Expression, purification, cross-reactivity and homology modeling of peanut profilin

Cabanos, Cerrone; Tandang‐Silvas, Mary Rose; Odijk, Van; Brostedt, Peter; Utsumi, Shigeru; Maruyama, Nobuyuki

doi:10.1016/j.pep.2010.03.005

Cited by 36 publications

(34 citation statements)

References 36 publications

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“…Several comprehensive reviews 94,109,275,95,110,277−285 and textbooks 95,110,286 exist on this topic and its applications 286−300 in the drug discovery process.…”

Section: Drug Design Approaches In the Absence Of Knowledge About Thementioning

confidence: 99%

Integrated Approach to Structure-Based Enzymatic Drug Design: Molecular Modeling, Spectroscopy, and Experimental Bioactivity

et al. 2013

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“…Several comprehensive reviews 94,109,275,95,110,277−285 and textbooks 95,110,286 exist on this topic and its applications 286−300 in the drug discovery process.…”

Section: Drug Design Approaches In the Absence Of Knowledge About Thementioning

confidence: 99%

Integrated Approach to Structure-Based Enzymatic Drug Design: Molecular Modeling, Spectroscopy, and Experimental Bioactivity

et al. 2013

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“…In Western blot experiments rBet v 2 is not able to inhibit patients' IgE reactivity to Ara h 5 but the vice versa experiment is successful. These findings were supported by homology screening and epitope analysis where Ara h 5 possesses a specific, non-crossreactive epitope [64] . Mittag et al [65] investigated the function of Ara h 5 and, especially, Ara h 8.…”

Section: Ara H 5 and Ara Hmentioning

confidence: 67%

Peanut Allergens

Becker

Jappe

2014

Chemical Immunology and Allergy

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The earliest known evidence of peanut farming dates back 7,600 years. With a prevalence of roughly 1%, peanut allergy is a diagnostic and treatment challenge, but is also a very good model for studying all aspects of food allergy, including its molecular basis and pathomechanisms. Therefore, the very starting point for elucidating all these aspects is the identification of peanut allergens with subsequent clearing of their structure and their preparation as pure recombinant and/or natural allergens. This is the basis for in vitro diagnostic tests as well as the development of immunotherapeutic drugs. With regard to class I food allergy, peanut allergy affects by far the largest group of patients. In peanuts, 12 allergens have been identified and their molecular characteristics are described herein. Ara h 1, Ara h 3.01 and Ara h 3.02 (the former Ara h 4) belong to the cupin superfamily. The conglutins Ara h 2, Ara h 6 and Ara h 7, and the non-specific lipid transfer protein Ara h 9 belong to the prolamin superfamily. Ara h 5 (profilin) and Ara h 8 (Bet v 1-homologous protein) cause class II food allergies and are associated with inhalation allergy to pollen via the sequential and/or conformational similarity of molecules. Two peanut oleosins are listed as Ara h 10 and Ara h 11 and two defensins as Ara h 12 and Ara h 13 by the WHO/IUIS Allergen Nomenclature Subcommittee. The effect of the above-specified allergens has to be considered in the context of their matrix, which is influenced by processing factors and the individual's immune system.

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“…This is also true for several isoallergens which structures were not studied. In some cases, due to the high sequence identity/similarity between these molecules it is possible to calculate reliable 3D models and use them, for example, for epitope mapping (Barre et al, 2005a;Barre et al, 2005b;Cabanos et al, 2010;Power et al, 2013). However, one has to remember that even when a relatively good template for homology modeling is present some regions of a protein, like loops and disordered fragments cannot be modeled accurately.…”

Section: Discussionmentioning

confidence: 99%

Structural Biology of Peanut Allergens

Offermann¹,

Perdue²,

He³

et al. 2015

JCI

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Peanuts are a cause of one of the most common food allergies. Allergy to peanuts not only affects a significant fraction of the population, but it is relatively often associated with strong reactions in sensitized individuals. Peanut and tree nut allergies, which start in childhood are often persistent and continue through life, as opposed to other food allergies that resolve with age. Therefore, peanut allergens are one of the most intensively studied food allergens. In this review we focus on the structural studies of peanut allergens.

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Expression, purification, cross-reactivity and homology modeling of peanut profilin

Cited by 36 publications

References 36 publications

Integrated Approach to Structure-Based Enzymatic Drug Design: Molecular Modeling, Spectroscopy, and Experimental Bioactivity

Integrated Approach to Structure-Based Enzymatic Drug Design: Molecular Modeling, Spectroscopy, and Experimental Bioactivity

Peanut Allergens

Structural Biology of Peanut Allergens

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