G Pauli

University of Strasbourg, Strasburg, Alsace, France

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Publications (431)787.43 Total impact

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    ABSTRACT: Study objective The aim of this study was to investigate the added value of using a panel of fish allergens in component-resolved diagnosis of fish-allergic patients. Patients and methods Sixty-two patients were diagnosed as being allergic to fish by clinical history and with positive skin prick-tests and specific IgE to fish extracts (cod, salmon and tuna). Allergen-specific IgE levels to fish parvalbumin, enolase, aldolase and gelatin were quantified by Elisa. Results Forty-five of the patients were sensitized to parvalbumin. Among the cod parvalbumin-sensitized patients, 50% were also sensitized to both enolase and aldolase. Of the patients with positive skin tests to salmon and to tuna (75.6% and 67.6%, respectively), isolated sensitization to parvalbumin was observed. Mean levels of specific IgE to cod and enolase parvalbumin were positively correlated with the severity of the patients’ clinical symptoms; this was not the case for cod aldolase. Patients were clustered into three groups according to their parvalbumin-specific IgE-reactivity. In the first group, the 36 patients who were sensitized to three different fish reported mild to severe symptoms; their symptoms were correlated with the presence of IgE to total cod extract and to cod parvalbumin. The second group of 9 mono-sensitized patients had only minor symptoms of fish allergy, most often to salmon; their symptoms were positively correlated with specific IgE levels of salmon extract and cod parvalbumin-specific IgE. The third group consisted of 17 patients who were sensitized to a small number of fish; they had moderate to severe symptoms. While this group of patients had no detectable parvalbumin-specific IgE, 70.6% of them were found to have IgE specific for fish aldolase, enolase or gelatin; in this group, the presence of IgE specific for cod was rarely observed. Conclusion The use of a panel with a number of allergenic fish proteins may contribute to the improvement of the diagnosis of fish allergy. Specific sensitization profiles appear to be associated with certain profiles of clinical symptoms.
    Revue Française d'Allergologie 01/2014; · 0.35 Impact Factor
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    ABSTRACT: Ash (Fraxinus excelsior) is an important source of allergenic pollen in temperate areas of Europe. Profilin and polcalcin are 2 important panallergens involved in cross-reactivity between different sources.
    Journal of investigational allergology & clinical immunology. 01/2014; 24(4):257-66.
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    ABSTRACT: This mini review focuses on four rare sources of pollinosis. Oak pollinosis, which is seldom observed during periods of pollinosis due to other common trees, occurs during the same period as grass pollinosis. The major oak pollen allergen Que a 1 has close homology with birch pollen allergen Bet v 1, and positive cutaneous reactions to oak extract are usually due to sensitization to birch pollen rather than to oak pollen. A detailed clinical history of the seasonality of the symptoms is fundamental since birch and oak flowering seasons rarely overlap. Plane tree (Platanus) pollinosis is very rare in France and mono-sensitization to plane tree pollen is found only exceptionally. In contrast, plane tree sensitization is the most frequent pollen sensitization found in Spain, second to grass pollen sensitization. It is considered a risk factor for vegetable food allergies. When the two major plane tree allergens Pla a 1 and Pla a 2 are used in in vitro tests, a positive diagnosis can be established in 100% of the cases. Plantago (Plantain) pollinosis can occur in successive waves from March to September. Rare in France, it occurs often in the United Kingdom. The major plantago allergen Pla l 1 shares common sequences with the major allergen of the Oleaceae family, which may explain frequent co-sensitization. Melon allergy and sensitization to plantago pollen are often associated. Mugwort (Artemisia vulgaris) pollinosis has its own period of flowering in the North and the South of France. This pollen is the major cause of pollinosis during autumn in China. Co-sensitization to Artemisia and Ambrosia (ragweed) pollen is often observed. Artemisia pollen has a specific major allergen, Art v 1, but other allergens may be responsible for cross-reactions with Ambrosia pollen, especially Art v 6, a pectatelyase. Numerous, often very complex food cross-reactions are now better understood at the molecular level. In addition to the published data, the results of a retrospective study of 273 allergen skin tests performed in patients with pollinosis will be reported. The results of this study point out the rare occurrence of co-sensitization to the four above pollens and the frequent association of sensitization to various other pollens.
    Revue Française d'Allergologie 01/2014; · 0.35 Impact Factor
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    ABSTRACT: The majority of fish-allergic patients are sensitized to parvalbumin, known to be the cause of important IgE cross-reactivity among fish species. Little is known about the importance of fish allergens other than parvalbumin. The aim of this study was to characterize hitherto undefined fish allergens in three commonly consumed fish species, cod, salmon and tuna, and to evaluate their importance for in vitro IgE-diagnosis in addition to parvalbumin and fish gelatin. Sixty-two patients were diagnosed by clinical history, skin prick tests and specific IgE to fish extracts. Two new fish allergens from cod, salmon and tuna were identified by microsequencing. These proteins were characterized by immunoblot, ELISA and mediator release assay. Purified parvalbumin, enolase, aldolase and fish gelatin were used for quantification of specific IgE in ELISA. Parvalbumin and two other allergens of 50 and 40 kDa were detected in IgE-immunoblots of cod, salmon and tuna extracts by most patient sera. The 50 and 40 kDa proteins were identified as beta-enolase and fructose-bisphosphate aldolase A respectively. Both purified enzymes showed allergenic activity in the mediator release assay. Indeed, 72.6% of the patients were sensitized to parvalbumin, 20% of these had specific IgE to salmon parvalbumin only. IgE to enolases were found in 62.9% (0.5-95.0 kUA /L), to aldolases in 50.0% (0.4-26.0 kUA /L) and to fish gelatin in 19.3% (0.4-20.0 kUA /L) of the patients. Inter-species cross-reactivity, even though limited, was found for enolases and aldolases by IgE-inhibition ELISA. Fish enolase and aldolase have been identified as important new fish allergens. In fish allergy diagnosis, IgE to enolase and aldolase are especially relevant when IgE to parvalbumin are absent.
    Clinical & Experimental Allergy 07/2013; 43(7):811-822. · 4.79 Impact Factor
  • G Pauli, C Metz-Favre
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    ABSTRACT: The association of food allergies and pollinosis are numerous, implicating tree, grass and weed pollens on one hand and on the other, several plant foods which after ingestion can induce an oral syndrome or more severe reactions such as urticaria, Quincke's edema, asthma and even anaphylactic shock. The molecular basis of cross reactions between pollens and vegetable food allergens is increasingly understood. The principal allergens involved are those of the Bet v 1 family, and profilins found in all pollens as well as in many fruits and vegetables; these two groups of allergens are denatured by high temperatures and by gastric enzymes, in contrast to LTP, which is only found in weeds and some tree pollens. Other molecules can be involved in cross reactions such as Bet v 6 (an isoflavone reductase), 1 beta glucanases and thaumatine-like proteins. Inhibition experiments confirmed that the epitopes responsible for primary sensitization come mainly from pollen allergens; the cross-reactive molecular allergen is related to the geographic environment of the patients. The practical aspects of managing these patients are underlined: explanations of co-sensitization, explanations for the lack of efficacy of some extracts, usefulness of a molecular diagnosis obtained either by CAP or microarray, prediction of severe clinical reactions induced by specific molecular allergens and the effectiveness of pollen immunotherapy on the cross-related food allergy.
    Revue des Maladies Respiratoires 04/2013; 30(4):328-37. · 0.50 Impact Factor
  • G. Pauli, C. Metz-Favre
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    ABSTRACT: Introduction The association of food allergies and pollinosis are numerous, implicating tree, grass and weed pollens on one hand and on the other, several plant foods which after ingestion can induce an oral syndrome or more severe reactions such as urticaria, Quincke's edema, asthma and even anaphylactic shock. Background The molecular basis of cross reactions between pollens and vegetable food allergens is increasingly understood. The principal allergens involved are those of the Bet v 1 family, and profilins found in all pollens as well as in many fruits and vegetables; these two groups of allergens are denatured by high temperatures and by gastric enzymes, in contrast to LTP, which is only found in weeds and some tree pollens. Other molecules can be involved in cross reactions such as Bet v 6 (an isoflavone reductase), 1 beta glucanases and thaumatine-like proteins. Inhibition experiments confirmed that the epitopes responsible for primary sensitization come mainly from pollen allergens; the cross-reactive molecular allergen is related to the geographic environment of the patients. Conclusions The practical aspects of managing these patients are underlined: explanations of co-sensitization, explanations for the lack of efficacy of some extracts, usefulness of a molecular diagnosis obtained either by CAP or microarray, prediction of severe clinical reactions induced by specific molecular allergens and the effectiveness of pollen immunotherapy on the cross-related food allergy.
    Revue des Maladies Respiratoires. 04/2013; 30(4):328–337.
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    ABSTRACT: Work‐related asthma (WRA) is a relevant problem in several countries, is cause of disability and socioeconomic consequences for both the patient and the society and is probably still underdiagnosed. A correct diagnosis is extremely important to reduce or limit the consequences of the disease. This consensus document was prepared by a EAACI Task Force consisting of an expert panel of allergologists, pneumologists and occupational physicians from different European countries. This document is not intended to address in detail the full diagnostic work‐up of WRA, nor to be a formal evidence‐based guideline. It is written to provide an operative protocol to allergologists and physicians dealing with asthma useful for identifying the subjects suspected of having WRA to address them to in‐depth investigations in a specialized centre. No evidence‐based system could be used because of the low grade of evidence of published studies in this area, and instead, ‘key messages’ or ‘suggestions’ are provided based on consensus of the expert panel members.
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    ABSTRACT: Defensins are small disulfide-rich proteins, which are widely distributed in plants. They all have a knottin domain with an abcabc topology, which is characterized by the existence of a knot interlaced with disulfide bridges. The knot is made up of a disulphide bridge, which is crossed by a loop formed by two other disulfide bridges connected to a peptide backbone. This structure denotes that the crossing disulfide bridge(s) is oriented perpendicularly to the two other disulfide bridges forming the loop. The knottin domain can be connected either by a long C-terminal tail rich in hydroxyproline (definsins with a long chain with about 110 amino acids) or by a short C-terminal chain (with about 50 amino acids). The Art v 1 allergen of mugwort (Artemisia vulgaris) pollen is the prototype of the long-chain defensins whereas defensins of the Brassicaceae essentially belong to the short-chain defensin group. Except for Art v 1 and the closely-related Amb a 4 allergen from ragweed (Ambrosia artemisiifolia) pollen, both of which are well-known allergens, the allergenicity of other plant defensins is far from being clinically demonstrated. Nevertheless, the fact that electropositive amino acid patches (with lysine and arginine) and electronegative patches (with aspartic and glutamic acids) which have been identified on the surface of both Art v 1 and Amb a 4 also exist in a few other defensins suggests that other defensins could also be allergenic. Further clinical and immunological investigations are necessary to ascertain the allergenicity of these putative defensin allergens.
    Revue Française d'Allergologie 01/2013; 53(7):585–590. · 0.35 Impact Factor
  • G. Pauli, J.-C. Bessot
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    ABSTRACT: The taxonomy, anatomy, life cycle and ecology of Pyroglyphidae mites and strorage mites (Acaridae, Glycyphagidae, B.tropicalis) are described. Morphologies are quite similar but fecundity is superior in storage mites compared to the Pyroglyphides. Relative humidity is the main parameter, which regulates mite development. Bedding is the ecological niche of Pyroglyphidae which feed on human skin. Food products are the storage mites biotope from which they can spread in urban dwellings. B.tropicalis, in tropical regions is a true domestic mite. Since 1988, molecular knowledge has considerably increased and structures and functions have been determined for most of mite allergens. Of the 23 denominated allergens, the major IgE-binding has been reported for groups 1 and 2 accounting for 40-60% of the anti-house dust mite titers. Der p 1, 2, 4, 5, 7 allergens account for about 80% of the IgE-response. The IgE-binding to groups 3, 8, 10, 20 is low. Most allergens are proteolytic enzymes: Der p1 for instance is a cysteine protease. Der p 2 has structural homology with MD-2, a co-receptor of the Toll-like receptor (TLR4) whose ligand is LPS. Knowledge of the mite allergens structure has allowed better interpretation of cross reactions between allergens from the same family or from more distant families. Molecular epidemiology has allowed a better choice of allergen molecules useful for diagnosis and also for future immunotherapy.
    Revue Française d'Allergologie 01/2013; 53:45–58. · 0.35 Impact Factor
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    [Show abstract] [Hide abstract]
    ABSTRACT: Work-related asthma (WRA) is a relevant problem in several countries, is cause of disability and socioeconomic consequences for both the patient and the society and is probably still underdiagnosed. A correct diagnosis is extremely important to reduce or limit the consequences of the disease. This consensus document was prepared by a EAACI Task Force consisting of an expert panel of allergologists, pneumologists and occupational physicians from different European countries. This document is not intended to address in detail the full diagnostic work-up of WRA, nor to be a formal evidence-based guideline. It is written to provide an operative protocol to allergologists and physicians dealing with asthma useful for identifying the subjects suspected of having WRA to address them to in-depth investigations in a specialized centre. No evidence-based system could be used because of the low grade of evidence of published studies in this area, and instead, 'key messages' or 'suggestions' are provided based on consensus of the expert panel members.
    Allergy 01/2012; 67(4):491-501. · 5.88 Impact Factor
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    ABSTRACT: The authors describe an unusual case of LTP allergy. A 35 years old patient presented repeated episodes of angiooedema after food intake and complained 10 years ago of contact urticaria and rhinoconjunctivitis when exposed to cannabis leaves and to marijuana smoke. The suspected responsible foods, such as wheat flour in bread, are known to contain LTR Oral syndrome occurred after ingestion of walnuts. Cutaneous tests confirmed immediate responses to several flours and nuts and also to cannabis leaf and flower. A few months later he had similar accidents following peach ingestion and drinking of beer and several wines which all induced positive skin tests. Serological investigations using ImmunoCAP and ISAC microarray confirmed IgE positivity for n Pru p3, r Cor a 8 and n Art v3. It was assumed that sensitization to LTP, the major allergen of cannabis, was responsible of the primary sensitization and induced further LTP food allergies.
    European annals of allergy and clinical immunology 12/2011; 43(6):193-5.
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    ABSTRACT: Taxonomy, morphology, biological cycle and ecology are compared between pyroglyphidae (Dermatophagoides) and storage mites (acaridae, glycyphagidae). Pyroglyphidae and storage mites have a similar morphology; however, some keys allow their differentiations, such as the presence of numerous hair-like structures on Glycyphagidae and the existence of a primitive urinary system in Acaridae. Storage mites fecundity is superior to these of Glycyphagidae. Optimal temperature and humidity are respectively 30°C and 80 % RH. If bedding dust is the main pyroglyphidae feeding habit, storage mites mainly feed on damaged grains and moulds. Storage mites were initially associated with agricultural environment. However, these mites are also present in urban homes. Rhinitis and asthma are the main storage mite symptoms but they can also be able to induce dermatological and anaphylactic symptoms. Major allergens from storage mites are present in group 2. Cross reactivity at the immunoglobulin E (IgE)-level is common between group 2 storage mite allergens. Cross-reactivity studies of pyroglyphidae and storage mite allergens suggest a low cross reactivity between pyroglyphidae and storage mites.
    Revue Francaise D Allergologie - REV FR ALLERGOL. 11/2011;
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    J C Bessot, G Pauli
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    ABSTRACT: Mite allergens from the Pyroglyphidae family are the most frequent and potent sources of perennial asthma and rhinitis. Since 1988 molecular knowledge has considerably increased and structures and functions have been determined for most of them. Of the 22 denominated allergens, Der p 1 and Der p 2 are major allergens recognized by more than 80% of lgE from Dpt allergic patients in Europe. Der p 4, Der p 5 and Der p 7 appeared to be intermediate allergens. The binding of IgE to groups 3, 6, 8, 9, 10 and 20 is constantly low. Most of the allergens can be identified by amino-acid sequences and the tertiary structure of the major allergens has been solved. Most Dpt mite allergens are proteolytic enzymes: Der p 1 for instance is a cysteine protease. Der p 2 has structural homology with MD-2, a co-receptor of the Toll-like receptor (TLR4) whose ligand is LPS. Knowledge of the mite allergens structure has allowed a better interpretation of cross reactions between allergens from the same family or from more distant families. From a practical point of view molecular epidemiology has allowed a better choice of allergen molecules useful for diagnosis. Finally, new concepts of immunotherapy based on genetically engineered hypoallergenic variants of major allergens, used alone or in combination, can be considered.
    European annals of allergy and clinical immunology 10/2011; 43(5):141-56.
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    ABSTRACT: Cow's milk is one of the most common causes of food allergy. In two-thirds of patients, adverse symptoms following milk ingestion are caused by IgE-mediated allergic reactions, whereas for one-third, the mechanisms are unknown. Aim of this study was to investigate whether patients suffering from non-IgE-mediated cow's milk protein intolerance can be distinguished from persons without cow's milk protein intolerance based on serological measurement of IgG and IgA specific for purified cow's milk antigens. We determined IgG(1-4) subclass and IgA antibody levels to purified recombinant αS1-casein, αS2-casein, β-casein, κ-casein, α-lactalbumin, and β-lactoglobulin in four patient groups by ELISA: Patients with IgE-mediated cow's milk allergy (CMA, n=25), patients with non-IgE-mediated cow's milk protein intolerance (CMPI, n=19), patients with gastrointestinal symptoms not associated with cow's milk ingestion (GI, n=15) and control persons without gastrointestinal problems (C, n=26). Cow's milk-specific IgE levels were determined by ImmunoCAP. Only CMA patients had IgE antibodies to cow's milk. Cow's milk allergic patients mounted the highest IgG(1) and IgG(4) antibody levels to αS1-casein, αS2-casein, β-casein, κ-casein, and α-lactalbumin. No elevated levels of IgG(4) , IgA, and complement-binding IgG subclasses (IgG(1) , IgG(2) , IgG(3) ) to purified cow's milk allergens were found within the CMPI patients compared to persons without cow's milk protein intolerance (GI and C groups). Cow's milk protein intolerant patients cannot be distinguished from persons without cow's milk protein intolerance on the basis of IgG subclass or IgA reactivity to cow's milk allergens.
    Allergy 05/2011; 66(9):1201-7. · 5.88 Impact Factor
  • J-C Bessot, G Pauli
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    ABSTRACT: House dust mite allergens from the Pyroglyphidae family are one of the most frequent and potent causes of allergic sensitatisation. Since 1988, molecular knowledge has increased considerably and structures and functions have been determined for most of them. Of the 22 defined allergens, the major IgE-binding has been reported for groups 1 and 2 accounting for 40-60% of the anti-house dust mite titres. Der p 1, 2, 4, 5, 7 allergens account for about 80% of the IgE-response. Der p 4, 5, 7, 11, 14, 15 have a prevalence of sensitization of about 10% each. The IgE-binding to groups 3, 8, 10, 20 is low. Most of the allergens can be identified by amino-acid sequences and the tertiary structures of the major allergens have been solved. Most allergens are proteolytic enzymes: Der p1 for instance is a cysteine protease. Der p 2 has structural homology with MD-2, a co-receptor of the Toll-like receptor (TLR4) whose ligand is LPS. Knowledge of the structure of mite allergens has allowed better interpretation of cross-reactions between allergens from the same family or from more distant families. From a practical point of view: the occurrence of multisensitisation is better explained and molecular epidemiology has allowed a better choice of allergen molecules useful for diagnosis. Finally, new concepts of immunotherapy based on genetically engineered hypoallergenic variants of major allergens, used alone or in combination, may lead to useful therapeutic approach.
    Revue des Maladies Respiratoires 04/2011; 28(4):475-95. · 0.50 Impact Factor
  • J-C Bessot, G Pauli
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    ABSTRACT: The taxonomy, anatomy, life cycle and ecology of Pyroglyphidae mites and storage mites (Acaridae, Glycyphagidae, B. tropicalis) are described. Pyroglyphidae and storage mites have similar morphologies: they are octopods, with characteristic gnathosoma and sensory hairs. Salivary glands and the mid gut produce most of the allergens excreted, which are enzymatic proteins. Biological cycles and development are similar, although fecundity is superior in storage mites compared to the Pyroglyphides. Relative humidity is the main parameter, which regulates mite development, with a higher degree of temperature and humidity required for storage mites. Bedding is the ecological niche of Pyroglyphidae, which feed on human skin. Moulds and food products are the storage mite biotope from which they spread in the dwelling. Initially considered as rural mites, storage mites are also present in urban dwellings. B. tropicalis, in tropical regions is a true domestic mite. Because of this, it is justified to denominate Pyroglyphidae "house dust mites" and storage mites "domestic mites". In addition to the respiratory allergic symptoms, the storage mites can also cause occupational contact dermatoses.
    Revue des Maladies Respiratoires 02/2011; 28(2):227-39. · 0.50 Impact Factor
  • J.-C. Bessot, G. Pauli
    [Show abstract] [Hide abstract]
    ABSTRACT: The taxonomy, anatomy, life cycle and ecology of Pyroglyphidae mites and storage mites (Acaridae, Glycyphagidae, B. tropicalis) are described. Pyroglyphidae and storage mites have similar morphologies: they are octopods, with characteristic gnathosoma and sensory hairs. Salivary glands and the mid gut produce most of the allergens excreted, which are enzymatic proteins. Biological cycles and development are similar, although fecundity is superior in storage mites compared to the Pyroglyphides. Relative humidity is the main parameter, which regulates mite development, with a higher degree of temperature and humidity required for storage mites. Bedding is the ecological niche of Pyroglyphidae, which feed on human skin. Moulds and food products are the storage mite biotope from which they spread in the dwelling. Initially considered as rural mites, storage mites are also present in urban dwellings. B. tropicalis, in tropical regions is a true domestic mite. Because of this, it is justified to denominate Pyroglyphidae “house dust mites” and storage mites “domestic mites”. In addition to the respiratory allergic symptoms, the storage mites can also cause occupational contact dermatoses.
    Revue des Maladies Respiratoires. 01/2011; 28(2):227-239.
  • J.-C. Bessot, G. Pauli
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    ABSTRACT: Introduction House dust mite allergens from the Pyroglyphidae family are one of the most frequent and potent causes of allergic sensitatisation. Since 1988, molecular knowledge has increased considerably and structures and functions have been determined for most of them. Background Of the 22 defined allergens, the major IgE-binding has been reported for groups 1 and 2 accounting for 40–60% of the anti-house dust mite titres. Der p 1, 2, 4, 5, 7 allergens account for about 80% of the IgE-response. Der p 4, 5, 7, 11, 14, 15 have a prevalence of sensitization of about 10% each. The IgE-binding to groups 3, 8, 10, 20 is low. Most of the allergens can be identified by amino-acid sequences and the tertiary structures of the major allergens have been solved. Most allergens are proteolytic enzymes: Der p1 for instance is a cysteine protease. Der p 2 has structural homology with MD-2, a co-receptor of the Toll-like receptor (TLR4) whose ligand is LPS. Knowledge of the structure of mite allergens has allowed better interpretation of cross-reactions between allergens from the same family or from more distant families. Conclusions From a practical point of view: the occurrence of multisensitisation is better explained and molecular epidemiology has allowed a better choice of allergen molecules useful for diagnosis. Finally, new concepts of immunotherapy based on genetically engineered hypoallergenic variants of major allergens, used alone or in combination, may lead to useful therapeutic approach.
    Revue Des Maladies Respiratoires - REV MAL RESPIR. 01/2011; 28(4):475-495.
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    ABSTRACT: Cow's milk is one of the most common causes of food allergy affecting approximately 2.5% of infants in the first years of their life. However, only limited information regarding the allergenic activity of individual cow's milk allergens is available. To analyse the frequency of IgE reactivity and to determine the allergenic activity of individual cow's milk allergens. A nitrocellulose-based microarray, based on purified natural and recombinant cow's milk allergens was used to determine IgE reactivity profiles using sera from 78 cow's milk-sensitized individuals of varying ages. The allergenic activity of the individual allergens was tested using patients' sera for loading rat basophil leukaemia cells (RBL) expressing the α-chain of the human receptor FcεRI. Using the microarray and the RBL assay, cow's milk allergens were assessed for frequency of IgE recognition and allergenic activity. Moreover, the RBL assay allowed distinguishing individuals without or with mild clinical reactions from those with severe systemic or gastrointestinal symptoms as well as persons who grew out cow's milk allergy from those who did not. Component-resolved testing using milk allergen microarrays and RBL assays seems to provide useful additional diagnostic information and may represent a basis for future forms of prophylactic and therapeutic strategies for cow's milk allergy.
    Clinical & Experimental Allergy 12/2010; 40(12):1809-18. · 4.79 Impact Factor
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    ABSTRACT: Since tropomyosin is cross reactive in many arthropods, it was assumed that this highly conserved protein could be responsible for cross reactions in house dust mite (HDM) allergic patients who experienced adverse reactions after crustacean and mollusc ingestion. Here we report two clinical cases where the role of tropomyosin is a matter of debate. In the first case, the clinical history, as well as the results of in vivo and in vitro investigations, are in favour of a shrimp allergy without any snail allergy in a patient sensitized to HDM. In the second, the clinical history and the cutaneous tests are in favour of an allergy to snails without any allergy to shrimps in a patient suffering from HDM allergies. The clinical presentation is different in shrimp and snail allergies. In shrimp allergy, symptoms are mainly urticaria or angio-oedema. In snail allergies, adverse reactions are especially severe asthma. Shrimp tropomyosin is a dominant allergen in crustaceans whereas has a much less prominent role in HDM sensitization. Cross reactivities between HDM and snails have been confirmed by inhibition experiments. However, tropomyosin appears to be a minor allergen or even is not involved in snail allergy. It is necessary to clarify the allergens shared between HDMI and snails. The effects of HDM immunotherapy in snail allergy are questioned. Knowledge of taxonomy can contribute to more precise evaluation of cross reactivities between crustaceans and molluscs.
    European annals of allergy and clinical immunology 02/2010; 42(1):3-10.

Publication Stats

3k Citations
787.43 Total Impact Points

Institutions

  • 1987–2014
    • University of Strasbourg
      • • Faculty of Medicine
      • • Faculté de pharmacie
      • • Laboratoire d'Epidémiologie et de Santé Publique
      Strasburg, Alsace, France
  • 1985–2013
    • CHRU de Strasbourg
      Strasburg, Alsace, France
  • 2008–2011
    • Medical University of Vienna
      • Klinische Abteilung für Medizinisch-chemische Labordiagnostik
      Vienna, Vienna, Austria
    • Hopitaux Civils De Colmar
      Kolmar, Alsace, France
  • 2009
    • Public Research Centre for Health
      • Laboratory of Immunogenetics and Allergology (LIGA)
      Letzeburg, Luxembourg, Luxembourg
  • 1983–2009
    • Unité Inserm U1077
      Caen, Lower Normandy, France
  • 2004
    • Vienna General Hospital
      Wien, Vienna, Austria
    • Karolinska Institutet
      • Institutionen för medicin, Huddinge
      Solna, Stockholm, Sweden
  • 1999–2004
    • French Institute of Health and Medical Research
      Lutetia Parisorum, Île-de-France, France
  • 2003
    • Institut des Systèmes Complexes, Paris Île-de-France
      Lutetia Parisorum, Île-de-France, France
  • 2002
    • Société Française de Cardiologie
      Lutetia Parisorum, Île-de-France, France
  • 1996–2002
    • University of Vienna
      • Universitätsklinik für Innere Medizin I
      Vienna, Vienna, Austria
  • 1997
    • Institut de Génétique et de Biologie Moléculaire et Cellulaire
      Strasburg, Alsace, France
  • 1991–1994
    • Centre Hospitalier Régional et Universitaire de Besançon
      Becoinson, Franche-Comté, France
  • 1993
    • Civil Hospital, Raikot
      Rāikot, Punjab, India
  • 1987–1991
    • Centre Hospitalier Universitaire de Lyon
      • Service de Pneumologie
      Lyon, Rhone-Alpes, France
  • 1981–1988
    • Hospices Civils de Lyon
      Lyons, Rhône-Alpes, France
  • 1982–1985
    • Centre Hospitalier Universitaire de Caen
      Caen, Lower Normandy, France
  • 1984
    • Centre Hospitalier Régional d'Orléans
      Orléans, Centre, France