Safefoodera project final meeting copenhaguen 06-2011x · En los últimos años se han ensayado con algún éxito medida de desensibilización según las pautas clásicas de la inmunoterapia

SAFEFOODERA

DETECTION OF TRACES OF ALLERGENS IN FOODS (ERA-NET PROJECT 08125)

Project duration: march 2009-march 2011

Topic: Allergens

Coordinator: Jorge Martínez-Quesada (UPV/EHU)

University of the Basque Country (UPV/EHU). Faculty of Pharmacy. June, 2011.

Adverse reactions to foods

ToxicNon-toxic

Immune meditedFOOD ALLERGY

Non-immune meditedFOOD INTOLERANCE

Clasificación de las reacciones adversas por alimentos. M. Fernández , S. Miles. Plant Food allergens. EN Clare and P Shewrry Eds. Blackwell Pub. 2004.

UndefinedPharmacologicEnzimaticNon-IgE mediatedIgE mediated

Non-toxic (enzyme deficiency)

Lactose intolerance, galactosemia.Toxic (pharmacologic)

Caffeine (jitteriness), tyramine in aged cheeses (migraine), alcohol, histamine (scromboid fish poisoning).Heavy metal poisoning, bacterial food poisoningMimickers of food intolerance/allergy

Pancreatic insufficiency, gallbladder or liver disease, hiatal hernia and gustatory rhinitis, anorexia nervosa, auriculotemporal syndrome (facial flush with salivation).

IgE mediated

Urticaria, angioedema, morbilliform rashes, acuterhinoconjunctivitis,acute asthma exacerbation, anaphylaxis, food-associated exercise-induced anaphylaxis, oral allergy syndrome.Non IgE associated

Food protein–induced proctocolitis and/or enterocolitis, contact dermatitis, dermatitis herpetiformis, celiac disease.Mixed IgE-mediated/non-IgE-mediated

Atopic dermatitis, asthma, allergic eosinophilicesophagitis, and/or gastroenteritis

Adapted with permission from Sicherer and Sampson

DIAGNÓSTICO

Historia clínica

Datos complementarios� Pruebas cutáneas� Pruebas funcionales� Pruebas de laboratorio (IgE Total, IgE específica, otros datos generales e inmunológicos)� Datos radiológicos (Imagen)

Datos medioambientalesDatos medioambientales� Aerobiología� Detección de alérgenos medioambientales

CONTROL

Tratamiento (Sintomático y específico)EvitaciónDetección y cuantificación de alérgenos causales en medioambiente y alimentos.

España USA< 5 años > 5 años Niños (con DA y

alergia alimentaria)Adultos

Alergológica Alergológica Sampson, 1997 Sampson, 1997

Huevo 44 Frutas 37 Huevo 57 Crustáceos 50

Leche 44 F. secos 36 Leche 38 Cacahuete 20

Pescado 14 Pescado 12 Cacahuete 29 Huevo 10

!UNO DE LOS MUCHOS EJEMPLOS!

Prevalencia (%) de alergias específicas a alimentos según edad y localización geográfica.

Pescado 14 Pescado 12 Cacahuete 29 Huevo 10

Frutas 11 Marisco 12 Soja 16 Cerveza 10

F. secos 7 Huevo 10 Trigo 11 Zanahoria 10

Legumbres 7 Cereales 8

Legumbres 6

Leche 5

Hortalizas 5

M. Fernández , S. Miles. Plant Food allergens. EN Clare and P Shewrry Eds. Blackwell Pub. 2004

Food Infants/Young children

Older children and adults

Anaphylaxis

Milk (cow/goat) • •

Chicken egg • •

Soy •

Peanut • • •

Tree nuts (walnut, hazel/filbert, cashew, pistachio, Brazil , pine

nut, almond)

• •

Common Food Allergens

nut, almond)

Wheat •

Fish •

Shellfish (shrimp, crab, lobster, oyster, scallops)

• •

Fruit • •

Vegetables • •

Seeds (cotton, sesame, psyllium, mustard)

• •

Spices •

O.M.S., Worldallergy.org

Protein Family Allergen examples

Parvalbumins Gad c 1, Cyp c 1

Tropomyosins Pen a 1, Hom a 1, Top d 1

Arginine kinases Pen m 2

Alfa lactalbumins Bos d 4

Lysozymes Gal d 4

Beta lactalbumins Bos d 5

PRINCIPALES ALÉRGENOS DE ORIGEN ANIMAL

Beta lactalbumins Bos d 5

Serum albumins Bos d 6

Alfa/Beta Caseins Bos d 8

Immunoglobulins Bos d 7

Transferrins Cow lactoferrin, gal d 3

Ovomucoids Gal d 1

Ovoalbumins Gal d 2

SJ Koppelman, SL Hefle. Detecting allergens in foods. CRC Press. Boca Raton. 2006

Superfamilia Prolamina

Prolaminas (α-amilasa, gliadinas) Cerales, …

nS-LTPs (Pru p 3) Frutos/as, vegetales, …

Albuminas 2S (Sian a 1 , Ara h 2) Cereales, semillas

Superfamilia Cupin

PRINCIPALES ALÉRGENOS VEGETALES

Superfamilia Cupin

Globulinas 7 S (Vicilinas: Ara h 1) Legumbres, frutos secos

Globulinas 11 S (Leguminas: Ara h 3, glicininas,…)

Legumbres, frutos secos

Familia Cistein-proteasa

Papain-like, Act c 1 Frutas

Familia Profilinas

Profilinas Polen, frutas, vegetales


Plant pathogenesisrelated proteins families

PR-2 Beta 1-3 glucanases Plátano, patata, tomate

PR-3 Class I chitinases Aguacate, castaña

PR-4 Hevein and Win-like chitinases Latex-frutas

PRINCIPALES ALÉRGENOS VEGETALES

PR-5 Thaumatin-like proteins Pru av 2, Mal d 2

PR-9 Peroxidases trigo

PR-10 Bet v 1 homologues Mal d 1, Pru p 1, Api g 1, Gly m 4

PR-14 Non specific LTPs Pru p 3, Mal d 3, Cor a 8, Ara h 9, Lac s 1


IMPACTO DE LA ALERGIA A ALIMENTOS EN LA CALIDAD DE VIDA

Alta prevalencia, raramente fatal pero en alergia a alimentos los casos de anafilaxia son relativamente comunes (1/3 de las anafilaxias son por alimentos). El diagnóstico correcto impone el uso de dietas libres de estos alérgenos y por consiguiente el exhaustivo conocimiento de la composición (alergénica) de los alimentos.

� Vigilancia . Vigilancia continua. Educación dirigida. El desconocimiento de la composición de los alimentos supone una causa de estrés.

� Costes. Absentismo laboral y escolar, medicación o tratamientos inadecuados. …

� EtiquetadoInadecuadoPreventivo

� Informe de riesgos a los grupos de pacientes

� Educación sobre alergia e intolerancia

TRATAMIENTO

El único tratamiento probado para la alergia alimentaria es la evitación del alérgeno implicado, aunque no siempre es fácil; bien sea por la presencia de alérgenos escondidos en alimentos o por reactividad cruzada con alérgenos de origen no alimentario.

En los últimos años se han ensayado con algún éxito medida de desensibilización según las pautas clásicas de la inmunoterapia específica con extractos alergénicos.específica con extractos alergénicos.

Land MH, Kim EH, Burks AW.Oral desensitization for food hypersensitivityImmunol Allergy Clin North Am. 2011 May;31(2):367-76.

AbstractFood allergy has become an increasingly prevalent international health problem. Allergic reactions can result in life-threatening anaphylaxis in a short period of time, so the current standard of care dictates strict avoidance of suspected trigger foods and accessibility to injectable epinephrine. Intervention at the time of exposure is considered a rescue therapy rather than a disease-modifying treatment. Investigators have been studying allergen immunotherapy to promote induction of oral tolerance. This article examines the mechanisms of oral tolerance and the breakdown that leads to food allergy, as well as the history and current state of oral and sublingual immunotherapy development.

LEGISLACIÓN CONCERNIENTE AL ETIQUETADO DE ALÉRGENOS

• Cereales conteniendo gluten• Crustaceos• Huevo• Leche• Pescado• Cacahuete• Soja• Frutos secos (almendra, avellana, anacardo, castaña, nueces, pistacho.• Frutos secos (almendra, avellana, anacardo, castaña, nueces, pistacho.• Apio• Mostaza• Sésamo• Dióxido de sulfuro y sulfitos

European Union Regulation

Faltan alimentos e indicacionesNo hay límites de detección ni estándares

MÉTODOS DE DETECCIÓN DE ALÉRGENOS EN ALIMENTOS

� Anticuerpos (monoclonales y policlonales).

� Análisis mediante determinación de IgE específica. Inmunoensayos competitivos.

� Inmunotransferencia (immunoblotting).

� E.L.I.S.A.

� P.C.R.

� Proteómica (EF2D-Espectrometría de masas).

� Surface Plasmon Resonance Immunoassay (Biosensores para la detección de sustancias).

� Lateral flow devices.

NECESIDADES FUTURAS PARA MÉTODOS DE CONTROL

• Especificidad suficiente• Sensibilidad suficiente• Detección rápida• De fácil manejo• Económico• Apto para uso industrial • Apto para uso industrial • Apto para uso fuera o dentro del laboratorio• De fácil automatización

University of the Basque Country Department of Immunology, Microbiology and ParasitologyFaculty of Pharmacy. Pº Universidad, 7. 01006-Vitoria/[email protected]

VTT Technical Research Centre of FinlandP.O. Box 1000. FI-02044Espoo. [email protected]

PARTICIPANTS

[email protected]

Food Research Institute Prague Department of Nutritive SubstancesRadiová 7. 102 31 Praha 10 . Praha.Czech [email protected]

AZTI Tecnalia Technological Park of Biskay. Astondo bidea, Edif. 609. 48160-Derio. Bizcay. Basque Conutry.Spain. [email protected]

THE PARTNERS

Main objectives

VALIDACIÓN DE MÉTODOS CLÁSICOS: LA REFERENCIA ACTUAL.Estandarización de métodos clásicos para cuantificar alérgenos en alimentos. Producción de estándares de referencia (in-house references) para los estudios colaborativos. Desarrollo de ELISAs para la detección de alérgenos de leche y mostaza y gliadina (ring trials).

INNOVACIÓN. MÉTODOS Y REACTIVOS.Desarrollo de reactivos y métodos alternativos de alta, sensibilidad, especificidad y eficacia. Aislamiento de anticuerpos quiméricos (IgE humanizada) con diferentes especificidades frente a alérgenos alimentarios.

According to the the background of the topic, the objectives of each member and thepotential for common goals, the main objectives were defined as follows:

especificidades frente a alérgenos alimentarios. Desarrollo de métodos innovativos para la detección de alérgenos de parásitos del pescado a través de genes codificadores.Detección y cuantificación de alérgenos individualizados mediante inmunoensayos-inhibición.

PROCESOS.Influencia del procesamiento de los alimentos en la detectabilidad de alérgenos

COROLARIOSAumento y mejora de la información. Influencia sobre la legislación y etiquetado. Información a la población general.

ORGANIZATION AND WORK PROGRAM

WP 1. Establishment of homogeneous reference systems (allergens and validated detection methods)(UPV, FRIP, VTT)

In house allergen referencesCommercial ELISA Kits

WP 3. Development of innovative methodologies for allergen traces WP 4. Validation of detection methods

WP 0.

Coordination (UPV)

methodologies for allergen traces detection

(VTT, AZTI, UPV)AntibodiesELISA kits

Immunoarrays

WP 4. Validation of detection methods with collaborative studies (FRIP, VTT, UPV, AZTI)

Ring Test

WP 2. Evaluation of food processing on allergen

detectability(AZTI)

Impact of technologyImpact of matrix

WP 5. Diffusion and exploitation of results(AZTI, UPV, FRIP, VTT)

RESUME OF RESULTS

WP 1. Establishment of homogeneous

reference systems (allergens and validated

detection methods)

Partner : UPV/EHU

The production and standardization of in-house references to AZTI and UPV/EHU house references to AZTI and UPV/EHU (Anisakis, ovoalbumin, avomucoid and betta-lactoalbumin) were obtained and purified (HR chromatography) from biological sources.Quantification was performed by mass-spectrometry together with competitive immunoassays.

Assessment of inhibition assays in molecular allergen platforms to measure individual allergenic components in foods

Idoia Postigo, Jorge Guisantes, Ester Suñén, Maialen Ceballos, Dana Gabrovská* and Jorge Martínez

Laboratory of Parasitology and Immunoallergy. Centro de Investigación y Estudios Avanzados “Lucio Lascaray” and Faculty of Pharmacy. University of the Basque Country. Pº Universidad 7.

01006-Vitoria. Spain and *Food Research Institute Prague. Radiová, 7, 10231 Praha 10. Czech Republic

FEIA ImmunoCAP platform

WP3: Development

of innovative

methodologies for

allergen traces

detection.

Partner: UPV/EHU

y = 45,02x + 35,41R² = 0,919

0102030405060708090

100

% of inhibtionSTANDARD CURVE

y = 32,17x + 36,56R² = 0,969

0102030405060708090

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Linear measurement: from 0.1 to 50 μg/g

y = 0,935x - 0,543R² = 0,989

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Linear correlation FEIA (ovoalbumin) - ELISA (egg)

y = 0,949x - 1,213R² = 0,930

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Assessment of inhibition assays in molecular allergen platforms to measure individual allergenic components in foods

Idoia Postigo, Jorge Guisantes, Ester Suñén, Maialen Ceballos, Dana Gabrovská* and Jorge Martínez

Laboratory of Parasitology and Immunoallergy. Centro de Investigación y Estudios Avanzados “Lucio Lascaray” and Faculty of Pharmacy. University of the Basque Country.

Pº Universidad 7. 01006-Vitoria. Spain and *Food Research Institute Prague. Radiová, 7, 10231 Praha 10. Czech Republic

WP3: Development

of innovative

methodologies for

allergen traces

detection.

Partner:

UPV/EHU

Immuno Solid Phase Allergen Chip Platform ( multiparametric FIA)

Protein microarrays technology does not work!

The equivalence zone (allergen↔antibody) is not reached with this tecnique,probably because the scarce amount of proteins in solid phase in relation to theallergen quantity in foods.

UPV/EHU

WP 4. Validation of detection methods with a

collaborative studies

Partner : UPV/EHU

VTT participated in the ring test ELISA for egg, gliadin and mustard samples organised by FRIP.

WP 1. Establishment of homogeneous reference

systems (allergens and validated detection

methods)

Partner 4: VTT Technical Research Centre of Finland

The production and purification of the recombinant ovalbumin was optimised, because purification of a commercial ovalbumin contaminated with ovomucoid to homogeneity was not successful. The recombinant ovalbumin was expressed in the soluble form in E.coli BL21 strain in to the periplasmic space. Purification was performed with ion exchange Purification was performed with ion exchange chromatography followed by an affinity column prepared from a commercial rabbit polyclonal anti-ovalbumin antibody. The yield of the purified ovalbumin was ~0.5 mg from a 1.8 L shake flask cultivation. The homogeneous recombinant ovalbumin will be used for the isolation of IgEantibodies, this was not accomplished completely during the “DETECTION OF TRACES OF ALLERGENS IN FOODS (PROJECT 08125)”.

WP3: Development of innovative methodologies for

allergen traces detection


Task 1: Generation of recombinant anti-ovalbumin and anti-ovomucoid IgE antibodies

In the SAFEFOODERA project VTT Research Centre of Finland has focused on the milk and egg allergies to develop recombinant IgEantibodies and allergens as well as optimize and validate immunoassay formats for specific and sensitive detection of trace amounts of allergens in food.

A human IgE scFv library from a clinically validated, voluntary egg-allergic patient has been constructed. The blood donor for the

…/… ovomucoid-specific IgE scFv fragments were converted to Fab fragments produced, purified and their binding properties characterised. Two of these antibodies bind ovomucoid with a high, nanomolar, affinity. A sensitive ovomucoid immunoassay applying the best recombinant IgE Fab fragment as the detection antibody has been optimised. These results will be published (Reinmanet al. manuscript in preparation).

Ovalbumin specific IgE antibodies were not isolated during the project due to the ovomucoid contamination of the commercial ovalbumin preparation. The commercial ovalbumin was subjected to further allergic patient has been constructed. The blood donor for the

construction of IgE library had very high allergen-specific IgE levels for several different allergens including Gal d 1 (ovomucoid) and Gal d 2 (ovalbumin) as determined by Phadia ISAC.

Selection of recombinant IgE antibodies was first carried out using commercial ovalbumin (Sigma, A2512). The ovalbumin was chemically biotinylated and the selection was performed in solution to promote isolation of antibodies binding conformational epitopes. The enrichment of the phages was observed after first and second selection rounds. Surprisingly, when the binding specificity of the isolated clones was characterised further, it was observed that they are binding to ovomucoid, regardless that ovalbumin was used in the selection. It is known that the commercial ovalbumin contains ovomucoid as an impurity and this is the reason for isolating ovomucoid specific antibodies although ovalbumin was used as the selection antigen. ../…

preparation. The commercial ovalbumin was subjected to further purification experiments in order to get rid of the ovomucoidcontamination, but these were not successful. To obtain a homogeneous preparation a production and purification of the recombinant ovalbumin was optimised. Recombinant ovalbumin was expressed in a soluble form in E.coli and purified with an immunoaffinity column. This homogeneous recombinant ovalbumin has been used to select antibodies from the patient specific library, but the characterisation of clones is still on-going.

In addition to the development of recombinant IgE antibodies we aimed to isolate IgG antibodies from phage display libraries constructed from mice immunized with ovalbumin, ovomucoid or beta-lactoglobulin, one of the major allergens of cow’s milk. The goal was to isolate allergen specific capture antibodies from these libraries. However, the project resources were not sufficient to complete this task.

WP3: Development of innovative methodologies for

allergen traces detection


Task 2: Optimisation of allergen traces immuno-detection systemsPartner 4: VTT Technical Research Centre of Finland

Beta-lactoglobulin (BLG) detection assay (VTT)

A BLG sandwich assay was optimised by using an earlier isolated high affinity recombinant IgE Fab fragment (Jylhä et al. (2009) J. Immunol. Methods 350, 63) The aim was to label the IgE Fab fragment with a fluorescent label, but this approach was not valid since the binding activity of the antibody was decreased substantially upon labelling. The BLG sandwich assay was established by using a high affinity rabbit polyclonal as the capture antibody (Mäkinen-polyclonal as the capture antibody (Mäkinen-Kiljunen, S., Palosuo, T.(1992) Allergy 47, 347). The IgE Fab fragment was used for the detection with in combination with an alkaline phosphatase labelled anti-human IgG antibody. By this assay set-up a sensitivity level of 1 µg/ L of BLG from milk samples was achieved.

Ovomucoid detection assay (VTT)

The ovomucoid detection assay was established by using the best recombinant IgE Fab fragment isolated from the patient specific library as the detection antibody. In the sandwich assay a commercial polyclonal rabbit anti-ovomucoid antibody is used as the capture antibody and for the detection the recombinant IgE Fab fragment recognised by an alkaline phosphatase conjugated anti-human IgGantibody. The detection level of ovomucoid was 0.01 mg/l. Isolated

WP 4. Validation of detection methods with a

collaborative studies


VTT participated in the ring test ELISA for egg and mustard samples organised by FRIP.

WP2.- Evaluation of Food Processing on Allergen Detectability

In general we have observed that β-Lactoglubulin is more sensitive in pressure treatments. However,

depending on the pH of the medium and intense heat treatment, can hide the presence of this protein in

foods when analysed by ELISA testfoods when analysed by ELISA test

Our results underline the fact that the determination of allergenic proteins in food products is greatly

influenced by the particularities of ELISA format used as well as by processing conditions applied to

food products. These considerations should be taken into account for a correct interpretation of results

obtained when using different immunoassays to detect allergens in foods


Temperature/time effect

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Effect of pressure treatment at pH 6.8 on the detection of β-LG by ELISA sandwich

Effect of thermal treatment at pH 6.8 on the detection of β-LG by ELISA sandwich.


Heat treatment pH 6.8

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Effect of medium composition at pH 4.6 on the detection of β-LG by ELISA sandwich after heat treatment. Samples are identified by the following numbers: (1) 2.5 mg/mL β-lactoglobulin, (2) β-LG + Lactose, (3) β-LG + Sucrose, (4) β-LG + Glucose, (5) β-LG + Fructose, (6) β-LG + Starch and (7) β-LG + Gelatine.

Effect of medium composition at pH 4.6 on the detection of β-LG by ELISA sandwich after heat treatment. Samples are identified by the following numbers: (1) 2.5 mg/mL β-lactoglobulin, (2) β-LG + Lactose, (3) β-LG + Sucrose, (4) β-LG + Glucose, (5) β-LG + Fructose, (6) β-LG + Starch and (7) β-LG + Gelatine.

High Pressure Treatment pH 6.8

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450 Mpa- 5 min.

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Effect of medium composition at pH 4.6 on the detection of β-LG by ELISA sandwich after pressure treatment at 450 and 600 MPa for 2.5 and 5 minutes. Samples are codified by the following numbers: (1) 2.5 mg/mLβ-lactoglobulin, (2) β-LG + Lactose, (3) β-LG + Sucrose, (4) β-LG + Glucose, (5) β-LG + Fructose, (6) β-LG + Starch and (7) β-LG + Gelatine.

Effect of medium composition at pH 6.8 on the detection of β-LG by ELISA sandwich after pressure treatment at 450 and 600 MPa for 2.5 and 5 minutes. Samples are codified by the following numbers: (1) 2.5 mg/mLβ-lactoglobulin, (2) β-LG + Lactose, (3) β-LG + Sucrose, (4) β-LG + Glucose, (5) β-LG + Fructose, (6) β-LG + Starch, (7) β-LG + Gelatine, (8) β-LG + Ovomucoid and (9) β-LG + Casein

Fructose, (6) β-LG + Starch and (7) β-LG + Gelatine.LG + Sucrose, (4) β-LG + Glucose, (5) β-LG + Fructose, (6) β-LG + Starch and (7) β-LG + Gelatine.

WP3.- Development of innovative methodologies for allergen traces detection

We have obtained a recombinant scFv library from sera of Anisakis simplex immunized

Rabbits. This library can be used to obtain recombinant IgE antibodies by means of Phage

Display technique

The recombinant antibodies are useful to design more sensitive detection systems toThe recombinant antibodies are useful to design more sensitive detection systems to

detect trace Anisakis allergens in seafood

Ring trial: Conducted by FRIP (D. Gabrovska) and all participantes

MUSTARD PROTEINS DETECTION IN FOODS

Ring trial: Conducted by FRIP (D. Gabrovska) and all participantes

EGG WHITE PROTEINS DETECTION IN FOODS

�The parameters that define (sensitivity, specificity, etc) the current diagnostic methods for the detection of allergens in foods need to be improved .

TO IMPROVE THESE PARAMETERS TO OFFER MORE SENSITIVE AND SPECIFIC METHODS TO TRACES ALLERGEN DETECTION

� Validated methods need to be obligatory to ensure that food labelling is in the compliancewith legal demands.

VALIDATION ACCORDING TO THE LEGAL REQUIREMENTS

KEY FACTORS SUPPORTING THE CONCEPT OF EUROPEAN COLLABORATIVEWORK FOR THIS PROJECT AND EXPEDCTED BENEFITS

VALIDATION ACCORDING TO THE LEGAL REQUIREMENTS

�The development of new validated and homogeneous reagents and standards allows to fulfil more accurately the detection limits required for food allergens.

�To work under the same protocol and with the same validated standards are the key elements for the successful evaluation and comparison of the results obtained within the consortium partners.

USE OF WELL KNOWN METHODS WITH WIDE CONSENSUS. INVESTIGATION OF NEW REAGENTS AND NEW NEEDS TO COVER THE MAXIMUM OF ACCURACY

� To set homogeneous reference systems (standards, allergens, antibodies and validated detection methods).

� Evaluation of food processing on allergen detectability

� Development of innovative methodologies and reagents for allergen traces detection

� Validation of detection methods through collaborative studies (ring trials)

EXPECTED RESULTS AND IMPLEMENTATION

� Validation of detection methods through collaborative studies (ring trials)

Diffusion and exploitation of results

(Institutions, patents –if required, publications and congresses communications, position reports, authorities, consumers associations, bussiness companies, QC departments, research labs, …)

• How will your project strengthen European food safety?

• How will the project results be implemented?

• Define the three main target groups of your project• Define the three main target groups of your project

• How does your project benefit from being a European collaboration project?

1. How will your project strengthen European food safety?

The labeling of the content of allergens in foods is a must

•Needs: Standardization of methods to measure traces of allergens in foods

Ring trials: Multicentric evaluation of the ELISA as basic assay for the detection of traces

of allergens in foods (egg, milk, mustard, wheat).

•Needs: Development of alternative methods to detection of trace of allergens in foods

Development of chimeric antibodies with different sensitivity and specificity to quantify

a high number of allergens using multiparametric platforms .

Use of alternative platforms (inhibition immunoassays) to detecting food individualized

allergens .

•Needs: Detection of traces of allergens through their encoding genes

Detection of allergens of fish parasites (Anisakis) using “omics” alternative methods.

2. How will the project results be implemented?

• Availability of validated tests with universal applicability

• Advances in the detection of non available allergens by DNA and othermolecular approaches.

Research

Industrialaplications

Markets

Detecting traces of allergens in foods”. International

Innovation. Disseminaring science, research and

technology. Research Media Ltd. 204 Cheltenham Road.

Bristol, BS6 5QZ UK. Pp.: 67-69. ISSN: 2041-4551









Book of Abstracts, 4th International Symposium on Recent Advances in Food Analysis, November 4-6, 2009, Prague, Czech Republic, pages 498 and 508, ISSN 978-80-7080-726-2

Symposium on Recent Advances in Food Analysis, November 4-6, 2009, Prague.

Fruit & Veg Processing. 1st Euro-Mediterranean Symposium. The Abstracts book.

Joint Research Unit for Safety and Quality of Plant products, INRA/University of

Avignon. Book of abstracts, pp: 130. 2011.

3. Define the three main target groups of your project

1. Standardization of classical methods to quantify traces of

allergens in foods

2. Development of alternative methods with high sensitivity and

specificity

3. To transfer the need of the food labeling and the need of

legislation to the interested forum: people, experts and authorities

4. How does your project benefit from being a European collaboration project?

• Developing and validation of new tests and new technologies

for the detection of allergens in foods.

• Unification of valid criteria for reporting on the composition

and quantity of relevant food allergens.

• Agreements for the labeling.

• Clinically relevant allergen panel design.

[email protected]

Documents

Safefoodera project final meeting copenhaguen 06-2011x · En los últimos años se han ensayado con algún éxito medida de desensibilización según las pautas clásicas de la inmunoterapia