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1.
Eur Ann Allergy Clin Immunol ; 52(5): 205-209, 2020 09.
Artículo en Inglés | MEDLINE | ID: mdl-31594291

RESUMEN

Summary: Background and Objective. Sensitization and allergy to shrimp among Italian house dust mite allergic patients are not well defined and were investigated in a large multicenter study. Methods. Shrimp sensitization and allergy were assessed in 526 house dust mite (HDM)-allergic patients submitted to the detection of IgE to Der p 10 and 100 atopic control not sensitized to HDM. Results. Shrimp allergy occurred in 9% of patients (vs 0% of 100 atopic controls not sensitized to HDM; p minor 0.001). Shrimp-allergic patients were less frequently hypersensitive to airborne allergens other than HDM than crustacean-tolerant subjects (35% vs 58.8%; p minor 0.005). Only 51% of tropomyosin-sensitized patients had shrimp allergy, and these showed significantly higher Der p 10 IgE levels than shrimp-tolerant ones (mean 22.2 KU/l vs 6.2 KU/l; p minor 0.05). Altogether 53% of shrimp-allergic patients did not react against tropomyosin. Conclusions. Shrimp allergy seems to occur uniquely in association with hypersensitivity to HDM allergens and tropomyosin is the main shrimp allergen but not a major one, at least in Italy. Along with tropomyosin-specific IgE levels, monosensitization to HDM seems to represent a risk factor for the development of shrimp allergy among HDM allergic patients.


Asunto(s)
Antígenos Dermatofagoides/inmunología , Proteínas de Artrópodos/inmunología , Hipersensibilidad a los Alimentos/epidemiología , Tropomiosina/inmunología , Adolescente , Adulto , Animales , Reacciones Cruzadas , Femenino , Hipersensibilidad a los Alimentos/inmunología , Humanos , Inmunoglobulina E/metabolismo , Italia/epidemiología , Masculino , Persona de Mediana Edad , Penaeidae , Prevalencia , Pyroglyphidae , Adulto Joven
2.
J Investig Allergol Clin Immunol ; 29(2): 118-123, 2019 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-31017108

RESUMEN

BACKGROUND AND OBJECTIVE: Wheat ingestion can lead to disorders such as IgE-mediated food allergy and wheat-dependent exercise-induced anaphylaxis (WDEIA), both of which are associated with impaired quality of life and significant morbidity. Allergy to wheat is relatively benign in children, although its natural history in adults is still unknown. Objective: We used placebo-controlled challenge to evaluate the natural history of wheat hypersensitivity in atopic patients with adultonset wheat allergy. METHODS: We enrolled 13 patients from an initial cohort of adult patients with IgE-mediated wheat allergy (mean age, 40 years). After diagnosis, the patients observed a wheat-free diet and were followed as outpatients for 5 years to evaluate wheat exposure. Wheat-IgEtiters were determined at the end of follow-up, and a second wheat-challenge was performed. RESULTS: Ten out of 13 patients took part in the study. The mean period of wheat avoidance was 4.2 years. Three patients had spontaneously reintroduced wheat before the second evaluation, after a mean (IQR) of 28 (18-36) months, with only mild gastrointestinal discomfort at reintroduction. At the end of follow-up, 9 of the 10 patients were wheat-tolerant. Two patients had a history of WDEIA. We observed a reduction in IgE levels, with median (IQR) IgE falling from 2.77 (0.35-100) kU/L at diagnosis to 0.88 (0.1-20.8) kU/L. The association between IgE and a negative challenge result was not statistically significant. CONCLUSION: IgE-mediated wheat allergy in adults is benign and represents a temporary break in gastrointestinal tolerance. Future studies may improve our knowledge of wheat allergens, routes of and factors leading to sensitization, and prognostic biomarkers.


Asunto(s)
Hipersensibilidad al Trigo/epidemiología , Adolescente , Adulto , Alérgenos/inmunología , Reacciones Cruzadas/inmunología , Femenino , Estudios de Seguimiento , Humanos , Inmunoglobulina E/inmunología , Masculino , Persona de Mediana Edad , Evaluación del Resultado de la Atención al Paciente , Pronóstico , Pruebas Cutáneas , Triticum/efectos adversos , Hipersensibilidad al Trigo/diagnóstico , Hipersensibilidad al Trigo/inmunología , Adulto Joven
4.
J. investig. allergol. clin. immunol ; 29(2): 118-123, 2019. tab
Artículo en Inglés | IBECS | ID: ibc-184054

RESUMEN

Background: Wheat ingestion can lead to disorders such as IgE-mediated food allergy and wheat-dependent exercise-induced anaphylaxis (WDEIA), both of which are associated with impaired quality of life and significant morbidity. Allergy to wheat is relatively benign in children, although its natural history in adults is still unknown. Objective: We used placebo-controlled challenge to evaluate the natural history of wheat hypersensitivity in atopic patients with adult-onset wheat allergy. Methods: We enrolled 13 patients from an initial cohort of adult patients with IgE-mediated wheat allergy (mean age, 40 years). After diagnosis, the patients observed a wheat-free diet and were followed as outpatients for 5 years to evaluate wheat exposure. Wheat-IgE titers were determined at the end of follow-up, and a second wheat-challenge was performed. Results: Ten out of 13 patients took part in the study. The mean period of wheat avoidance was 4.2 years. Three patients had spontaneously reintroduced wheat before the second evaluation, after a mean (IQR) of 28 (18-36) months, with only mild gastrointestinal discomfort at reintroduction. At the end of follow-up, 9 of the 10 patients were wheat-tolerant. Two patients had a history of WDEIA. We observed a reduction in IgE levels, with median (IQR) IgE falling from 2.77 (0.35-100) kU/L at diagnosis to 0.88 (0.1-20.8) kU/L. The association between IgE and a negative challenge result was not statistically significant.Conclusion: IgE-mediated wheat allergy in adults is benign and represents a temporary break in gastrointestinal tolerance. Future studies may improve our knowledge of wheat allergens, routes of and factors leading to sensitization, and prognostic biomarkers


Introducción: La ingesta de trigo puede originar varias patologías como alergia alimentaria mediada por IgE y la anafilaxia inducida por ejercicio previa ingesta de trigo. Todas ellas originan un descenso en la calidad de vida y una importante morbilidad. La alergia a trigo es relativamente benigna en niños, sin embargo, su historia natural en adultos es aún desconocida. Objetivo: Evaluamos la historia natural de la hipersensibilidad al trigo de inicio en la edad adulta en pacientes atópicos confirmado mediante pruebas de exposición oral. Métodos: Se incluyeron 13 pacientes de una cohorte de pacientes adultos (edad media 40 años) con alergia a trigo mediada por IgE. Tras el diagnóstico los pacientes siguieron una dieta exenta de trigo y fueron seguidos durante 5 años para valorar su tolerancia tras la exposición al trigo. Al final del seguimiento se determinaron los valores de IgE específica a trigo y se realizó una segunda provocación oral con trigo. Resultados: 10 de los 13 pacientes tomaron parte en el estudio. La duración media del periodo de no ingesta de trigo fue de 4,2 años. 3 pacientes reintrodujeron por iniciativa propia la ingesta de trigo antes de la segunda evaluación, después de un periodo medio de 28 meses (RIQ 18-36 meses), presentando solo leves síntomas gastrointestinales. Al final del seguimiento, 9/10 pacientes toleraron la ingesta de trigo. 2 pacientes tenían historia de anafilaxia inducida por ejercicio. Se observó una disminución de los valores de IgE específica desde una mediana de 2,77 kU/l (RIQ 0,35-100 kU/L) en el momento del diagnóstico hasta 0,88 kU/l (RIQ 0,1-20,8 Ku/L) al final del seguimiento. No se observó correlación entre los valores de IgE específica y los resultados de la tolerancia final. Conclusión: La alergia a trigo mediada por IgE en adultos es una patología benigna y representa una interrupción temporal de la tolerancia gastrointestinal. Futuros estudios podrían mejorar nuestro conocimiento sobre los alérgenos del trigo, rutas y factores que llevan a la sensibilización, y biomarcadores de pronóstico


Asunto(s)
Humanos , Adulto , Hipersensibilidad al Trigo/tratamiento farmacológico , Hipersensibilidad a los Alimentos/tratamiento farmacológico , Intolerancia Alimentaria/epidemiología , Estudios de Casos y Controles , Placebos/uso terapéutico , Hipersensibilidad Inmediata/inmunología , Pronóstico
6.
Allergy ; 72(9): 1423-1429, 2017 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-28328103

RESUMEN

Food allergies are recognized as an increasing health concern. Proteins commonly identified as food allergens tend to have one of about 30 different biochemical activities. This leads to the assumption that food allergens must have specific structural features which causes their allergenicity. But these structural features are not completely understood. Uncovering the structural basis of allergenicity would allow improved diagnosis and therapy of allergies and would provide insights for safer food production. The availability of recombinant food allergens can accelerate their structural analysis and benefit specific studies in allergology. Plant chitinases are an example of food allergenic proteins for which structural analysis of allergenicity has only partially been reported. The recombinant maize chitinase, rChiA, was purified from Pichia pastoris extracellular medium by differential precipitation and cation exchange chromatography. Enzyme activity was evaluated by halo-assays and microcalorimetric procedures. rChiA modeling was performed by a two-step procedure, using the Swiss-Model server and Modeller software. Allergenicity of rChiA was verified by immunoblot assays with sera from allergic subjects. rChiA is active in the hydrolysis of glycol chitin and tetra-N-acetylchitotetraose and maintains its activity at high temperatures (70°C) and low pH (pH 3). The molecule is also reactive with IgE from sera of maize-allergic subjects. rChiA is a valuable molecule for further studies on structure-allergenicity relationships and as a tool for diagnosing allergies.


Asunto(s)
Antígenos de Plantas/inmunología , Quitinasas/inmunología , Hipersensibilidad a los Alimentos , Alérgenos , Quitinasas/química , Quitinasas/aislamiento & purificación , Humanos , Inmunoglobulina E , Pichia , Proteínas de Plantas/inmunología , Proteínas Recombinantes/química , Relación Estructura-Actividad , Zea mays
7.
J Investig Allergol Clin Immunol ; 27(3): 175-182, 2017.
Artículo en Inglés | MEDLINE | ID: mdl-27959286

RESUMEN

BACKGROUND AND OBJECTIVE: Skin prick testing (SPT) with commercial extracts is the first step in the diagnosis of shrimp allergy, although its clinical efficiency is unknown. Objective: To analyze the clinical usefulness of all commercial crustacean extracts available for SPT in Italy. METHODS: We performed a multicenter study of 157 shrimp-allergic patients who underwent SPT with 5 commercial crustacean extracts and with house dust mite (HDM) extract. Commercial extracts were analyzed using SDS-PAGE and compared with a freshly prepared in-house shrimp extract. IgE to Pen a 1/Pen m 1, Pen m 2, and Pen m 4 was determined, and immunoblot analysis was performed on a large number of sera. RESULTS: The skin reactions caused by commercial crustacean extracts were extremely heterogeneous, resulting in 32 clinical profiles, with marked differences in protein content and missing proteins at molecular weights corresponding to those of major shrimp allergens. Only strong Pen a 1/Pen m 1 reactors reacted to both HDM and all 5 commercial extracts in SPT. Most patients, including those who were tropomyosin-negative, reacted to HDM. Patients reacted to a large and variable array of proteins, and IgE reactivity was common at high molecular weights (>50 kDa). CONCLUSIONS: The in vivo diagnosis of shrimp allergy must continue to be based on SPT with fresh material. Shrimp-allergic patients frequently react to a number of ill-defined high-molecular-weight allergens, thus leaving currently available materials for component-resolved diagnosis largely insufficient. Mites and crustaceans probably share several allergens other than tropomyosin.


Asunto(s)
Alérgenos/inmunología , Proteínas de Artrópodos/inmunología , Inmunoglobulina E/inmunología , Hipersensibilidad a los Mariscos/diagnóstico , Adolescente , Adulto , Anciano , Animales , Niño , Preescolar , Electroforesis en Gel de Poliacrilamida , Femenino , Humanos , Immunoblotting , Italia , Masculino , Persona de Mediana Edad , Pyroglyphidae/inmunología , Hipersensibilidad a los Mariscos/inmunología , Pruebas Cutáneas , Tropomiosina/inmunología , Adulto Joven
8.
J. investig. allergol. clin. immunol ; 27(3): 175-182, 2017. tab, ilus
Artículo en Inglés | IBECS | ID: ibc-163167

RESUMEN

Background: Skin prick testing (SPT) with commercial extracts is the first step in the diagnosis of shrimp allergy, although its clinical efficiency is unknown. Objective: To analyze the clinical usefulness of all commercial crustacean extracts available for SPT in Italy. Methods: We performed a multicenter study of 157 shrimp-allergic patients who underwent SPT with 5 commercial crustacean extracts and with house dust mite (HDM) extract. Commercial extracts were analyzed using SDS-PAGE and compared with a freshly prepared in-house shrimp extract. IgE to Pen a 1/Pen m 1, Pen m 2, and Pen m 4 was determined, and immunoblot analysis was performed on a large number of sera. Results: The skin reactions caused by commercial crustacean extracts were extremely heterogeneous, resulting in 32 clinical profiles, with marked differences in protein content and missing proteins at molecular weights corresponding to those of major shrimp allergens. Only strong Pen a 1/Pen m 1 reactors reacted to both HDM and all 5 commercial extracts in SPT. Most patients, including those who were tropomyosin-negative, reacted to HDM. Patients reacted to a large and variable array of proteins, and IgE reactivity was common at high molecular weights (>50 kDa). Conclusions: The in vivo diagnosis of shrimp allergy must continue to be based on SPT with fresh material. Shrimp-allergic patients frequently react to a number of ill-defined high-molecular-weight allergens, thus leaving currently available materials for componentresolved diagnosis largely insufficient. Mites and crustaceans probably share several allergens other than tropomyosin (AU)


Introducción: Las pruebas cutáneas con extractos comerciales representan el primer paso en el diagnóstico de alergia a gamba, si bien, su eficacia clínica no está bien definida. Objetivos: El objetivo de este estudio fue analizar la utilidad clínica de todos los extractos comerciales disponibles en Italia frente a crustáceos en pruebas cutáneas. Métodos: En un estudio multicéntrico, se incluyeron 157 pacientes alérgicos a gamba a los que se realizaron pruebas cutáneas con cinco extractos comerciales de crustáceos y con ácaros del polvo doméstico. Los extractos comerciales fueron analizados mediante SDS-PAGE y comparados con un extracto de gamba preparado en fresco. Se determinó IgE frente a Pen a 1/Pen m 1; Pen m 2, y Pen m 4; y el análisis mediante inmunoblotting se realizó en un amplio número de sueros. Resultados: Los extractos de gamba comercializados dieron lugar a reacciones cutáneas muy poco homogéneas en 32 perfiles clínicos diferentes; así mismo, mostraron grandes diferencias en contenido proteico y, en algunos casos, a falta de proteína a pesos moleculares correspondientes a alérgenos mayoritarios de gamba. Únicamente los reactores más fuertes a Pen a1 /Pen m 1 reaccionaron tanto a ácaros del polvo de casa como a los cinco extractos comerciales en pruebas cutáneas. La mayoría de los pacientes, incluyendo los negativos a tropomiosina, reaccionaron a los ácaros del polvo. Los pacientes reaccionaron a un amplio y variable array de proteínas y se detectó con frecuencia reactividad de IgE en pesos moleculares altos (>50 kDa). Conclusiones: El diagnóstico in vivo de alergia a gamba todavía debe estar basado en pruebas cutáneas prick con producto fresco. Los pacientes alérgicos a gamba a menudo reaccionan a un número de alérgenos de peso molecular alto poco definido, lo que hace que las moléculas disponibles hoy en día para el diagnóstico por componentes sean muy insuficiente. Ácaros y crustáceos probablemente comparten varios alérgenos además de la tropiomiosina (AU)


Asunto(s)
Humanos , Alérgenos/análisis , Alérgenos/aislamiento & purificación , Hipersensibilidad a los Alimentos/diagnóstico , Pruebas Cutáneas/métodos , Mariscos/efectos adversos , Hipersensibilidad Inmediata/diagnóstico , Extractos Vegetales/análisis , Pruebas Cutáneas , Inmunoglobulina E/análisis , Peso Molecular , Técnicas In Vitro
9.
Artículo en Inglés | MEDLINE | ID: mdl-26182684

RESUMEN

UNLABELLED: Background: The role of allergens in the severity of tomato allergy symptoms has not yet been studied. OBJECTIVES: To evaluate the relationship between severe allergic reactions to peach and tomato and between tomato allergy symptoms and the pattern of IgE positivity for rPru p 1, rPru p 3, rPru p 4, rBetv 1, rBetv 2, rBetv4, rPhl p 1, and rPhl p 12 in order to identify the role of recombinant allergens in the severity of reactions to tomato. METHODS: We studied peach-allergic patients with clinical reactions to tomato by performing an open food challenge, skin prick test, and determination of serum specific IgE to tomato and to recombinant peach, birch, and grass allergens. Statistical analysis was carried out to evaluate the relationship between the severity of tomato symptoms and IgE positivity to the different allergens and to peach-induced symptoms. RESULTS: We found a significant association between severe reactions to tomato and severe reactions to peach (P = .01 7) and levels of IgE to rPru p3 (P = .029) and between mild tomato allergy symptoms and levels of IgE to rPru p1 (P = .047), anti-rBetv 1 (P = .0414), anti-rBetv 2 (P = .0457), and Phleum pratense (P = .0022). CONCLUSION: We observed a significant relationship between peach and symptoms of tomato allergy. IgE positivity for rPru p3 seems to be a surrogate biochemical marker for severe tomato allergy, whereas the presence of anti-rPru p 1 IgE may be an indicator of mild tomato allergy.


Asunto(s)
Antígenos de Plantas/inmunología , Hipersensibilidad a los Alimentos/diagnóstico , Proteínas de Plantas/inmunología , Prunus/efectos adversos , Solanum lycopersicum/efectos adversos , Adolescente , Adulto , Anciano , Biomarcadores/sangre , Femenino , Hipersensibilidad a los Alimentos/sangre , Hipersensibilidad a los Alimentos/inmunología , Frutas , Humanos , Inmunoglobulina E/sangre , Pruebas Intradérmicas , Italia , Solanum lycopersicum/inmunología , Masculino , Persona de Mediana Edad , Valor Predictivo de las Pruebas , Prunus/inmunología , Proteínas Recombinantes/inmunología , Pruebas Serológicas , Índice de Severidad de la Enfermedad , Adulto Joven
10.
Eur Ann Allergy Clin Immunol ; 47(2): 58-61, 2015 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-25781196

RESUMEN

INTRODUCTION: From the literature, patients with a history of anaphylaxis to hymenoptera venom and positive specific IgE have shown a correlation between elevated tryptase levels and two clinical situations: systemic mastocytosis and an increased risk of reactions to venom immunotherapy or hymenoptera sting. Other clinical scenarios could explain elevated tryptase levels. MATERIAL AND METHODS: A 67 year old male (P1) and a 77 year old male (P2) were evaluated for previous severe anaphylaxis to hymenoptera sting. They underwent standard diagnostic work-up for hymenoptera venom allergy. Having found elevated tryptase levels, these were followed by a bone marrow biopsy to rule out systemic mastocytosis. RESULTS: P1: specific IgE and skin tests were positive for Vespula species; tryptase 52.8 ng/ml; P2: specific IgE and skin tests were positive for Vespa cabro and tryptase 153 ng/ml. Bone marrow biopsy results were negative for mastocytosis. We carried out magnetic resonance imaging, in P1 to better characterize the severe osteoporosis and in P2 because during physical examination a pulsating mass had been identified in the mesogastrium, and an aneurysm of the abdominal aorta which required surgical intervention in both patients was detected. Eight months after surgery, tryptase levels had diminished significantly (P1: 11.6 ng/ml and P2: 14.5 ng/ml). DISCUSSION: The elevated tryptase levels were correlated to abdominal aneurysm in both patients. In fact, post-surgery tryptase levels dramatically decreased. These two cases demonstrate that high tryptase levels in subjects with a history of hymenoptera venom anaphylaxis can be associated to undiagnosed aneurysmatic disease.


Asunto(s)
Anafilaxia/inmunología , Aneurisma de la Aorta Abdominal/enzimología , Mordeduras y Picaduras de Insectos/inmunología , Triptasas/sangre , Venenos de Avispas/inmunología , Avispas/inmunología , Anciano , Anafilaxia/sangre , Anafilaxia/diagnóstico , Anafilaxia/enzimología , Anafilaxia/terapia , Animales , Aneurisma de la Aorta Abdominal/diagnóstico , Aneurisma de la Aorta Abdominal/cirugía , Biomarcadores/sangre , Humanos , Inmunoterapia/métodos , Masculino , Pruebas Cutáneas , Factores de Tiempo , Resultado del Tratamiento , Regulación hacia Arriba , Venenos de Avispas/uso terapéutico
13.
Int Arch Allergy Immunol ; 158(3): 276-80, 2012.
Artículo en Inglés | MEDLINE | ID: mdl-22398453

RESUMEN

BACKGROUND: Elevated baseline serum tryptase levels are associated with severe systemic reactions following hymenoptera stings or venom immunotherapy. Little is known about baseline tryptase levels in patients with respiratory allergy and whether a relationship exists with systemic reactions induced by injection specific immunotherapy (SIT) with airborne allergens. The objective of this study was to measure tryptase levels in subjects with respiratory allergy and analyze the results in the light of tolerance/intolerance to injection SIT. METHODS: Baseline serum tryptase levels were measured in 106 adults allergic to different airborne allergens and in 40 normal controls. Thirty-one patients underwent injection SIT, and 15 of these 31 experienced at least one SIT-induced systemic reaction. RESULTS: Patients and normal controls showed similar median tryptase levels (2.98 vs. 3.13 ng/ml, respectively), although these were elevated in 6 patients (6%) versus 0 of 40 controls (0%). Tryptase levels did not differ between those patients with or without a history of systemic reactions (median 3.7 vs. 5.91 ng/ml, not significant). Three of 4 patients showing elevated tryptase levels belonged to the SIT-tolerant group. Elevated tryptase levels were not associated with specific allergens nor with distance from the specific pollen season. A bone marrow aspirate performed in the only patient with a history of systemic reactions following injection SIT and tryptase >11.4 ng/ml showed a normal morphology and phenotype. CONCLUSIONS: Unlike patients with hymenoptera venom allergy, in patients with respiratory allergy, elevated serum tryptase levels do not represent a risk factor for adverse reactions to SIT.


Asunto(s)
Alérgenos/efectos adversos , Desensibilización Inmunológica/efectos adversos , Desensibilización Inmunológica/métodos , Polen/efectos adversos , Hipersensibilidad Respiratoria/terapia , Triptasas/sangre , Adolescente , Adulto , Anciano , Alérgenos/administración & dosificación , Femenino , Humanos , Masculino , Persona de Mediana Edad , Hipersensibilidad Respiratoria/inmunología , Factores de Riesgo , Triptasas/inmunología , Adulto Joven
14.
J Agric Food Chem ; 54(26): 9930-5, 2006 Dec 27.
Artículo en Inglés | MEDLINE | ID: mdl-17177523

RESUMEN

Oral allergy syndrome is an immediate food allergic event that affects lips, mouth, and pharynx, is often triggered by fruits and vegetables, and may be associated with pollinosis. Here, we report on the allergenic pattern of different varieties of cherry (Prunus avium) and results obtained by applying several technological processes to the selected varieties. Whole cherries were submitted to chemical peeling, thermal treatment, and syruping processes, and the relative protein extracts were analyzed by in vitro (sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting analysis) and in vivo tests (skin prick test). Electrophoretic analyses demonstrated that there was no marked difference among cherry cultivars. Chemical peeling successfully removed Pru av 3, a lipid transfer protein (LTP) responsible for oral allergy syndrome in patients without pollinosis, leading to the industrial production of cherry hypoallergenic derivatives. Furthermore, the syruping process removed almost all allergenic proteins to whom patients with pollinosis are responsive. In vivo tests confirmed electrophoretic results.


Asunto(s)
Manipulación de Alimentos/métodos , Hipersensibilidad a los Alimentos/inmunología , Frutas/inmunología , Prunus/inmunología , Adulto , Femenino , Hipersensibilidad a los Alimentos/prevención & control , Frutas/química , Calor , Humanos , Masculino , Proteínas de Plantas/análisis , Proteínas de Plantas/química , Proteínas de Plantas/inmunología , Prunus/química , Pruebas Cutáneas , Especificidad de la Especie
15.
G Ital Med Lav Ergon ; 26(2): 97-101, 2004.
Artículo en Italiano | MEDLINE | ID: mdl-15270436

RESUMEN

House dust mite and other indoor allergens play a prominent role in the pathogenesis of asthma and other allergic diseases. Several studies have shown a close relationship between sensitisation and/or onset of asthmatic symptoms and levels of indoor allergen exposure. Aim of the study was to investigate the concentration of specific markers of the indoor allergenic pollution, such as Der p 1, Der f 1, Mite Group 2, Fel d 1 and Bla g 2. Dust samples were taken using a standard method by means of a 1200 W vacuum cleaner connected with a dust-sampling device (MITEST). A standard A4 size area has been vacuumed four times during 2 min. The concentrations of Der p 1, Der f 1, Mite Group 2, Fel d 1 and Bla g 2 were determined in dust samples from 53 different sources (office chair and carpet) using a commercial kit (DUSTSCREEN). House dust mite allergens were not always detectable in the offices. Indoor allergen concentrations (Der p 1, Der f 1, Mite Group 2, Fel d 1) were significant higher in the work station (chair) than in the carpet (p < 0.0001). Der 1 exceeded the current threshold for sensitization in about 1/4 of the samples. Der f 1 was predominant over Der p 1 according to other studies. A good correlation between the results of Der p 1 and Der f 1 was observed both in carpet and work station. Cat allergen was ubiquitous and predominantly detected in the chairs because of the employees' clothes. No appreciable levels for Mite Gr 2 and Bla g 2 were detected. Such an exposure for 8 hours in every working day may be an important occupational risk for the development of sensitization/elicitation symptoms to house dust mite. To reduce mite allergen levels are necessary preventive measure by means of specific techniques and products as barriers for preventing the direct contact with allergens.


Asunto(s)
Contaminación del Aire Interior/análisis , Alérgenos/análisis , Antígenos Dermatofagoides/análisis , Lugar de Trabajo , Humanos
18.
G Ital Med Lav Ergon ; 23(1): 55-9, 2001.
Artículo en Italiano | MEDLINE | ID: mdl-11386189

RESUMEN

The availability of specific monoclonal and policlonal antibodies and the standardization of allergen extracts enables to quantify the exposure to airborne allergens in the domestic environment and at the workplace. In this article we report our experience coming from three studies based upon the measurement of airborne allergens in different environments. In a pharmaceutical factory we measured levels of laboratory animals allergens and evaluated the prevalence of sensitization to the same allergens among the workers. Airborne latex allergens and latex allergens content in latex gloves were measured in hospitals. In bakeries we evaluated the prevalence of sensitization to flour and measured flour allergens levels. The results of our studies give information useful to improve methods of prevention, diagnosis, and therapy of occupational allergic diseases.


Asunto(s)
Contaminación del Aire/análisis , Alérgenos/análisis , Humanos , Hipersensibilidad/epidemiología , Enfermedades Profesionales/epidemiología , Salud Laboral
19.
J Chromatogr B Biomed Sci Appl ; 756(1-2): 123-9, 2001 May 25.
Artículo en Inglés | MEDLINE | ID: mdl-11419703

RESUMEN

It has been recently demonstrated that the major allergen of apricot is a protein of molecular mass (Mr) 9000 belonging to the family of Lipid Transfer Protein. The aim of this study was the determination of the primary structure of apricot LTP by micro-sequencing and mass spectrometric analyses. Apricot LTP is a 91 amino acids protein like peach and almond LTPs with a sequence identity of 91% and 94%, respectively. Like for the peach LTP, out of the 25 amino acids forming the inner surface of the tunnel-like hydrophobic cavity in maize ns-LTP, 16 are identical and 7 similar in the apricot LTP, supporting the hypothesis of a similar function.


Asunto(s)
Proteínas Portadoras/química , Rosales/química , Secuencia de Aminoácidos , Animales , Antígenos de Plantas , Proteínas Portadoras/inmunología , Cromatografía Líquida de Alta Presión , Reacciones Cruzadas , Hipersensibilidad a los Alimentos , Ratones , Datos de Secuencia Molecular , Proteínas de Plantas , Rosales/inmunología , Homología de Secuencia de Aminoácido , Espectrometría de Masa por Ionización de Electrospray
20.
J Chromatogr B Biomed Sci Appl ; 756(1-2): 85-93, 2001 May 25.
Artículo en Inglés | MEDLINE | ID: mdl-11419730

RESUMEN

BACKGROUND: Allergic reactions induced by ingestion of foods containing sesame seeds are a well recognized cause of severe food-induced anaphylaxis. OBJECTIVE: This study aimed to identify and characterize the clinically most important major allergen of sesame seeds. METHODS: Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and IgE immunoblotting were performed on sera of 10 patients selected for severe and documented allergic reaction after eating food containing sesame. The major allergen was purified by gel filtration and characterized by isoelectric point (pI), glycosylation and amino acid sequencing. RESULTS: All the patients had positive IgE antibodies and skin prick tests (SPTs) to sesame. The major, clinically most important allergen was a protein with molecular mass of about 9000. It was not glycosylated, the amino acid sequence showed it was a 2S albumin with a pI of 7.3; the small and the large subunits, forming the whole protein, showed pI values of 6.5 and 6.0.


Asunto(s)
Albúminas/análisis , Alérgenos/análisis , Antígenos de Plantas/análisis , Magnoliopsida/embriología , Semillas/inmunología , Albuminas 2S de Plantas , Adulto , Western Blotting , Niño , Cromatografía en Gel , Cromatografía Líquida de Alta Presión , Electroforesis en Gel de Poliacrilamida , Femenino , Humanos , Inmunoglobulina E/análisis , Inmunoglobulina E/inmunología , Punto Isoeléctrico , Masculino , Peso Molecular , Pruebas Cutáneas
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