What is a legume allergy


Recent Food Allergen Research

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


Soybean

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.

Corn

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.

Peanut

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.

What is a legume allergy

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 100 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.

Fish

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

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.

What is a legume allergy

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.

Pecan

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.


FARRP Food Allergen Publications

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


Fish

  1. Chen, L., S. L. Hefle, S. L. Taylor, I. Swoboda, and R. E. Goodman. 2006. Detecting fish parvalbumin with commercial mouse monoclonal anti-frog parvalbumin IgG.

    J. Agric. Food Chem. 54:5577-5582.

  2. Koppelman, S. J., R. Romijn, H. H. J. deJongh, J. A. Nordlee, S. Piersma, M. Hessing, and S. L. Taylor. 2010. Purification of parvalbumin from carp; a protocol that avoids heat-treatment. J. Food Sci. 75:T49-T56.

Sunflower Seed

  1. Kelly, J. D., J. J. Hlywka, and S. L. Hefle. 2000. Identification of sunflower seed IgE-binding proteins. Int. Arch. Allergy Immunol. 121:19-24.
  2. Kelly, J.D. and S. L. Hefle. 2000. 2S Methionine-rich protein (SSA) from sunflower seed is an IgE-binding protein.

    Allergy 55:556-560.

Hazelnut

  1. Akkerdaas, J.H., M. Wensing, A. C. Knulst, O. Stephan, S. L. Hefle, R. C. Aalberse, and R. van Ree. 2004. A novel approach for the detection of potentially hazardous stable hazelnut proteins in food products. J. Agr. Food Chem. 52:7726-31.

Peanut

  1. Piersma, S.R., M. Gaspari, S.L. Hefle, and S. J. Koppelman. 2005. Proteolytic processing of the peanut allergen Ara h 3. Mol. Nut. Food Res.49:744-755.
  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. 2004. 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. 114:1410-1417.

  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. 2005. Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: Evidence for cross-reactivity with Ara h 2. Clin. Exp. Allergy 35:490-297.
  4. Koppelman S. J., E, F. Knol, R. A. A. Vlooswijk, M. Wensing, A.

    C. Knulst, S. Hefle, H. Gruppen, and S. Piersma. 2003. Peanut allergen Ara h 3; isolation from peanuts and biochemical characterization. Allergy 58:1144-1151.

Kiwi

  1. Chen, L., J. S. Lucas, J. O. Hourihane, J. Lindemann, S. L. Taylor, and R. E. Goodman. 2006. 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 Chem.Toxicol. 44:1100-1107.

Lupine

  1. Hefle, S.L., R. Lemanske, and R. K. Bush. 1994. Adverse reaction to lupine-fortified pasta.

    J. Allergy Clin. Immunol. 94:167-172.

  2. Peeters, K. A. B. M., S. J. Koppelman, A. H. Penninks, A. Lebens, C. A. F. M. Bruijnzeel-Koomen, S. L.
  3. Peeters, K. A. B.

    What is a legume allergy

    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. 2007. Lupine allergy: not simply cross-reactivity with peanut or soy. J. Allergy Clin. Immunol. 120:647-653.

  4. Hefle, S. L. Taylor, E.

    What is a legume allergy

    Van Hoffen, and A. C. Knulst. 2009. Clinical relevance of sensitization to lupine in peanut-sensitized adults. Allergy 64:549-555.

Brazil Nut

  1. Nordlee, J. A., S. L. Taylor, J. A. Townsend, L. A. Thomas, and R. K. Bush. 1996. Identification of a Brazil nut allergen in transgenic soybeans. New Engl. J. Med. 334:688-692.
  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. 2005. Reversible denaturation of Brazil nut 2S albumin (Ber e1) and implication of structural destabilization on digestion by pepsin. J. Agric. Food Chem. 53:123-131.

Soybean

  1. Herian, A.

    M., S. L. Taylor, and R. K. Bush. 1990. Identification of soybean allergens by immunoblotting with sera from soy-allergic adults. Int. Arch. Allergy Appl. Immunol. 92:193-198.

Almond

  1. Bargman, T. J., J. H. Rupnow, and S. L. Taylor. 1992. Identification of IgE-binding proteins in almonds (Prunus amygdalus) by immunoblotting with sera from almond-allergic adults. J. Food Sci. 57:717-720.

Allergen Stability

  1. Taylor, S. L., R.

    F. Lemanske, Jr., and R. K. Bush. 1987. Chemistry of food allergens. Comments Agr. Food Chem. 1:51-70.

  2. 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.

    What is a legume allergy

    A. Rice, L. S. Privalle, H. Y. Steiner, R. Teshima, R. van Ree, M. Woolhiser, and J. Zawodny.

    What is a legume allergy

    2004. A multi-laboratory evaluation of a common in vitro pepsin digestion assay protocol used in assessing the safety of novel proteins. Reg. Toxicol. Pharmacol. 39:87-98.

  3. Taylor, S. L., R. F. Lemanske, Jr., R. K. Bush, and W. W. Busse. 1987. Food allergens: structure and immunologic properties. Ann. Allergy 59:93-99.
  4. Hefle, S.L. 1999. Impact of processing on food allergens. Advances in Experimental Medicine and Biology 459:107-119.
  5. Taylor, S.

    and S. Lehrer. 1996. Principles and characteristics of food allergens. CRC Crit. Revs. Food Sci. Nutr. 36:S91-S118.

  6. Ofori-Anti, A. O., H. Ariyarathna, L. Chen, H. L. Lee, S. N. Pramod, and R. E. Goodman. 2008. Establishing objective detection limits for the pepsin digestion assay used in the assessment of genetically modified foods. Reg. Toxicol. Pharmacol. 52:94-103.

The Fairfield Country Day School in Connecticut still serves peanut butter but has eliminated peanuts from its dessert menu, banning them from brownies, cookies and ice-cream sundaes.

''Who would own thought an old-fashioned favorite love peanut butter and jelly could be considered so dangerous?'' said Robert Vitalo, the Fairfield headmaster.

Among public schools, Mount Kisco Elementary School in Westchester County and the Cos Cob Elementary School in Greenwich, Conn., own set aside a peanut-free table that is scrubbed below before and after meals. Schools in Buffalo, North Andover, Mass., Orange County, Calif., and Toronto own taken similar measures.

At the opposite finish of the spectrum, the New York City public school system, the country's largest with more than one million children, has remained immune to the peanut phenomenon, largely because no one has complained.

In city schools, peanut butter and jelly sandwiches are still offered as a cold-lunch option in every school almost every day, said a spokesman, J. D. LaRock. When peanut butter is not the choice of the day, it is available on request, he said. ''There's peanut butter aplenty in our system,'' Mr. LaRock said. Peanuts are not served, but that is because they are a choking hazard, he added.

While peanut butter has been slow to become an issue in the New York public schools, the city's private schools own fallen in line love so numerous dominoes.

Mark E. Brossman, a lawyer who represents numerous New York City private schools, said schools are concerned that peanut allergies might qualify as a disability that must be accommodated under the Americans with Disabilities Act. Neither Mr. Brossman nor the Food Allergy Network knew of any litigation on peanut allergy that has resulted in a court decision.

But a recent directive by the Federal Department of Transportation construed peanut allergies as a disability and ordered airlines to set up peanut-free zones. That decision may set a precedent for schools, advocates say.

Beyond bans, schools are trying to decide whether to provide individualized supplies — tell, blocks and sets of wooden rods for solving math problems — to children with severe allergies so they will not be contaminated by the peanut-smeared hands of classmates.

Concerned that a kid who has just eaten peanut butter might hold hands with an allergic kid, schools now urge children to become regular hand-washers.

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