MS analysis of the walnut extracts identified ellagic acid monomers, polymeric ellagitannins and other phenolics, principally nonflavonoid compounds. These results demonstrate that walnut polyphenolics are effective inhibitors of in vitro plasma and LDL oxidation. The polyphenolic content of walnuts should be considered when evaluating their antiatherogenic potential.

Adult↗

PubMed1999

Identification and cloning of a complementary DNA encoding a vicilin-like proprotein, jug r 2, from english walnut kernel (Juglans regia), a major food allergen.

BACKGROUND: Walnuts and other tree nuts are important food-allergen sources that have the potential to be associated with life-threatening, IgE-mediated systemic reactions in some individuals. OBJECTIVE: The purpose of this study was to characterize a complementary (c)DNA clone encoding one of the walnut food allergens. METHODS: A cDNA expression library prepared from walnut somatic embryo was screened for IgE reactivity with patient serum. A reactive clone of 2060 bp, which encoded a protein of 593 amino acids in length, was subcloned by excision into the pGEX expression vector. IgE-binding inhibition experiments were performed. RESULTS: A recombinant fusion protein was induced and shown to bind serum IgE from 9 of 15 patients tested, thus identifying a major allergen. This clone, named Jug r 2, exhibited significant homology with genes encoding the vicilin group of seed proteins. An IgE-binding inhibition experiment suggested that the encoded protein undergoes posttranslational modification into at least one major polypeptide (47 kd) and possibly several others, which is similar to the vicilin-like proteins characterized in cocoa bean (Theobroma cacao) and cottonseed (Gossypium hirsutum). N-terminal sequencing of the 47-kd band, Jug r 2, identified it as a mature protein obtained from the precursor. A second IgE-binding inhibition experiment showed that there is minimal or no cross-reactivity between Jug r 2 and pea vicilin, peanut proteins, or cacao proteins. CONCLUSION: Jug r 2 is the third vicilin food allergen identified in addition to vicilins from soy and peanut. The availability of recombinant food allergens should help advance studies on the immunopathogenesis and possible treatment of IgE-mediated food hypersensitivity.

Allergens↗

PubMed1999

Systemic allergic reaction to coconut (Cocos nucifera) in 2 subjects with hypersensitivity to tree nut and demonstration of cross-reactivity to legumin-like seed storage proteins: new coconut and walnut food allergens.

BACKGROUND: Two patients with tree nut allergy manifested by life-threatening systemic reactions reported the subsequent onset of systemic reactions after the consumption of coconut. OBJECTIVE: Herein, the IgE-binding proteins from coconut are described, and in vitro cross-reactivity with other nuts is investigated. METHODS: The IgE-binding profile of coconut endosperm tissue extract was analyzed by SDS-PAGE followed by immunoblotting. Immunoblot inhibition studies with walnut, almond, peanut, and coconut were performed. RESULTS: Sera IgE from both patients recognized reduced coconut allergens with molecular weights of 35 and 36.5 kd. IgE from 1 patient also bound a 55-kd antigen. Preabsorption of sera with nut extracts suppressed IgE binding to coconut proteins. Preabsorption of sera with coconut caused the disappearance of IgE binding to protein bands at 35 and 36 kd on a reduced immunoblot of walnut protein extract in 1 patient and suppression of IgE binding to a protein at 36 kd in the other patient. CONCLUSION: The reduced coconut protein at 35 kd was previously shown to be immunologically similar to soy glycinin (legumin group of seed storage proteins). The clinical reactivity in these 2 patients is likely due to cross-reacting IgE antibodies primarily directed against walnut, the original clinical allergy reported, and most likely to a walnut legumin-like protein. Coconut allergy in patients with tree nut allergy is rare; these are the first 2 patients ever reported, and therefore there is no general indication to advise patients with tree nut allergy to avoid coconut.

Adult↗

PubMed1999

An unproven technique with potentially fatal outcome: provocation/neutralization in a patient with systemic mastocytosis.

OBJECTIVE: To describe the risks associated with use of an unproven technique, provocation/neutralization, in diagnosis and treatment of a putative "food allergy" in a patient with systemic mastocytosis. METHODS: A case report of a 68-year-old woman with mastocytosis is reported. The patient was interviewed, examined, and all medical records were reviewed. Photos were taken, and skin and colonic biopsies were performed. RESULTS: The patient was previously diagnosed with urticaria pigmentosa but also had significant diarrhea that was well-controlled by oral cromolyn sodium. She saw a physician who practiced provocation/neutralization and was told that food allergies were the cause of her gastrointestinal symptoms. She was placed on "neutralizing" injections of milk and wheat, but experienced flushing, palpitations, and lightheadedness with syncope upon injections into her thigh, which is a skin area highly involved by visible lesions of cutaneous mastocytosis. Later evaluation revealed increased numbers of mast cells in her colonic mucosa as well as confirmation of cutaneous mastocytosis. CONCLUSIONS: The patient's previous history of urticaria pigmentosa, orally communicated by the patient, documented in medical records, and easily visible on physical examination, was discounted by a practitioner of an alternative and unproven medical treatment, provocation/neutralization. She subsequently had potentially life-threatening reactions to "provocative" skin testing and "neutralizing" injections. Patients with systemic mastocytosis are at risk for significant mast cell mediator release during immunotherapy, conventional or alternative.

Aged↗

PubMed1999

Production and characterization of rabbit polyclonal antibodies to almond (Prunus dulcis L.) major storage protein.

Rabbits were immunized with purified almond major protein (AMP), the primary storage protein in almonds. Rabbit anti-AMP polyclonal antibodies (PA) could detect AMP when as little as 1-10 ng/mL were used to coat microtiter plates in a noncompetitive enzyme linked-immunosorbent assay (ELISA). Competitive inhibition ELISA assays detected the AMP down to 300 ng/mL. PA recognized the AMP in protein extracts from all U.S. major marketing cultivars of almonds (Mission, Neplus, Peerless, Carmel, and Nonpareil) with specific reactivity of 52.6-75% as compared to that of the AMP alone. Immunoreactivity of protein extracts prepared from commercial samples of blanched almonds, roasted almonds, and almond paste was respectively reduced by 50.0%, 56.6%, and 68.4% (noncompetitive ELISA) when compared to the immunoreactivity of the AMP. Moist heat (121 degrees C, 15 min) pretreatment of the AMP reduced the PA reactivity by 87% (noncompetitive ELISA). Exposing AMP to pH extremes (12.5 and 1.5-2.5) caused a 53% and 57% reduction in PA reactivity, respectively (noncompetitive ELISA). PA showed some cross-reactivity with the cashew major globulin, and to a lesser extent, the Tepary and Great Northern bean major storage protein (7S or phaseolin). The presence of almonds in a commercial food was detected using PA in a competitive ELISA.

Allergens↗

PubMed1999

Severe migratory granulomatous reactions to silicone gel in 3 patients.

In humans implanted with silicone gel breast prostheses, a mild foreign body response results in the formation of a collagenous capsule around the prosthesis. Although many such patients may show evidence of a microscopic granulomatous foreign body reaction upon examination of capsular material at explantation of a prosthesis, it is unusual to have large, palpable granulomas, even in the presence of rupture or leakage. Rare patients have had severe local inflammation and complications resulting from silicone migration to the axilla, arm, or abdominal wall. We describe 3 patients who had deforming granulomas after implant rupture, along with other consequences of silicone gel migrating down the upper extremity. Silicone gel, once it leaves the implant, is not biologically inert and in some persons can elicit profound pathologic responses.

Adult↗

PubMed1998

Cloning and sequencing of a gene encoding a 2S albumin seed storage protein precursor from English walnut (Juglans regia), a major food allergen.

BACKGROUND: Walnuts rank third in per capita consumption of tree nuts in the United States and can be associated with systemic IgE-mediated reactions in some individuals. OBJECTIVE: The objectives of the study were to clone a gene encoding one of the major food allergens in the walnut kernel and to characterize the recombinant allergen. METHODS: A cDNA expression library in the lambda vector Uni-ZAP, which was prepared from walnut somatic embryos, was screened by using a patient's sera that reacted with multiple protein bands on immunoblotting. RESULTS: A cDNA clone containing an insert of 663 bp was identified and named Jug r 1. DNA sequence analysis of this clone revealed that it encoded a protein 142 amino acids in length. Comparison of the encoded protein sequences with protein databases revealed that this clone exhibits a 46.1% identity with the Brazil nut (Bertholletia excelsa) methionine-rich 2S albumin seed storage protein precursor, Ber e 1. Jug r 1 appears to be an important walnut food allergen; 12 of 16 sera from patients allergic to walnuts demonstrated IgE binding to the 2S albumin seed storage protein precursor fusion protein. An IgE-binding inhibition study suggests that the walnut 2S protein precursor undergoes posttranslational modification into a large and small subunit that is similar to castor seed, cottonseed, mustard seed, and Brazil nut 2S seed storage protein allergens. Interestingly, the gene encoding this allergenic protein in Brazil nuts has recently gained notoriety because of its experimental use as a transgene to enhance the nutritional quality of legumes. CONCLUSION: This is now the sixth definitive 2S albumin seed storage protein demonstrated to bind IgE, suggesting that this class of proteins is inherently allergenic.

2S Albumins, Plant↗

PubMed1997

Allergenicity of gourmet nut oils processed by different methods.

BACKGROUND: No information is available on allergenicity of tree nut oils, and information on peanut oils has been conflicting. Many of the nut oils now on the market undergo minimal processing and may contain residual antigen. OBJECTIVE: This study was carried out to determine whether several of the new "gourmet" tree nut oils, as well as peanut oils, contain residual proteins that could bind IgE from sera of patients with allergy. METHODS: Several brands of walnut, almond, hazelnut, pistachio, and macadamia nut oils were examined. Peanut oils, both unrefined oils (which have been shown to contain allergenic proteins) and refined oils (without previously demonstrable allergens), were also examined to confirm reproducibility of immunoreactivity as reported by other investigators. Oils were extracted with 0.2 mol/L ammonium bicarbonate, and protein concentrations in the aqueous extracts were measured. IgE binding was assayed by slot-blot and Western immunoblotting. Pooled sera from patients with a history of systemic reactions to various tree nuts or peanuts were used as appropriate. RESULTS: The oil extracts known to be from oils that had undergone less processing at lower temperatures tended to demonstrate qualitatively greater IgE binding and higher protein concentrations. CONCLUSIONS: Tree nut and peanut oils may pose a threat to patients with allergy, depending on the method of manufacture and processing.

Allergens↗

PubMed1996

Comparative epitope mapping of antibodies to collagen in women with silicone breast implants, systemic lupus erythematosus and rheumatoid arthritis.

Previous work has shown that women with silicone gel breast implants have an increased frequency of autoantibodies to collagen types I and II. 70 women without a specific autoimmune disease, using criteria of the American College of Rheumatology, but who had silicone breast implants were studied for the presence of serum antibodies to native and denatured human types I and II collagen by ELISA. 82 women with systemic lupus erythematosus (SLE), 94 women with rheumatoid arthritis (RA), and 133 healthy controls were also studied. There was a high frequency of autoantibodies to collagen in each of the groups when compared to the healthy controls. The specificities of these antibodies were found to differ markedly when examined by immunoblotting using peptides derived by cyanogen bromide digestion of the collagens. Sera from women with silicone implants reacted with multiple peptides of type I collagen in an individual-specific manner, but sera from women with SLE or RA reacted weakly with a restricted range of peptides. Against type II collagen, sera from women with RA reacted strongly with multiple peptides, while sera from women with silicone implants or SLE reacted only weakly or not at all. The patterns of reactivity against collagens by sera from women with silicone implants suggest that silicone can act as an adjuvant to enhance the immunogenicity of type I collagen.

Adult↗

PubMed1996

Serum silicon levels are elevated in women with silicone gel implants.

The metabolic fate of silicone gel leaked into the body from an implant is unknown. In this study, serum from 72 women with silicone gel breast implants and 55 control women was blindly assayed by inductively coupled plasma atomic emission spectroscopy (ICP-AES) for elemental silicon. Samples were processed using materials free of silicon. The mean silicon level in controls was 0.13 +/- 0.07 mg/l (range 0.06-0.35 mg/l), while in implant patients, the mean was significantly higher at 0.28 +/- 0.22 mg/l (range 0.06-0.87 mg/l) (P < 0.01, Student's t-test with correction for unequal variances). Using the mean of the control group + 2 SD as a cutoff for normal range (0.27 mg/l), 25/72 (34.7%) implant patients exceeded this value, compared with 2/55 (3.6%) controls. There was no significant correlation between past rupture of one or both implants, current rupture at the time of the blood draw or the number of years with implants and silicon levels. The results suggest that elevations of serum silicon are seen in many women with silicone gel breast implants. The kinetics of this elevation and the actual chemical species of the measured silicon remain to be determined.

Adult↗

PubMed1996

Lack of autoantibody expression in children born to mothers with silicone breast implants.

OBJECTIVE: We determined systematically the prevalence of autoantibodies in children born to mothers with silicone breast implants and the relationships with clinical symptoms and methods of exposure. METHODS: Autoantibody expression was determined in 80 children born to mothers with silicone implants and in 42 controls. A clinical assessment score was assigned to each patient. Antinuclear antibodies as well as antibodies to mitochondrial, smooth muscle, striational, myocardial, parietal cell, reticulin tissues, or subcellular compartments were measured by indirect fluorescent assay. Antibodies to nRNP (U1-RNP/snRNP); Sm; SS-A; SS-B; Scl-70; thyroid microsome; immunoglobulin (Ig)G, IgM, and IgA antibodies to cardiolipin; and antibodies to native and denatured human types I and II collagen were measured by enzyme-linked immunosorbent assay. Serum complement components C3 and C4 and IgM rheumatoid factor were measured by nephelometry. RESULTS: Autoantibody prevalence was not significantly different between children born to mothers with silicone implants and controls. The presence of autoantibodies was not related to the children's clinical symptoms or to the method of exposure. CONCLUSIONS: Determination of autoantibody production is of limited clinical utility in the evaluation of children born to mothers with silicone breast implants.

Adolescent↗

PubMed1996

Latex allergy.

Explore the source record for details and available documents.

Asthma↗

PubMed1995

Silicone breast implants: immunotoxic and epidemiologic issues.

Silicone gel implants for breast augmentation and reconstruction have been in use since 1962. Significant local complications include capsular contracture, rupture, gel "bleed", and spread of the implant material to regional lymph nodes (1-7) as well as histologic findings of foreign body granulomas in the capsular tissue and in lymph nodes (7-9). Through magnetic resonance spectroscopy and atomic emission spectroscopy, silicon compounds were found in the blood of some women with silicone breast implants; silicone and silica have also been found in liver (10). Well-publicized case reports have raised significant concerns regarding an association between implants and systemic disease. However, despite the availability of silicone implants for over 30 years, controlled epidemiological studies were not carried out until 1992. Currently available epidemiologic data are extremely limited. In part, because the majority of implants were used after 1981, the incidence of long-term problems is not yet known. In 1992, due to the unavailability of studies demonstrating the safety of implants, the U.S. Food and Drug Administration advised that silicone breast implants should be used only in reconstructive surgery and as part of clinical trials (11). This decision spurred a wave of research on the bioreactivity of silicone and clinical observations of patients with implants. Herein, we review the adverse immune effects following contact with silicone as well as the epidemiologic data available.

Animals↗