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PubMed1993

Stage-specific binding of peanut agglutinin to aggregates of degenerating photoreceptor cells in the rd mouse retina.

Peanut agglutinin, a lectin with high binding affinity for galactose-galactosamine disaccharide, was used to monitor changes in the photoreceptor cell layer of mice with inherited retinal degeneration. Mice homozygous for the retinal degeneration (rd) gene exhibit a rapid loss of rod photoreceptor cells in the first postnatal month. Previous studies have shown that aggregates of peanut agglutinin-binding cells are observed in the outer nuclear layer in the retinal degenerative mouse at between postnatal days 10 and 18, a period during which massive photoreceptor degeneration occurs in this mutant. This study was performed to determine whether these peanut agglutinin-positive cell clusters represent degenerating photoreceptor cells or, alternatively, macrophages that have migrated into the photoreceptor cell layer. Electron microscopic cytochemistry, using horseradish-peroxidase-conjugated peanut agglutinin, was used to trace cellular processes of peanut-agglutinin-stained cell clusters. Additionally, macrophage-specific antibodies were employed to determine whether macrophages were present in the clusters. The cell clusters did not react with macrophage-specific antibodies. However, processes of cells in peanut-agglutinin-bound clusters could be traced by electron microscopic serial sections to both the outer limiting membrane and the outer synaptic layer. These results provide strong evidence that peanut-agglutinin-bound cells seen during this stage of degeneration in the rd mouse are degenerating photoreceptor cells. Since peanut agglutinin has been shown to bind preferentially to cone, but not to rod, photoreceptor cells, the results also suggest that the clusters may be aggregates of degenerating cones.

Animals↗

PubMed1991

Effects of denervation on the distribution of peanut agglutinin binding molecules in frog muscles.

The extracellular matrix has been shown to play an important role in the differentiation of neuromuscular junctions during reinnervation in frogs. Peanut agglutinin, a lectin, is known to specifically bind to some glycoconjugates in the extracellular matrix at the frog neuromuscular junction and myotendinous junction. In order to determine if innervation has any role in regulating the specific binding of peanut agglutinin at neuromuscular junctions and myotendinous junctions, the distribution of peanut agglutinin binding was examined in muscles chronically denervated for various periods. Short-term denervated muscles (less than or equal to 2 months) showed no changes in peanut binding agglutinin binding at neuromuscular junctions and no extrajunctional binding. In contrast, long-term denervation (greater than 2 months - 7.5 months) resulted in altered peanut agglutinin distribution and a substantial reduction or a total loss in its binding at denervated neuromuscular junctions; binding at myotendinous junctions was not affected. Results of electron microscopic studies suggest that the presence of Schwann cells at denervated endplates delays the loss of peanut agglutinin binding. Reinnervation restores normal peanut agglutinin binding at neuromuscular junctions following long-term denervation. This report demonstrates that although the distribution of peanut agglutinin binding molecules is unchanged short-term denervation, intact innervation is necessary for the long-term maintenance of these molecules at neuromuscular junctions.

Animals↗

PubMed2005

A genetic engineering strategy to eliminate peanut allergy.

Peanut allergy is an IgE-mediated hypersensitivity reaction with an increasing prevalence worldwide. Despite its seriousness, to date, there is no cure. Genetic engineering strategies can provide a solution. The post-transcriptional gene silencing (PTGS) model can be used effectively to knock out the production of allergenic proteins in peanut by specific degradation of the endogenous target messenger RNA (mRNA). Ara h 2, the most potent peanut allergenic protein, was selected as a model to demonstrate the feasibility of this concept. Transgenic peanut plants were produced via microprojectile-mediated transformation of peanut embryos using a plasmid construct, which contains a fragment of the coding region of Ara h 2 linked to an enhanced CaMV 35S constitutive promoter. Molecular analyses, including polymerase chain reaction and Southern blots, confirmed the presence of the stable integration of the Ara h 2 transgene into the peanut genome. Northern hybridization showed the expression of the Ara h 2 transgene in all vegetative tissues of the mature transgenic peanut plants, indicating the stable expression of the truncated Ara h 2 transgene throughout the development of the plants. It is, therefore, reasonable to expect that the truncated Ara h 2 transgene transcripts will be synthesized in the seeds and will trigger the specific degradation of endogenous Ara h 2 mRNA. The next step will be to grow the transgenic peanut plants to full maturity for seed production and to determine the level of allergen Ara h 2.

Arachis↗

PubMed2005

The Chinese herbal medicine formula FAHF-2 completely blocks anaphylactic reactions in a murine model of peanut allergy.

BACKGROUND: Peanut allergy is potentially life threatening. There is no curative therapy for this disorder. We previously found that an herbal formula, food allergy herbal formula (FAHF)-1, blocked peanut-induced anaphylaxis in a murine model when challenged immediately posttherapy. OBJECTIVE: To test whether FAHF-2, an improved herbal formula, from which 2 herbs, Zhi Fu Zi (Radix Lateralis Aconiti Carmichaeli Praeparata) and Xi Xin (Herba Asari), were eliminated, is equally effective to FAHF-1, and if so, whether protection persists after therapy is discontinued. METHODS: Mice allergic to peanut treated with FAHF-2 for 7 weeks were challenged 1, 3, or 5 weeks posttherapy. Anaphylactic scores, core body temperatures, vascular leakage, and plasma histamine levels after peanut challenge were determined. Serum peanut-specific antibody levels and splenocyte cytokine profiles were also measured. RESULTS: After challenges, all sham-treated mice developed severe anaphylactic signs, significant decrease in rectal temperatures, significantly increased plasma histamine levels, and marked vascular leakage. In contrast, no sign of anaphylactic reactions, decrease in rectal temperatures, or elevation of plasma histamine levels was observed in FAHF-2-treated mice in 5 separate experiments. IgE levels were significantly reduced by FAHF-2 treatment and remained significantly lower as long as 5 weeks posttherapy. Splenocytes from FAHF-2-treated mice showed significantly reduced IL-4, IL-5, and IL-13, and enhanced IFN-gamma production to recall peanut stimulation in vitro . CONCLUSION: FAHF-2 treatment completely eliminated anaphylaxis in mice allergic to peanut challenged as long as 5 weeks posttherapy. This result was associated with downregulation of T H 2 responses. FAHF-2 may be a potentially effective and safe therapy for peanut allergy.

Administration, Oral↗

PubMed2006

Predictive value of skin prick tests using recombinant allergens for diagnosis of peanut allergy.

BACKGROUND: Current diagnosis of peanut allergy relies on natural extracts that lack standardization. Recombinant DNA technology allows production of pure biochemically characterized proteins. Their usefulness for peanut allergy diagnosis is not established. OBJECTIVE: This study aimed to evaluate the diagnostic value of the 3 major recombinant peanut allergens. METHODS: Recombinant (r) Ara h 1, rAra h 2, and rAra h 3 were produced according to the recommendations of good manufacturing practice for recombinant allergens. Skin prick tests (SPTs) and IgE ELISA assays were performed in 30 patients with peanut allergy and 30 control subjects without food allergy: 15 nonatopic and 15 sensitized to birch pollen. Disease severity was graded by clinical scoring. RESULTS: All patients with peanut allergy showed positive SPT results to rAra h 2; 40% reacted with rAra h 1 and 27% with rAra h 3. No control subjects reacted with any of the recombinant allergens. Monosensitization to rAra h 2 was observed in 53% of patients. Neither SPT size nor levels of specific IgE were correlated with the disease severity. However, patients with monosensitization to rAra h 2 had a significantly lower severity score than polysensitized subjects and a lower level of specific IgE against peanut extract and rAra h 2. CONCLUSION: Skin prick tests to individual recombinant peanut allergens appear to be a safe and effective diagnostic tool. Cosensitization to rAra h 2 and rArah 1 and/or rAra h 3 is predictive of more severe reactions. CLINICAL IMPLICATIONS: Recombinant peanut allergens can be used by SPTs for diagnosis and evaluation of allergy severity.

Adolescent↗

PubMed2005

Oral and nasal sensitization promote distinct immune responses and lung reactivity in a mouse model of peanut allergy.

Despite structural and functional differences between the initial sites of contact with allergens in the gastrointestinal and nasal tracts, few animal models have examined the influence of the mucosal routes of sensitization on host reactivity to food or environmental antigens. We compared the oral and nasal routes of peanut sensitization for the development of a mouse model of allergy. Mice were sensitized by administration of peanut proteins in the presence of cholera toxin as adjuvant. Antibody and cytokine responses were characterized, as well as airway reactivity to nasal challenge with peanut or unrelated antigens. Oral sensitization promoted higher levels of IgE, but lower IgG responses, than nasal sensitization. Both orally and nasally sensitized mice experienced airway hyperreactivity on nasal peanut challenge. The peanut challenge also induced lung eosinophilia and type 2 helper T-cell-type cytokines in orally sensitized mice. In contrast, peanut challenge in nasally sensitized mice promoted neutrophilia and higher levels of lung MAC-1(+) I-A(b low) cells and inflammatory cytokines. In addition, nasal but not oral, sensitization promoted lung inflammatory responses to unrelated antigens. In summary, both oral and nasal peanut sensitization prime mice for airway hyperreactivity, but the initial mucosal route of sensitization influences the nature of lung inflammatory responses to peanut and unrelated allergens.

Animals↗

PubMed2004

Allergenic properties of roasted peanut allergens may be reduced by peroxidase.

Peanut allergy is a public health issue. The culprits are the peanut allergens. Reducing the allergenic properties of these allergens or proteins will be beneficial to allergic individuals. In this study, the objective was to determine if peroxidase (POD), which catalyzes protein cross-linking, reduces the allergenic properties of peanut allergens. In the experiments, protein extracts from raw and roasted defatted peanut meals at pH 8 were incubated with and without POD in the presence of hydrogen peroxide at 37 degrees C for 60 min. The POD-treated and untreated samples were then analyzed by SDS-PAGE, western blots, and competitive inhibition ELISA. IgE binding or allergenicity was determined in blots and ELISA. Results showed that POD treatment had no effect on raw peanuts with respect to protein cross-linking. However, a significant decrease was seen in the levels of the major allergens, Ara h 1 and Ara h 2, in roasted peanuts after POD treatment. Also, polymers were formed. Despite this, a reduction in IgE binding was observed. It was concluded that POD induced the cross-linking of mainly Ara h 1 and Ara h 2 from roasted peanuts and that, due to POD treatment, IgE binding was reduced. The finding indicates that POD can help reduce the allergenic properties of roasted peanut allergens.

Allergens↗

PubMed1999

Allergenicity of Maillard reaction products from peanut proteins.

It is known that peanut allergy is caused by peanut proteins. However, little is known about the impact of roasting on the allergenicity of peanuts. During roasting, proteins react with sugars to form Maillard reaction products, which could affect allergenicity. To determine if the Maillard reaction could convert a nonallergenic peanut protein into a potentially allergenic product, nonallergenic lectin was reacted with glucose or fructose at 50 degrees C for 28 days. Browning products from heat-treated peanuts were also examined. The products were analyzed in immunoblot and competitive assays, using a pooled serum (i.e., IgE antibodies) from patients with peanut anaphylaxis. Results showed that the products were recognized by IgE and had an inhibitory effect on IgE binding to a peanut allergen. Thus, the findings suggest that these Maillard reaction products are potentially allergenic and indicate the need to verify whether the Maillard reaction products formed in peanuts during roasting increase their allergenicity.

Arachis↗

PubMed2006

Effects of peanut oil consumption on appetite and food choice.

OBJECTIVE: Peanut consumption may improve lipid profiles without promoting weight gain. Both properties have been attributed to their high-unsaturated fat content. Mono and polyunsaturated fatty acids reportedly hold stronger satiety value than saturated fats and may help appetite control. This study investigated the effects of chronic peanut oil consumption on appetite and food choice. RESEARCH METHODS AND PROCEDURES: A total of 129 healthy adults from three countries (Brazil, Ghana and US) were randomly assigned to one of four treatment arms: consumption of peanut oil, olive oil or safflower oil as 30% of individual resting energy expenditure (REE) for 8 weeks or no dietary intervention. Participants received no other dietary guidance. They completed appetite questionnaires eliciting information about hunger, fullness, desire to eat, and prospective consumption during all waking hours for 1 day at weeks 2 and 6 and for 1 or 3 days at weeks 0, 4 and 8. Diet records were completed at weeks 0, 4 and 8. RESULTS: No differences in appetitive ratings were observed over the 8-week trial. There were no significant treatment by time interactions. Total caloric intake was significantly higher at week 8 relative to baseline (F=10.08, P<0.05). The increases for each treatment were: peanut oil=197+/-114; olive oil=237+/-121; safflower oil=274+/-90; control=75+/-71. Free-feeding intake, an index of dietary compensation, was reduced significantly at weeks 4 and 8 compared to baseline (F=9.08, P<0.00). The declines (compensation scores) were (kcals): peanut oil=-208+/-105 (46%); olive oil=-235+/-105 (50%); safflower oil=-186+/-102 (44%). There were no significant differences across countries in appetite ratings. DISCUSSION: A prior intervention with whole peanuts reported a dietary compensation score of 66% over 8 weeks, this compares to a 46% compensation score observed with peanut oil. Our data suggests that the lipid fraction in peanuts elicits a weak effect on satiety.

Adult↗

PubMed2003

Effect of anti-IgE therapy in patients with peanut allergy.

BACKGROUND: Peanut-induced anaphylaxis is an IgE-mediated condition that is estimated to affect 1.5 million people and cause 50 to 100 deaths per year in the United States. TNX-901 is a humanized IgG1 monoclonal antibody against IgE that recognizes and masks an epitope in the CH3 region of IgE responsible for binding to the high-affinity Fc(epsilon) receptor on mast cells and basophils. METHODS: We conducted a double-blind, randomized, dose-ranging trial in 84 patients with a history of immediate hypersensitivity to peanut. Hypersensitivity was confirmed and the threshold dose of encapsulated peanut flour established by a double-blind, placebo-controlled oral food challenge at screening. Patients were randomly assigned in a 3:1 ratio to receive either TNX-901 (150, 300, or 450 mg) or placebo subcutaneously every four weeks for four doses. The patients underwent a final oral food challenge within two to four weeks after the fourth dose. RESULTS: From a mean base-line threshold of sensitivity of 178 to 436 mg of peanut flour in the various groups, the mean increases in the oral-food-challenge threshold were 710 mg in the placebo group, 913 mg in the group given 150 mg of TNX-901, 1650 mg in the group given 300 mg of TNX-901, and 2627 mg in the group given 450 mg of TNX-901 (P<0.001 for the comparison of the 450-mg dose with placebo, and P for trend with increasing dose <0.001). TNX-901 was well tolerated. CONCLUSIONS: A 450-mg dose of TNX-901 significantly and substantially increased the threshold of sensitivity to peanut on oral food challenge from a level equal to approximately half a peanut (178 mg) to one equal to almost nine peanuts (2805 mg), an effect that should translate into protection against most unintended ingestions of peanuts.

Adolescent↗

PubMed2005

The promiscuity of immunoglobulin E binding to peanut allergens, as determined by Western blotting, correlates with the severity of clinical symptoms.

BACKGROUND: IgE binding to a specific protein has been shown to be associated with severe anaphylaxis to hazelnuts; however, the relationship between IgE binding to specific peanut allergens and symptom severity is currently unclear. OBJECTIVE: To determine if the pattern of IgE binding to specific peanut allergens is associated with the severity of clinical symptoms. METHODS: Forty peanut allergic patients underwent a double-blind placebo-controlled low-dose peanut challenge, during which the severity of the patients' peanut allergy was scored. Serum peanut-specific IgE (psIgE) was measured and IgE binding patterns to peanut proteins analysed. RESULTS: Seventeen IgE binding bands were identified between 5 and 100 kDa with eight bound by >50% of patients. The total number of bands per patient correlated significantly with challenge score (P=0.001, r=0.505) and psIgE (P<0.001, r=0.820). Cluster analysis failed to reveal any association between a particular protein or pattern of proteins (based on presence/absence) and challenge score. However, two protein bands ( approximately 43 and 41 kDa) had peak intensities that correlated positively with challenge score and a third band ( approximately 48 kDa) that correlated negatively. The bands were identified as subunits of Ara h 3/4 and 1, respectively. CONCLUSIONS: Promiscuity of IgE binding appears more important than the recognition of individual proteins. This may mean that clinically useful specific immunotherapy for peanut allergy will be difficult to achieve if only selected allergenic proteins are used. Further investigation of Ara h 1 and 3/4 subunits and a possible association with symptom severity are also highlighted by this study.

Adult↗

PubMed2004

A novel model of sensitization and oral tolerance to peanut protein.

The prevalence of food allergic diseases is rising and poses an increasing clinical problem. Peanut allergy affects around 1% of the population and is a common food allergy associated with severe clinical manifestations. The exact route of primary sensitization is unknown although the gastrointestinal immune system is likely to play an important role. Exposure of the gastrointestinal tract to soluble antigens normally leads to a state of antigen-specific systemic hyporesponsiveness (oral tolerance). A deviation from this process is thought to be responsible for food-allergic diseases. In this study, we have developed a murine model to investigate immunoregulatory processes after ingestion of peanut protein and compared this to a model of oral tolerance to chicken egg ovalbumin (OVA). We demonstrate that oral tolerance induction is highly dose dependent and differs for the allergenic proteins peanut and OVA. Tolerance to peanut requires a significantly higher oral dose than tolerance to OVA. Low doses of peanut are more likely to induce oral sensitization and increased production of interleukin-4 and specific immunoglobulin E upon challenge. When tolerance is induced both T helper 1 and 2 responses are suppressed. These results show that oral tolerance to peanut can be induced experimentally but that peanut proteins have a potent sensitizing effect. This model can now be used to define regulatory mechanisms following oral exposure to allergenic proteins on local, mucosal and systemic immunity and to investigate the immunomodulating effects of non-oral routes of allergen exposure on the development of allergic sensitization to peanut and other food allergens.

Administration, Oral↗

PubMed2005

Maternal experiences of peanut avoidance during pregnancy/lactation: an in-depth qualitative study.

In 1998 the Department of Health Committee on Toxicity of Chemicals in Food, Consumer Products and the Environment issued a report to British general practitioners, which advised that pregnant mothers with a family history of atopy may wish to avoid peanuts during pregnancy/lactation. To explore the lived-in experience of mothers who avoided/did not avoid peanuts during pregnancy/lactation in the light of the information issued. A qualitative approach, using unstructured in-depth interviews to explore what it was like for mothers to have a particular experience. A purposive sample frame was designed to ensure a maximum variation of participants. Forty-two interviews were conducted: 25 participants avoided peanuts; 15 with a family history of atopy and 10 with no such history. Seventeen participants did not avoid peanuts; 10 with a family history of atopy and seven with no such history. Emergent themes included: variations in information provision, a lack of clarity in relation to information and advice about peanut avoidance, the risks entailed and the introduction of peanuts to the developing child's diet; the importance of atopy in influencing participants' decisions to avoid peanuts and the importance of individual's choice in the decision making process. There was a significant difference in family size with respect to avoidance behaviour with 'avoider' families being smaller (p = 0.007). Avoidance was more likely in single child families (71% vs. 53%) although this difference was not significant. Improvements to the experience of avoidance and/or non-avoidance were primarily focused around provision of information and advice. In particular, a need for clear, consistent factual information and advice about the real risks associated with peanut consumption during pregnancy/lactation, and to whom these risks apply.

Adult↗

PubMedDate not supplied

Peanut allergy.

Peanut allergies have become a major health concern in the United States. Peanuts are one of the most common causes of food allergies and along with tree nuts they account for most of the cases of fatal and near-fatal anaphylactic reactions to food. Not only is there a rise in the prevalence of peanut allergies in Westernized countries but also most patients with peanut allergies have lifelong clinical sensitivities to peanuts. Patient management involves strict avoidance, recognition of the early symptoms of anaphylaxis, and usage of an emergency treatment plan, including the self-administration of epinephrine in case of an accidental ingestion. Future treatment strategies may include recombinant peanut protein immunotherapy and anti-Immunoglobulin E therapy to modulate clinical reactivity to peanuts. This article reviews the current understanding of the clinical characteristics, pathogenesis, diagnosis, and management of the peanut allergy.

Anaphylaxis↗

PubMed1991

Peanut as a source of protein for human foods.

Peanut has traditionally been used as a source of oil; however, its worldwide annual protein harvest has reached nearly 4.5 million tons. India followed by China and the United States are the major producers of peanut. In recent years, several cereals and legumes-based foods using peanuts as protein supplements have been developed to alleviate protein calories-malnutrition problem. Peanut in the form of flour, protein isolates, and meal in a mixed product have been found to be very desirable from a sensory quality point of view. Peanut protein is deficient with respect to certain essential amino acids, but its true digestibility is comparable with that of animal protein. Even though various processing methods influence the nutritional and sensory quality of peanut fortified human foods available information on these aspects have been reviewed and summarised in this paper in order to optimize the utilization of peanut protein to increase protein value of cereal-based foods in developing countries of the peanut growing regions of the world.

Arachis↗

PubMed1981

Isolation and partial characterization of a major peanut allergen.

We isolated and partially characterized a major peanut allergen (Peanut-I) using the radioallergosorbent test (RAST) to monitor the allergenicity of various fractions. Raw peanuts were pulverized, defatted, and extracted; the resulting crude extract (CPE) was fractionated by diethylaminoethyl (DEAE) cellulose anion-exchange chromatography using a linear salt gradient. Peak allergenic fractions were further purified by a second DEAE cellulose chromatography step, followed by a preparative polyacrylamide gel electrophoresis (PAGE) step. The final product, Peanut-I, contained 11% nitrogen and 8.7% carbohydrate and was homogeneous by both analytical PAGE and immunoelectrophoresis against rabbit anti-CPE. Peanut-I was heterogeneous by thin-layer electrofocusing and by PAGE in 1% sodium dodecyl sulfate. Biologic activity of Peanut-I was demonstrated by positive skin tests and leukocyte histamine release assays in patients with peanut allergy. By RAST inhibition assay Peanut-I did not account for all of the allergenic activity of CPE.

Allergens↗

PubMed1999

Self-reported allergic reactions to peanut on commercial airliners.

BACKGROUND: Allergic reactions to food occurring on commercial airlines have not been systematically characterized. OBJECTIVE: We sought to describe the clinical characteristics of allergic reactions to peanuts on airplanes. METHODS: Participants in the National Registry of Peanut and Tree Nut Allergy who indicated an allergic reaction while on a commercial airliner were interviewed by telephone. RESULTS: Sixty-two of 3704 National Registry of Peanut and Tree Nut Allergy participants indicated a reaction on an airplane; 42 of 48 patients or parental surrogates contacted confirmed the reaction began on the airplane (median age of affected subject, 2 years; range, 6 months to 50 years). Of these, 35 reacted to peanuts (4 were uncertain of exposure) and 7 to tree nuts, although 3 of these 7 reacted to substances that may have also contained peanut. Exposures occurred by ingestion (20 subjects), skin contact (8 subjects), and inhalation (14 subjects). Reactions generally occurred within 10 minutes of exposure (32 of 42 subjects), and reaction severity correlated with exposure route (ingestion > inhalation > skin). The causal food was generally served by the airline (37 of 42 subjects). Medications were given in flight to 19 patients (epinephrine to 5) and to an additional 14 at landing/gate return (including epinephrine to 1 and intravenous medication to 2), totaling 79% treated. Flight crews were notified in 33% of reactions. During inhalation reactions as a result of peanut allergy, greater than 25 passengers were estimated to be eating peanuts at the time of the reaction. Initial symptoms generally involved the upper airway, with progression to the skin or further lower respiratory reactions (no gastrointestinal symptoms). CONCLUSIONS: Allergic reactions to peanuts and tree nuts caused by accidental ingestion, skin contact, or inhalation occur during commercial flights, but airline personnel are usually not notified. Reactions can be severe, requiring medications, including epinephrine.

Aerospace Medicine↗

PubMed2004

An outbreak due to peanuts in their shell caused by Salmonella enterica serotypes Stanley and Newport--sharing molecular information to solve international outbreaks.

Salmonellosis is a global problem caused by the international movement of foods and high incidence in exporting countries. In September 2001, in an outbreak investigation Australia isolated Salmonella Stanley from imported peanuts, which resulted in a wider investigation in Canada, England & Wales and Scotland. Patients infected with Salmonella serotypes known to be isolated from peanuts and reported to surveillance systems were interviewed to determine exposure histories. Tagged image file format (TIFF) images of pulsed-field gel electrophoresis (PFGE) patterns of Salmonella isolates were shared electronically amongst laboratories. Laboratories tested packets of 'Brand X' peanuts from various lots and product lines. In total, 97 cases of S. Stanley and 12 cases of S. Newport infection were found. Seventy-three per cent (71/97) of S. Stanley cases were in persons of Asian ethnicity. Twenty-eight per cent of cases recalled eating Brand X peanuts and a further 13% had peanuts in their house in the previous month or had eaten Asian-style peanuts. Laboratories isolated S. Stanley, S. Newport, S. Kottbus, S. Lexington and S. Unnamed from Brand X peanuts. Isolates of S. Stanley from peanuts and human patients were indistinguishable by PFGE. This international outbreak resulted from a product originating from one country affecting several others. Rapid sharing of electronic DNA images was a crucial factor in delineating the outbreak; multinational investigations would benefit from a harmonized approach.

Adolescent↗