What is a brazil nut allergy

If you own an allergic reaction to one type of nut, you might be tempted to avoid eating every others. After every, symptoms love itchy lips, hives and face swelling arent pleasant, and food allergies can be life threatening in the worst-case scenarios.

But now, a new study finds that just because youre diagnosed with a nut allergy doesnt necessarily mean youre allergic to it. In the research published in Annals of Allergy, Asthma and Immunology, at least half of people with a diagnosed nut allergy do not show allergic symptoms to other types of nuts—even when tests show that they are allergic.

And almost every of the people with allergies to peanuts—which are technically legumes—were capable to safely eat tree nuts love almonds, walnuts and Brazil nuts, even though tests had suggested they might be problematic.

Researchers looked at data from people who had tested positive for a tree nut allergy, according to blood and skin tests done in the past eight years. For example, if a person knew they were allergic to almonds and also tested positive for a cashew allergy—but had never eaten a cashew in her life—researchers fed her little amounts of cashews every 15 to 20 minutes to see if there was a reaction.

(Dont attempt this at home: doctors were standing by with life-saving medication, if necessary.) They looked for serious reactions, love hives or trouble breathing, but found that 50% of people displayed no allergic reaction, even though blood tests suggested otherwise.

That may be because some people own antibodies that react in blood or skin-prick tests, but they dont necessarily own any symptoms when they eat the food. In other words, theyre sensitized to the allergen.

While most people with peanut allergies were capable to eat tree nuts, that wasnt true for everyone. “Some of the individuals tested in the study had peanut allergies but never tried tree nuts, and when they tried them, they turned out to be allergic,” says Dr.

Christopher Sofa, an allergist-immunologist and lead author of the study.

If a person thinks they own a nut allergy, I propose they speak to their doctor about the symptoms and why they are suspicious,” says Dr. Scott Sicherer, a professor of pediatrics, allergy and immunology at the Mount Sinai Icahn School of Medicine. An allergist-immunologist can use a persons medical history and blood tests to decide if a nut allergy is really the problem, he says.

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Your child’s diet

There’s currently no cure for food allergies, although numerous children will grow out of certain ones, such as allergies to milk and eggs.

The most effective way you can prevent symptoms is to remove the offending food – known as an allergen – from their diet.

However, it’s significant to check with your GP or the doctor in charge of your child’s care first before eliminating certain foods.

Removing eggs or peanuts from a child’s diet isn’t going to own much of an impact on their nutrition. Both of these are a excellent source of protein, but can be replaced by other, alternative sources.

A milk allergy can own more of an impact as milk is a excellent source of calcium, but there are many other ways you can incorporate calcium into your child’s diet, including green leafy vegetables.

Numerous foods and drinks are fortified with additional calcium.

See your GP if you’re concerned that your child’s allergy is affecting their growth and development.

Reading labels

It’s extremely significant to check the label of any pre-packed food or drinks your kid has in case it contains ingredients they’re allergic to.

Under EU law, any pre-packed food or drink sold in the UK must clearly state on the label if it contains the following ingredients:

  1. fish
  2. tree nuts – such as almonds, hazelnuts, walnuts, brazil nuts, cashews, pecans, pistachios and macadamia nuts
  3. sesame seeds
  4. mustard
  5. eggs
  6. lupin (common garden plants) – seeds from some varieties are sometimes used to make flour
  7. peanuts
  8. celery
  9. molluscs – including mussels and oysters
  10. cereals that contain gluten – including wheat, rye, barley and oats
  11. soybeans
  12. crustaceans – including prawns, crabs and lobsters
  13. milk
  14. sulphur dioxide and sulphites (preservatives used in some foods and drinks) – at levels above 10mg per kg or per litre

Some food manufacturers also select to put allergy advice warning labels – for example, «contains nuts» – on their pre-packed foods if they contain an ingredient known to commonly cause an allergic reaction, such as peanuts, wheat, eggs or milk.

However, these aren’t compulsory.

If there’s no allergy advice box or «contains» statement on a product, it could still own any of the 14 specified allergens in it.

Look out for «may contain» labels, such as «may contain traces of peanut». Manufacturers sometimes put this label on their products to warn consumers that they may own become contaminated with another food product when being made.

Read more detailed information about allergen labelling on the Food Standards Agency website.

Some non-food products contain allergy-causing food:

  1. some soaps and shampoos contain soy, egg and tree nut oil
  2. some pet foods contain milk and peanuts
  3. some glues and adhesive labels used on envelopes and stamps contain traces of wheat

Again, read the labels of any non-food products your kid may come into shut physical contact with.

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Major Sections on this Page

From the inception of FARRP (and even prior to that), one of the major research efforts has surrounded the identification of the proteins in foods that cause sensitization in susceptible individuals and the elicitation of allergic reactions in those individuals who are sensitized.

Over the years, research has focused on allergens in commonly allergenic foods such as peanuts, soybeans, almonds, hazelnuts, Brazil nuts, and fish and in less commonly allergenic foods such as lupine, sunflower seeds, sesame seeds, and kiwi. During the first 10 years of FARRP, this area of research was led by our founding co-Director, the tardy Prof. Sue Hefle and included research done in collaborations with leading European research investigators including Stef Koppelman (now adjunct professor with FARRP) and Ronald van Ree.

Recently, this area of research has been restimulated by the addition of Prof. Joe Baumert, the continuing collaborative efforts of Prof. Stef Koppelman and the activities of Prof. Rick Goodman relating to cross-reacting allergens. FARRP has also historically been interested in the stability of allergens to food processing unit operations and to digestion (proteolytic stability).

FARRP Food Allergen Publications

«FARRP Food Allergen Publications» Sections
Almond | Brazil Nut | Fish | Hazelnut | Kiwi | Lupine | Peanut | Soybean | Sunflower Seed | Allergen Stability


  1. Chen, L., S.

    L. Hefle, S. L. Taylor, I. Swoboda, and R. E. Goodman. Detecting fish parvalbumin with commercial mouse monoclonal anti-frog parvalbumin IgG. J. Agric. Food Chem.

  2. Koppelman, S. J., R. Romijn, H. H. J. deJongh, J. A. Nordlee, S. Piersma, M. Hessing, and S. L. Taylor. Purification of parvalbumin from carp; a protocol that avoids heat-treatment. J. Food Sci. TT


  1. Piersma, S.R., M. Gaspari, S.L. Hefle, and S. J. Koppelman. Proteolytic processing of the peanut allergen Ara h 3. Mol. Nut. Food Res
  2. Mittag, D., J. Akkerdaas, B. K. Ballmer-Weber,L. Vogel, L., M. Wensing, W.-M. Becker, S. Koppelman, A.

    Helbling, S. L. Hefle, R. van Ree, and S. Vieths. Ara h 8; a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J. Allergy Clin. Immunol.

  3. Koppelman, S.J., G. A. H. de Jong, M. Laaper-Ertmann, K. A. B. M. Peeters, A. C. Knulst, S. L. Hefle, and E. F. Knols. Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: Evidence for cross-reactivity with Ara h 2. Clin. Exp. Allergy
  4. Koppelman S. J., E, F. Knol, R. A. A. Vlooswijk, M. Wensing, A. C. Knulst, S. Hefle, H. Gruppen, and S.

    Piersma. Peanut allergen Ara h 3; isolation from peanuts and biochemical characterization. Allergy

Sunflower Seed

  1. Kelly, J. D., J. J. Hlywka, and S. L. Hefle. Identification of sunflower seed IgE-binding proteins. Int. Arch. Allergy Immunol.
  2. Kelly, J.D. and S. L. Hefle. 2S Methionine-rich protein (SSA) from sunflower seed is an IgE-binding protein. Allergy


  1. Hefle, S.L., R. Lemanske, and R. K. Bush. Adverse reaction to lupine-fortified pasta. J. Allergy Clin. Immunol.
  2. Peeters, K. A. B. M., S. J. Koppelman, A. H. Penninks, A. Lebens, C. A. F. M. Bruijnzeel-Koomen, S.


  3. Peeters, K. A. B. M., J. A. Nordlee, A. H. Penninks, L. Chen, R. E. Goodman, C. A. F. M. Bruijnzeel-Koomen, S. L. Hefle, S. L. Taylor, and A. C. Knulst. Lupine allergy: not simply cross-reactivity with peanut or soy. J. Allergy Clin. Immunol.
  4. Hefle, S. L. Taylor, E. Van Hoffen, and A. C. Knulst. Clinical relevance of sensitization to lupine in peanut-sensitized adults. Allergy


  1. Akkerdaas, J.H., M. Wensing, A. C. Knulst, O. Stephan, S.

    L. Hefle, R. C. Aalberse, and R. van Ree. A novel approach for the detection of potentially hazardous stable hazelnut proteins in food products. J. Agr. Food Chem.

Brazil Nut

  1. Nordlee, J. A., S. L. Taylor, J. A. Townsend, L. A. Thomas, and R. K. Bush. Identification of a Brazil nut allergen in transgenic soybeans. New Engl. J. Med.
  2. Koppelman, S.J., W. F. Nieuwenhuizen, M. Gaspari, L. M. J. Knippels, E. F. Knol, S. L. Hefle, and H. H. J. de Jongh. Reversible denaturation of Brazil nut 2S albumin (Ber e1) and implication of structural destabilization on digestion by pepsin.

    J. Agric. Food Chem.


  1. Herian, A. M., S. L. Taylor, and R. K. Bush. Identification of soybean allergens by immunoblotting with sera from soy-allergic adults. Int. Arch. Allergy Appl. Immunol.


  1. Bargman, T. J., J. H. Rupnow, and S. L. Taylor. Identification of IgE-binding proteins in almonds (Prunus amygdalus) by immunoblotting with sera from almond-allergic adults. J. Food Sci.


  1. Chen, L., J. S. Lucas, J. O. Hourihane, J. Lindemann, S. L. Taylor, and R. E. Goodman. Evaluation of IgE binding to proteins of hardy (Actinidia arguta), gold (Actinidia chinensis), and green (Actinidia deliciosa) kiwifruits and processed hardy kiwifruit concentrate, using sera of individuals with food allergies to green kiwifruit.

    Food l.

Allergen Stability

  1. Taylor, S. L., R. F. Lemanske, Jr., and R. K. Bush. Chemistry of food allergens. Comments Agr. Food Chem.
  2. Hefle, S.L. Impact of processing on food allergens. Advances in Experimental Medicine and Biology
  3. Thomas, K, M. Aalbers, G. A., Bannon, M. Bartels, R. J. Dearman, D. J. Esdaile, T..J. Fu, C. M., Glatt, N. Hadfield, C. Hatzos, S. L. Hefle, J. R. Heylings, R. E. Goodman, B. Henry, C. Herouet, M. Holsapple, G. S. Ladics, T. D. Landry, S. C. MacIntosh, E. A. Rice, L. S. Privalle, H. Y. Steiner, R. Teshima, R. van Ree, M. Woolhiser, and J. Zawodny. A multi-laboratory evaluation of a common in vitro pepsin digestion assay protocol used in assessing the safety of novel proteins.

    Reg. Toxicol. Pharmacol.

  4. Taylor, S. and S. Lehrer. Principles and characteristics of food allergens. CRC Crit. Revs. Food Sci. Nutr. SS
  5. Taylor, S. L., R. F. Lemanske, Jr., R. K. Bush, and W. W. Busse. Food allergens: structure and immunologic properties. Ann. Allergy
  6. Ofori-Anti, A. O., H. Ariyarathna, L. Chen, H. L. Lee, S. N. Pramod, and R. E. Goodman. Establishing objective detection limits for the pepsin digestion assay used in the assessment of genetically modified foods.

    Reg. Toxicol. Pharmacol.

The advice here is primarily written for parents of a kid with a food allergy. However, most of it is also relevant if you’re an adult with a food allergy.

Recent Food Allergen Research

«Recent Food Allergen Research» Sections
Peanut | Soybean | Legume Cross-Reactivity | Fish | Corn | Pecan


A FARRP Ph.D. student, Ben Remington, under the joint supervision of Profs.

Taylor and Baumert, has initiated research on soybean allergens. The clinical picture on the reactivity of soy-allergic individuals with various soy proteins is far from clear. Diverse individuals seem to react to diverse soy allergens although differences also appear to be influenced by the selection of methods and perhaps even by the selection of soy-based materials to use in the research. Thus far, research by other groups has sure that Gly m 5 and Gly m 6 (conglycinin and glycinin, respectively) are major soybean allergens. Gly m 3 (profilin) and Gly m 4 (a Bet v 1 homologue) are other significant soy allergens.

An oleosin from soy, called P34, is another potential soy allergen. The soy trypsin inhibitor (STI) has been identified as a minor allergen. FARRP is particularly interested in the levels of these allergenic proteins in various soy-based ingredients.


A FARRP graduate student, Poi-Wah Lee (Ph.D. candidate) under the supervision of Prof. Taylor with collaboration from Prof. Koppelman is pursuing research on parvalbumin, the major allergen from fish. Parvalbumin has the distinction of being one of the first major food allergens to be identified and characterized. Considerable research has been done on parvalbumin from various species of fish over the years but much remains to be done.

The major goals of Poi-Wah Lee’s Ph.D. project will be:

  1. To investigate the effects of species, calcium, thermal processing, and Maillard reactions on the IgE and IgG binding characteristics of fish parvalbumins in the immunoassay
  2. To determine the immunoreactivity of IgG and IgE to parvalbumin isotypes expressed in diverse species of fish
  3. To quantify the relative content of parvalbumin in various species of fish
  4. To study the evolutionary relationship of parvalbumins and verify the IgE-binding epitopes of fish parvalbumins


Corn is not a major allergenic food and is, in fact, rarely allergenic.

However, some corn-allergic individuals do exist. Because of the rare nature of this allergy, the allergens in corn own been incompletely studied. FARRP M.S. student, Harsha Ariyarathna under the supervision of Prof. Goodman conducted research to isolate the major food allergen, lipid transfer protein (LTP) from corn seed and assess differences in LTP content in seeds from 9 commercial hybrids of corn grown in two locations in Nebraska.

This research also demonstrated that almost every of the LTP is concentrated in the embryo and pericarp of the seed.

Legume Cross-Reactivity

The Goodman group including Ph.D. student, Afua Ofori-Anti, and previous post-doc, Dr. Pramod Siddanakoppalu, own evaluated IgE-binding cross-reactivity in among a wide taxonomic range of legumes. Methods own been developed to distinguish binding to carbohydrate determinants from binding to the peptide structure of proteins. Basophil histamine release has been used to assess the biological activity of the various legume proteins. Publications are pending.


FARRP under the leadership of Prof.

Baumert has recently entered into a collaborative research agreement with USDA-ARS and specifically with Dr. Soheila Maleki from the USDA Southern Regional Research Middle in New Orleans. The USDA-ARS project is focused primarily on peanut and tree nut allergens including the identification and characterization of peanut, other legume, and tree nut allergens. However, the primary FARRP roles in this project will be focused on immunoassay development, evaluation and improvement and on peanut and tree nut thresholds.

A Ph.D. student in Prof. Goodman’s laboratory (Afua Ofori-Anti) has recently investigated the role of the peanut agglutinin protein as a possible allergen.

Previous research in other laboratories had suggested that peanut agglutinin was a minor peanut allergen based on its ability to bind IgE from the sera of some peanut-allergic individuals. However, these same individuals often had IgE binding to other peanut proteins as well. Dr. Ofori-Anti demonstrated that the IgE binding to peanut agglutinin was based largely upon carbohydrate epitopes (glycoprotein). This binding does not appear to be clinically significant and peanut agglutinin does not appear to be a peanut allergen.

Research led by Prof.

Baumert in collaboration with Prof. Koppelman focused on the in vivo distribution of a digestion-resistant peptide of the major peanut allergen, Ara h 2. Ara h 2 is comparatively resistant to digestion and a digestion-resistant peptide (DRP-Ara h 2) is released in model digestion experiments. DRP-Ara h 2 could theoretically sensitize infants upon exposure through breast milk or could elicit reactions by skin contact from saliva. A competitive inhibition ELISA for DRP-Ara h 2 was successfully developed utilizing rabbit polyclonal antisera and applied to the analysis of serum, saliva and breast milk.

The optimized ELISA has a limit of quantitation (LOQ) of ng DRP-Ara h 2/ml in every body fluids. A study has been completed on the llevels of intact peanut protein and/or DRP-Ara h 2 in serum, saliva, and breast milk of humans after ingestion of peanut (publication pending). Robert Bush, M.D. (University of Wisconsin — Madison) and Michael Levy, M.D. (University of Wisconsin — Milwaukee) collaborated on the clinical aspects of the serum and saliva studies while David Hill, M.D.

(Melbourne, Australia) designed and conducted the breast milk study providing samples to FARRP for analysis. DRP-Ara h 2 was detected in serum, saliva and breast milk during these investigations. The work on the purification and in vitro and in vivo digestion of the major peanut allergen, Ara h 2 (2S albumin), has provided insight into the stability of this allergenic 2S albumin and peptide fragments of this protein. Resistance to gastrointestinal digestion is believed to be a key characteristic of numerous food allergens due to the preservation of the protein structure. Sufficiently intact protein or immunologically athletic peptides derived from allergenic food proteins may be absorbed by gut epithelial cells or M cells and interact with the mucosal immune system for extended periods of time which may result in allergic sensitization.

Prof. Baumert intends to continue conducting research on allergenic proteins and their digestive resistance.


The prevalence of tree nut allergy appears to be increasing in children in the United States. Walnut allergy is the most frequently reported among the tree nuts in the U.S. while pecan allergy currently ranks fourth. Both walnut and pecan belong to the Juglandaceae family, however, little information is currently available regarding the potential for clinical cross-reactivity between these closely related tree nuts.

FARRP M.S. student, Jelena Spiric under the supervision of Prof. Baumert, is conducting research on characterization and stability of pecan allergens, and is examining the potential clinical cross-reactivity of pecan and walnut allergens using sera from pecan and walnut allergic individuals.