G Pauli

University of Strasbourg, Strasburg, Alsace, France

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Publications (486)1087.97 Total impact

  • G. Pauli · A. Nardi · C. Metz-Favre · F. de Blay

    No preview · Article · Dec 2015 · Revue Française d'Allergologie
  • C. Wurmser · A. Roos · C. Kokou · C. Metz-Favre · G. Pauli

    No preview · Article · Apr 2015 · Revue Française d Allergologie

  • No preview · Article · Jan 2015
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    ABSTRACT: Background: 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. Objective: To clone and produce Fra e 2 (profilin) and Fra e 3 (polcalcin) as recombinant proteins and evaluate their immunological properties using the natural forms obtained from ash pollen. Methods: Total RNA from ash pollen was used as a template to obtain the specific complementary DNA (cDNA) sequences of the 2 panallergens. The cDNA-encoding sequences were cloned into the pET11b expression vector and used to transform BL21 (DE3) Escherichia coli cells. Proteins were expressed, purified by chromatography, and characterized structurally by circular dichroism, mass spectrometry, and immunologically by western blot and ELISA using profilin and polcalcin polyclonal antibodies and human sera from ash pollen-sensitized patients. Results: Profilin and polcalcin amino acid sequences from ash pollen showed a high degree of identity with homologous allergens from different sources. The cDNA-encoding allergen sequences were expressed as nonfusion recombinant proteins and purified to homogeneity. Secondary structure values were similar to those obtained from other members of these families. Allergenic properties of the recombinant allergens were observed to be equivalent to those of the natural counterparts of F excelsior pollen. Conclusions: Fra e 2 and Fra e 3 recombinant allergens might be used in clinical diagnosis to determine profilin- and polcalcin-specific IgE levels present in the sera of ash pollen-sensitized patients, thus facilitating the finding of the sensitizing source in areas with complex sensitization profiles.
    No preview · Article · Sep 2014 · Journal of investigational allergology & clinical immunology: official organ of the International Association of Asthmology (INTERASMA) and Sociedad Latinoamericana de Alergia e Inmunología
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    Marianne van Hage · Gabrielle Pauli
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    ABSTRACT: Allergen-specific immunotherapy (SIT) offers a disease specific causative treatment by modifying the allergen-specific immune response allowing tolerance to higher doses of allergen and preventing progression of allergic diseases. It may be considered in patients allergic to furry animals. Current mammalian allergy vaccines are still prepared from relatively poorly defined allergen extracts and may induce immediate and late phase side effects. Although the mechanisms of SIT are still not fully understood, the more recent approaches report different strategies to reduce both allergen-specific IgE as well as T cell reactivity. The availability of recombinant allergens and synthetic peptides from the mammalian species has contributed to formulating new allergy vaccines to improve SIT for furry animal allergy. The majority of studies have focused on the major cat allergen Fel d 1 due to its extensive characterization in terms of IgE and T cell epitopes and to its dominant role in cat allergy. Here we review the most recent approaches, e.g., synthetic peptides, recombinant allergen derivatives, different hypoallergenic molecules, and recombinant allergens coupled to virus-like particles or immunomodulatory substances as well as strategies targeting the allergen to Fcγ receptors and the MHC class II pathway using a new route for administration. Many of the new vaccines hold promise but only a few of them have been investigated in clinical trials which will be the gold standard for evaluation of safety and efficacy in allergic patients.
    Full-text · Article · Mar 2014 · Frontiers in Immunology
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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.
    No preview · Article · Mar 2014 · Revue Française d'Allergologie
  • 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.
    No preview · Article · Nov 2013 · Revue Française d'Allergologie
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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.
    No preview · Article · Nov 2013 · Revue Française d'Allergologie
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    Verena Niederberger · Julia Eckl-Dorna · Gabrielle Pauli
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    ABSTRACT: Over the last 25 years, recombinant allergens from all important allergen sources have been cloned and are now available as recombinant proteins. These molecules can be produced in practically unlimited amounts without biological or batch-to-batch variability. It has been shown in provocation tests that recombinant allergens have similar clinical effects as their natural counterparts. With the help of these tools it is possible to reveal the precise reactivity profiles of patients and to uncover and differentiate cross-reactivity from genuine sensitization to an allergen source. Although it has been shown some time ago that it would be possible to replace crude allergen extracts with recombinant allergens for skin prick testing, and even though the use of allergen components can improve routine diagnosis, these tools are still not available for clinical routine applications. The use of provocation tests is a crucial step in the development of new, hypoallergenic vaccines for therapy of allergic disease. Here we describe important provocation methods (skin prick test, intradermal test, atopy patch test, nasal provocation, colonoscopic provocation test) and give an overview of the clinical provocation studies which have been performed with recombinant allergens so far.
    Preview · Article · Aug 2013 · Methods
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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.
    No preview · Article · Jul 2013 · Clinical & Experimental Allergy
  • 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.
    No preview · Article · Apr 2013 · Revue des Maladies Respiratoires
  • 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.
    No preview · Article · Apr 2013 · Revue des Maladies Respiratoires
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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.
    Full-text · Dataset · Jan 2013

  • No preview · Article · Jan 2012 · Revue des Maladies Respiratoires
  • Source
    [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.
    Full-text · Article · Jan 2012 · Allergy
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    C Metz-Favre · G Pauli · J C Bessot · F De Blay
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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.
    Full-text · Article · Dec 2011 · European annals of allergy and clinical immunology
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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.
    No preview · Article · Nov 2011 · Revue Française d Allergologie
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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.
    Preview · Article · Oct 2011 · European annals of allergy and clinical immunology
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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.
    Full-text · Article · May 2011 · Allergy
  • 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.
    No preview · Article · Apr 2011 · Revue des Maladies Respiratoires

Publication Stats

5k Citations
1,087.97 Total Impact Points

Institutions

  • 1992-2014
    • University of Strasbourg
      • • Faculty of Medicine
      • • Service de Pneumologie
      Strasburg, Alsace, France
    • Institut Hospitalo-Universitaire
      Pessac, Aquitaine, France
  • 1971-2014
    • IHU de Strasbourg
      Strasburg, Alsace, France
  • 1985-2013
    • CHRU de Strasbourg
      Strasburg, Alsace, France
  • 2008
    • Hopitaux Civils De Colmar
      Kolmar, Alsace, France
  • 2006
    • Centre de Pneumologie et d'Allergologie
      Avinyó, Provence-Alpes-Côte d'Azur, France
  • 2005
    • Indoor Biotechnologies Inc
      Charlottesville, Virginia, United States
    • Ain Shams University
      Al Qāhirah, Muḩāfaz̧at al Qāhirah, Egypt
  • 2003
    • Institut des Systèmes Complexes, Paris Île-de-France
      Lutetia Parisorum, Île-de-France, France
  • 1994-2001
    • French Institute of Health and Medical Research
      Lutetia Parisorum, Île-de-France, France
  • 2000
    • CHU de Lyon - Groupement Hospitalier Edouard Herriot
      Lyons, Rhône-Alpes, France
  • 1999
    • Institut Pasteur
      Lutetia Parisorum, Île-de-France, France
  • 1998
    • Unité Inserm U1077
      Caen, Lower Normandy, France
  • 1993-1995
    • French National Centre for Scientific Research
      Lutetia Parisorum, Île-de-France, France
  • 1991
    • Centre Hospitalier Régional et Universitaire de Besançon
      Becoinson, Franche-Comté, France
    • Centre Hospitalier Universitaire de Limoges
      Limages, Limousin, France
  • 1988
    • Hospices Civils de Lyon
      Lyons, Rhône-Alpes, France
  • 1982-1987
    • Centre Hospitalier Universitaire de Dijon
      • Pneumology Service
      Dijon, Bourgogne, France
  • 1984
    • Centre Hospitalier Régional d'Orléans
      Orléans, Centre, France