Allergen stabilities and compatibilities in mixtures of high-protease fungal and insect extracts

Grier, Thomas J.; LeFevre, Dawn M.; Duncan, Elizabeth A.; Esch, Robert E.; Coyne, Terrance C.

doi:10.1016/j.anai.2012.04.012

Cited by 28 publications

(20 citation statements)

References 16 publications

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“…A confirmation of IgE reactivity to allergens is performed either in vivo by skin tests using allergen extracts or by provocation tests, which are the gold standard for allergy diagnosis, or in vitro by serological analysis. However, the variability in allergen composition and content of commercial allergen extracts can affect their in vivo allergenic activity [2, 3]. Food challenges, specifically double-blind placebo-controlled food challenges, represent the most reliable way to diagnose food allergies, but it cannot always be performed if patients are very sensitive to a certain food [4].…”

Section: Introduction: When Allergen Extracts Are Not Sufficient For mentioning

confidence: 99%

Interfaces Between Allergen Structure and Diagnosis: Know Your Epitopes

Pomés

Chruszcz

Gustchina

et al. 2015

Curr Allergy Asthma Rep

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Allergy diagnosis is based on the patient’s clinical history and can be strengthened by tests that confirm the origin of sensitization. In the past 25 years, these tests have evolved from the exclusive in vivo or in vitro use of allergen extracts, to complementary molecular-based diagnostics that rely on in vitro measurements of IgE reactivity to individual allergens. For this to occur, an increase in our understanding of the molecular structure of allergens, largely due to the development of technologies such as molecular cloning and expression of recombinant allergens, X-ray crystallography, or nuclear magnetic resonance (NMR), has been essential. New in vitro microarray or multiplex systems are now available to measure IgE against a selected panel of purified natural or recombinant allergens. The determination of the three-dimensional structure of allergens has facilitated detailed molecular studies, including the analysis of antigenic determinants for diagnostic purposes.

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Section: Introduction: When Allergen Extracts Are Not Sufficient For mentioning

confidence: 99%

Interfaces Between Allergen Structure and Diagnosis: Know Your Epitopes

Pomés

Chruszcz

Gustchina

et al. 2015

Curr Allergy Asthma Rep

View full text Add to dashboard Cite

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“…Proteases cause degradation of proteins through cleavage of peptide bonds and can ultimately compromise the stability of the antibody-binding activities of proteins in extracts used for immunotherapy. Some allergenic extracts (e.g., pollen, mite, animal) are classified as low-protease or protease-susceptible extracts, whereas most fungal and insect extracts are classified as high-protease extracts [6]. To date, allergen mixology research has focused primarily on the effects of combining low-protease with other low-protease allergenic extracts or lowprotease with high-protease allergenic extracts to determine the effects of mixing on shelf life and stability of allergens [6].…”

Section: Degradation Of Allergens In Mixturesmentioning

confidence: 99%

“…In a study [6] published in the Annals of Allergy, Asthma and Immunology, the official publication of the American College of Allergy, Asthma & Immunology, researchers asked the question: What if 2 highly proteolytic allergenic extracts were combined in the same extract mixture? The researchers thought it was particularly important to answer this question because, while immunotherapy practice parameters state that these extracts can be combined, data to support this practice had not been published prior to this paper.…”

Section: Insights Into High-protease Extractsmentioning

confidence: 99%

Considerations for Combining High-Protease Extracts in Immunotherapy Vaccines

Lilley¹,

Rekkerth²,

Teske³

2014

OJN

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Current practice parameters state that extracts rich in proteases, such as fungal and insect extracts, can be combined during preparation of allergy immunotherapy vaccines. However, until recently, this guideline has not been the subject of investigation. Scientists now have data that shed light on high-protease allergenic extract mixtures used in allergy immunotherapy. A study published in Annals of Allergy, Asthma & Immunology in 2012 reports on the compatibility of combining fungal and insect extracts and emphasizes the importance of understanding how protease activities and total glycerin levels in allergy extracts can affect the stability of allergy immunotherapy vaccine mixtures. This research provides a critical assessment of the mixing compatibilitiesof several well-characterized high-protease extracts and may influence future immunotherapy practice parameters and immunotherapy extract preparation guidelines.

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“…El diagnóstico de alergias para este u otro tipo de hongos es difícil de realizar, ya que a diferencia de los otros alergenos, no es claro cuál es la fuente original de sensibilización: si los micelios, las esporas o los metabolitos secundarios; además, se conoce que las proteínas de estos hongos pueden variar de acuerdo con las condiciones geográficas y topográficas, lo que aumenta la dificultad de estandarizar técnicas para la obtención de extractos con actividad antigénica, efectivos para el diagnóstico y el tratamiento específico mediante inmunoterapia (Bisht, Arora, Singh, Gaur, & Sridhara, 2004;Grier, LeFevre, Duncan, Esch, & Coyne, 2012;Nosanchuk & Taborda, 2013;Shah & Grammer, 2012).…”

Section: Introductionunclassified

Caracterización parcial de proteínas de una cepa de Cladosporium sp

Rengifo¹,

Cerón²,

Caicedo³

2013

Ingenium

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El objetivo de esta investigación fue la caracterización parcial de proteínas de la fracción acuosa y micelio del cultivo de una cepa de Cladosporium sp, aislada de la casa de un paciente reactivo a las conidias de este hongo, ubicada en la zona nor-oriental de la ciudad de Cali. Se determinó la concentración de proteínas con el método de Lowry, el patrón electroforético en gel de poliacrilamida con dodecil sulfato de sodio (SDS) y la actividad de las enzimas proteasas y fosfatasa ácida y alcalina. En el micelio se encontró un contenido proteico de 5.88 ug/mL, bandas de electrofóresis entre 11 y 74 kDa, actividad proteolítica en un rango de pH entre 6.0 y 8.0, actividad de fosfatasa negativa en medio ácido y alcalino. Las pruebas realizadas con el extracto acuoso fueron negativas. Investigaciones realizadas en otras partes del mundo han demostrado que existe variación en la cantidad y actividad de las proteínas de estos hongos, lo que hace difícil la estandarización de técnicas diagnósticas e inmunoterapia, resultados que están de acuerdo con los obtenidos. Este es el primer estudio realizado en la ciudad de Cali; se espera continuar con otras investigaciones que permitan caracterizar los componentes alergénicos de especies de este hongo, el más prevalente en el ambiente de esta ciudad.

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Allergen stabilities and compatibilities in mixtures of high-protease fungal and insect extracts

Cited by 28 publications

References 16 publications

Interfaces Between Allergen Structure and Diagnosis: Know Your Epitopes

Interfaces Between Allergen Structure and Diagnosis: Know Your Epitopes

Considerations for Combining High-Protease Extracts in Immunotherapy Vaccines

Caracterización parcial de proteínas de una cepa de Cladosporium sp

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