Purification, Characterization, and Analysis of the Allergenic Properties of Myosin Light Chain in <i>Procambarus clarkii</i>

Zhang, Yongxia; Chen, Heng-Li; Maleki, Soheila J.; Cao, Min‐Jie; Zhang, Ling‐Jing; Su, Wen‐Jin

doi:10.1021/acs.jafc.5b01318

Cited by 51 publications

(54 citation statements)

References 29 publications

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“…Was identified in American white shrimp, Litopenaeusvannamei( Lit v 3) [40]. It was later described in other shrimp species, lobster [41], crabs [42] and cockroaches [20].…”

Section: Myosin Light Chainmentioning

confidence: 99%

Shellfish Allergy: Unmet Needs in Diagnosis and Treatment

Gelis¹,

Rueda²,

Valero³

et al. 2020

J Investig Allergol Clin Immunol

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“…Was identified in American white shrimp, Litopenaeusvannamei( Lit v 3) [40]. It was later described in other shrimp species, lobster [41], crabs [42] and cockroaches [20].…”

Section: Myosin Light Chainmentioning

confidence: 99%

Shellfish Allergy: Unmet Needs in Diagnosis and Treatment

Gelis¹,

Rueda²,

Valero³

et al. 2020

J Investig Allergol Clin Immunol

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“…Like tropomyosin and arginine kinase, shrimp MLC displays a significant amino acid sequence homology with homologues in other arthropods such as Bla g 8 from Blattella germanica (German cockroach) . MLC molecules are highly resistant to heat, acid–alkali, and digestion, and retain weakly IgE‐binding activity when their secondary structure is altered .…”

Section: Allergensmentioning

confidence: 99%

Shellfish allergens: tropomyosin and beyond

Faber

Pascal

Kharbouchi

et al. 2017

Allergy

133

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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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“… 47 Myosin light chain (MLC) is a 20 kDa allergen displaying IgE reactivity in both raw and cooked shrimp extracts despite the alteration in its secondary structure under high temperature or acid treatment. 50 , 51 Sarcoplasmic calcium-binding protein (SCP) is an allergen recognized by serum IgE in 38% of patients with shrimp allergy. 52 Similar to other allergenic components, SCP is highly conserved among crustaceans (alpha chain: 90%–94% identity, beta chain: 80% identity).…”

Section: Shellfish Allergens and Cross-reactivitymentioning

confidence: 99%

Diagnosis of fish and shellfish allergies

Tong¹,

Yuen²,

Wai³

et al. 2018

JAA

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Seafood allergy is a hypersensitive disorder with increasing prevalence worldwide. Effective and accurate diagnostic workup for seafood allergy is essential for clinicians and patients. Parvalbumin and tropomyosin are the most common fish and shellfish allergens, respectively. The diagnosis of seafood allergies is complicated by cross-reactivity among fish allergens and between shellfish allergens and other arthropods. Current clinical diagnosis of seafood allergy is a complex algorithm that includes clinical assessment, skin prick test, specific IgE measurement, and oral food challenges. Emerging diagnostic strategies, such as component-resolved diagnosis (CRD), which uses single allergenic components for assessment of epitope specific IgE, can provide critical information in predicting individualized sensitization patterns and risk of severe allergic reactions. Further understanding of the molecular identities and characteristics of seafood allergens can advance the development of CRD and lead to more precise diagnosis and improved clinical management of seafood allergies.

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Purification, Characterization, and Analysis of the Allergenic Properties of Myosin Light Chain in Procambarus clarkii

Cited by 51 publications

References 29 publications

Shellfish Allergy: Unmet Needs in Diagnosis and Treatment

Shellfish Allergy: Unmet Needs in Diagnosis and Treatment

Shellfish allergens: tropomyosin and beyond

Diagnosis of fish and shellfish allergies

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