Crystal structure of the major peanut allergen Ara h 1

Cabanos, Cerrone; Urabe, Hiroyuki; Tandang‐Silvas, Mary Rose; Utsumi, Shigeru; Mikami, Bunzo; Maruyama, Nobuyuki

doi:10.1016/j.molimm.2011.08.004

Cited by 50 publications

(74 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The template and the modelled monomer can be divided into two similar modules (N- and C-terminal), each showing an extended loop domain. The models could be verified by the crystal based analysis of the Ara h 1 core fragment [39], [41]. Already identified IgE epitopes, were mapped on the models and it became evident that some of these epitopes were only surface exposed when the trimer formation was disrupted [42].…”

Section: Resultsmentioning

confidence: 89%

See 1 more Smart Citation

High-Throughput NMR Assessment of the Tertiary Structure of Food Allergens

et al. 2012

View full text Add to dashboard Cite

Background In vitro component-resolved diagnosis of food allergy requires purified allergens that have to meet high standards of quality. These include the authentication of their conformation, which is relevant for the recognition by specific IgE antibodies from allergic patients. Therefore, highly sensitive and reliable screening methods for the analysis of proteins/allergens are required to assess their structural integrity. In the present study one-dimensional 1H Nuclear Magnetic Resonance (1D 1H-NMR) analysis was adopted for the assessment of overall structural and dynamic properties and authentication of a set of relevant food allergens, including non-specific lipid transfer proteins from apple, peach and hazelnut, 7/8S seed storage globulins from hazelnut and peanut, 11S seed storage globulins from hazelnut and peanut, caseins from cows' and goats' milk and tropomyosin from shrimp.Methodology/Principal FindingsTwo sets of 1D 1H-NMR experiments, using 700 MHz and 600 MHz instruments at 298 K were carried out to determine the presence and the extent of tertiary structure. Structural similarity among members of the individual allergen families was also assessed and changes under thermal stress investigated. The nuclear magnetic resonance (NMR) results were compared with structural information available either from the literature, Protein Data Bank entries, or derived from molecular models.Conclusions/Significance1D 1H-NMR analysis of food allergens allowed their classification into molecules with rigid, extended and ordered tertiary structures, molecules without a rigid tertiary structure and molecules which displayed both features. Differences in thermal stability were also detected. In summary, 1D 1H-NMR gives insights into molecular fold of proteins and offers an independent method for assessing structural properties of proteins.

show abstract

Section: Resultsmentioning

confidence: 89%

“…Very recently, the structure from the Ara h 1 core region without the N-terminal extension and the C-terminal flexible region was determined [39]. Both isoforms could be modelled using the 7S globulin from adzuki bean [40] as a template (PDB accession 2ea7), with 48% of sequence identity (Fig.…”

Section: Resultsmentioning

confidence: 99%

High-Throughput NMR Assessment of the Tertiary Structure of Food Allergens

et al. 2012

View full text Add to dashboard Cite

show abstract

“…After Ara h 6 (Lehmann et al, 2006), Ara h 3 is the second peanut allergen that had its structure determined experimentally (Jin et al, 2009), and it is currently the only peanut allergen for which the structure was determined using protein originating from the natural source. The structure of core Ara h 1 fragment 1 was determined later and protein used for these studies corresponds to a truncated version of the allergen (Cabanos et al, 2011b;Chruszcz et al, 2011). As, both Ara h 1 and Ara h 3 are bicupins, their molecules may be described as having two modules related by a pseudo two-fold axis (Fig.…”

Section: Cupinsmentioning

confidence: 99%

Structural Biology of Peanut Allergens

Offermann¹,

Perdue²,

He³

et al. 2015

JCI

View full text Add to dashboard Cite

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.

show abstract

“…The 7S vicilin has no known function other than preserving nutrients for the development of young seedlings. The crystal structure of the peanut allergen Ara h 1 (the 7S vicilin from peanut; Cabanos et al, 2011;Chruszcz et al, 2011) has recently been determined and we recently reported the crystal structure of Korean pine vicilin, which revealed a copper center (Jin et al, 2013). Based on sequence alignment, the copper center is conserved in a number of tree species, but it does not exist in the vicilins of legumes.…”

Section: Structural Biology Communicationsmentioning

confidence: 99%

Expression, purification and crystallization of pecan (Carya illinoinensis) vicilin

Lee

Zhang

et al. 2014

Acta Cryst Sect F

View full text Add to dashboard Cite

Tree nuts are responsible for many cases of severe food allergies. The 7S seed storage protein vicilin has been identified as a food allergen in many kinds of tree nuts. The vicilin protein consists of an N-terminal low-complexity region with antimicrobial activity and a C-terminal domain that forms a trimeric structure that belongs to the cupin superfamily. In this study, vicilin from pecan (Carya illinoinensis) was isolated and was expressed in bacteria for the first time. The cupin structural core of the protein, residues 369-792, was purified by metalaffinity and gel-filtration chromatography to high purity. Vicilin crystals were obtained and the best crystal diffracted to 2.65 Å resolution in space group P2 1 2 1 2 1 .

show abstract

Crystal structure of the major peanut allergen Ara h 1

Cited by 50 publications

References 45 publications

High-Throughput NMR Assessment of the Tertiary Structure of Food Allergens

High-Throughput NMR Assessment of the Tertiary Structure of Food Allergens

Structural Biology of Peanut Allergens

Expression, purification and crystallization of pecan (Carya illinoinensis) vicilin

Contact Info

Product

Resources

About