Paramyosin from the Disc Abalone <i>Haliotis Discus Discus</i>

Suzuki, Midori; Shimizu, Keiko; Kobayashi, Yukihiro; Ishizaki, Shoichiro; Shiomi, Kazuro

doi:10.1111/jfbc.12072

Cited by 11 publications

(7 citation statements)

References 33 publications

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“…venosa PM had a high degree of sequence identity with PM from invertebrates, which also indicated that PM may cross-react with the PM of other molluscs. This supports the conclusion of the previous study where PM is a cross-reactive allergen in some molluscs . The 2D and 3D PM structures in the R.…”

Section: Discussionsupporting

confidence: 92%

“…This supports the conclusion of the previous study where PM is a cross-reactive allergen in some molluscs. 42 The 2D and 3D PM structures in the R. venosa were analyzed in order to enhance the knowledge of the structure function relationship and the conservation status of PM. In this work, 3D structure of PM was modeled based on the Robetta server to build model for domains with sequence homology to proteins of known structure using comparative modeling.…”

Section: ■ Discussionmentioning

confidence: 99%

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Purification, Characterization, and Three-Dimensional Structure Prediction of Paramyosin, a Novel Allergen of Rapana venosa

Gao

Lin

et al. 2020

J. Agric. Food Chem.

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Paramyosin (PM) is an important structural protein in molluscan muscles. However, as an important allergen, there is a little information on PM in the molluscs. In this study, a 99 kDa molecular weight allergen protein was purified from Rapana venosa and confirmed as PM by mass spectrometry. The results of immunoglobulin E (IgE)-binding activity and physicochemical characterization showed that R. venosa PM could react with a specific IgE of the sera from sea snail-allergic patients, and the IgE-binding activity could be reduced by thermal treatment. The full-length cDNA of R. venosa PM was cloned, which encodes 859 amino acid residues, and it has a higher homology among molluscan species. According to the circular dichroism results, Fourier transform infrared, and 2D and 3D structure analysis, both PM and tropomyosin are conserved proteins, which are mainly composed of the α-helix structure. These results are significant for better understanding the anaphylactic reactions in sea snail-allergic patients and allergy diagnosis.

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Section: Discussionsupporting

confidence: 92%

Section: ■ Discussionmentioning

confidence: 99%

Purification, Characterization, and Three-Dimensional Structure Prediction of Paramyosin, a Novel Allergen of Rapana venosa

Gao

Lin

et al. 2020

J. Agric. Food Chem.

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“…One of the very prominent IgE-reactive bands is paramyosin, observed at 100 kDa. Paramyosin is a major structural component of the invertebrate muscle thick filament and was identified as an additional major allergen in abalone ( Haliotis discus discus) [ 7 , 30 ] and recently in sea snail ( Rapana venosa ) [ 31 ]. The discovery of allergenic paramyosin in mollusc species was not surprising since this protein has been confirmed as a major allergen in other invertebrates such as house dust-mite [ 32 ] and anisakis [ 33 ].…”

Section: Discussionmentioning

confidence: 99%

Effects of Extraction Buffer on the Solubility and Immunoreactivity of the Pacific Oyster Allergens

Nugraha

Ruethers

Johnston

et al. 2021

Foods

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Despite recent technological advances, novel allergenic protein discovery is limited by their low abundance, often due to specific physical characteristics restricting their recovery during the extraction process from various allergen sources. In this study, eight different extraction buffers were compared for their ability to recover proteins from Pacific oyster (Crassostrea gigas). The protein composition was investigated using high resolution mass spectrometry. The antibody IgE-reactivity of each extract was determined using a pool of serum from five shellfish-allergic patients. Most of the investigated buffers showed good capacity to extract proteins from the Pacific oyster. In general, a higher concentration of proteins was recovered using high salt buffers or high pH buffers, subsequently revealing more IgE-reactive bands on immunoblotting. In contrast, low pH buffers resulted in a poor protein recovery and reduced IgE-reactivity. Discovery of additional IgE-reactive proteins in high salt buffers or high pH buffers was associated with an increase in allergen abundance in the extracts. In conclusion, increasing the ionic strength and pH of the buffer improves the solubility of allergenic proteins during the extraction process for oyster tissue. This strategy could also be applied for other difficult-to-extract allergen sources, thereby yielding an improved allergen panel for increased diagnostic efficiency.

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“…Other potential allergens identified in shellfish are paramyosins (identified in many mollusk species and Anisakis simplex ), triose phosphate isomerases such as Cra a 8 , myosin heavy chain , α‐ and β‐actin , smooth endoplasmic reticulum Ca ++ ATPase (SERCA) , glyceraldehyde phosphate dehydrogenase (GDPH), titin , and ubiquitin ; however, a deeper characterization is still required.…”

Section: Allergensmentioning

confidence: 99%

Shellfish allergens: tropomyosin and beyond

Faber

Pascal

Kharbouchi

et al. 2017

Allergy

132

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IgE-mediated shellfish allergy constitutes an important cause of food-related adverse reactions. Shellfish are classified into mollusks and crustaceans, the latter belonging to the class of arthropoda. Among crustaceans, shrimps are the most predominant cause of allergic reactions and thus more extensively studied. Several major and minor allergens have been identified and cloned. Among them, invertebrate tropomyosin, arginine kinase, myosin light chain, sarcoplasmic calciumbinding protein, and hemocyanin are the most relevant. This review summarizes our current knowledge about these allergens.IgE-mediated shellfish allergy constitutes an important and increasing health issue in both children and adults (1, 2). During the last two decades, significant progress in biochemistry and molecular biology enabled the characterization, cloning, and recombinant production of various shellfish allergen components and epitope-emulating peptides that might become available for quantification of specific IgE (sIgE) antibodies, namely molecular diagnosis. This review intends to summarize our current knowledge about shellfish allergens and their cross-reactivity as this might be the key to optimize diagnosis (3, 4). Table 1 summarizes the most relevant shellfish allergens that have currently been characterized. Tropomyosin is considered to be the major allergen in shellfish allergy. Actually, already in the early 1980s Hoffman et al. (5) identified a heat-stable IgE-binding allergen in shrimps that was later identified as tropomyosin in brown shrimp (Penaeus aztecus) reacting with 28/ 34 (82%) of shrimp-sensitive individuals (6). Moreover, tropomyosin has been identified as a panallergen of many invertebrate species including other crustaceans (lobster, crab), mollusks (mussels, oysters, scallops, octopus, squids, snails, abalones, whelk, clams, razor shell), cockroaches, and mites (7-18). Tropomyosins are present in both muscle and nonmuscle cells. In striated muscle, they mediate the interaction of troponin-actin complex to regulate contraction. Note that tropomyosins from crustaceans share a high homology (up to 98%), whereas the amino acid sequence identity between (3,(19)(20)(21)(22)(23)(24)(25). Children were once reported to recognize a greater epitope repertoire than adults and thus suggested that shrimp sensitization could decrease over age (22). However, more recent studies with challenged patients could not reproduce this observation with the same epitope mapping (3, 24). About one decade ago, a recombinant tropomyosin from Penaeus aztecus, rPen a 1, became commercially available for molecular diagnostic testing, with improved results as a diagnostic tool in comparison with the whole-shrimp extract (26,27). In addition to tropomyosin, several other allergenic components have been identified in shellfish. In 2003, Yu et al. identified a novel allergen in Penaeus monodon (black tiger shrimp) (28), designated as Pen m 2, with arginine kinase activity. Similar to tropomyosin, arginine kinase is highly abundant i...

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Paramyosin from the Disc Abalone Haliotis Discus Discus

Cited by 11 publications

References 33 publications

Purification, Characterization, and Three-Dimensional Structure Prediction of Paramyosin, a Novel Allergen of Rapana venosa

Purification, Characterization, and Three-Dimensional Structure Prediction of Paramyosin, a Novel Allergen of Rapana venosa

Effects of Extraction Buffer on the Solubility and Immunoreactivity of the Pacific Oyster Allergens

Shellfish allergens: tropomyosin and beyond

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