Crystal structure determination of Scylla paramamosain arginine kinase, an allergen that may cause cross-reactivity among invertebrates

Yang, Yang; Li, Guangyu; Huang, Yang; Hu, Mengjun; Cao, Min‐Jie; Su, Wen‐Jin; Jin, Tengchuan

doi:10.1016/j.foodchem.2018.08.003

Cited by 18 publications

(21 citation statements)

References 37 publications

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“…The NE2 atom of this residue formed a hydrogen bond with the backbone carbonyl oxygen of A135, as previously reported for the DmAK structure (Figure 5a) [25]. This hydrogen bond is commonly found in many AK structures, such as A131-H224 in Apostichopus japonicus [28] and P135-H227 in Scylla paramamosain [29], P135-H227 in Polybetes pythagoricus [30], P135-H227 in Penaeus vannamei [31] and P135-H227 in Limulus Polyphemus [14], in both the basal and transition states. In the case of the DmAK H227A structure, the hydrogen bond destruction between A135 and H227, resulted in the replacement of one water molecule (WAT684) at the imidazole group of histidine position (Figure 5b).…”

Section: Structural Features Of Dmak H227asupporting

confidence: 78%

Crystal Structure of H227A Mutant of Arginine Kinase in Daphnia magna Suggests the Importance of Its Stability

et al. 2022

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Arginine kinase (AK) plays a crucial role in the survival of Daphnia magna, a water flea and a common planktonic invertebrate sensitive to water pollution, owing to the production of bioenergy. AK from D. magna (DmAK) has four highly conserved histidine residues, namely, H90, H227, H284, and H315 in the amino acid sequence. In contrast to DmAK WT (wild type), the enzyme activity of the H227A mutant decreases by 18%. To identify the structure-function relationship of this H227A mutant enzyme, the crystal 3D X-ray structure has been determined and an unfolding assay using anilino-1-naphthalenesulfonic acid (ANS) fluorescence has been undertaken. The results revealed that when compared to the DmAK WT, the hydrogen bonding between H227 and A135 was broken in the H227A crystal structure. This suggests that H227 residue, closed to the arginine binding site, plays an important role in maintaining the structural stability and maximizing the enzyme activity through hydrogen bonding with the backbone oxygen of A135.

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Section: Structural Features Of Dmak H227asupporting

confidence: 78%

Crystal Structure of H227A Mutant of Arginine Kinase in Daphnia magna Suggests the Importance of Its Stability

et al. 2022

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“…The allergens AK [28, 34,69], SCBP[22, 44,70] and hemocyanin [39,70] are proteins which may be also involved in this cross-reactivity syndrome. [34].Finally, enolase could be an important allergen that justifies cross-reactivity in infants, according to Kamath et al [70].…”

Section: Involvement Of Other Allergensmentioning

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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“…Tropomyosin is a 34 to 38 kDa heatstable protein that belongs to a highly conserved family of actin filament binding proteins, which plays a functional role in contractile activities in muscle cells (Ruethers et al, 2018). Arginine kinase is a 40 to 42 kDa heat-labile protein that plays an important role in regenerating adenosine triphosphate (ATP) during bursts of cellular activity (Yang et al, 2019). Tropomyosin and arginine kinase from the prawn and crab have been isolated and the fulllength sequences were obtained.…”

Section: Resultsmentioning

confidence: 99%

Isolation and Cloning of Tropomyosin and Arginine Kinase from Tiger Prawn Penaeus monodon and Blue Swimming Crab Portunus trituberculatus

Yadzir¹,

Leecyous²,

Zamri³

2020

JSML

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Shellfish is an important source of food and plays a significant role in human nutrition and health. However, shellfish allergy is a long-lasting disorder which mostly persists throughout life and is often associated with severe reactions [1]. Among the various consumed shellfish, prawns and crabs are the most widely consumed and can lead to the most severe reactions. At present, allergies to shellfish are diagnosed similarly to other food allergies. The diagnosis relies upon careful evaluation of history, the presence of appropriate clinical signs and confirmation with in vivo or in vitro tests to demonstrate the presence of allergen-specific immunoglobulin E (IgE) [2]. However, both in vivo or in vitro diagnostic approaches are mainly based on the use of crude allergen extracts. Crude allergen extracts are obtained from biological sources and consist of mixture of allergenic components with high amounts of undesirable products that can interfere with diagnosis. In many cases, only few of the several proteins found in crude allergen extracts act as the essential allergens in the majority of patients that are allergic to the substance. The most important ones are called major allergens. Problems associated with using crude allergen extracts for allergy diagnosis may be overcome with recombinant allergens. Recombinant allergens with high purity can be produced by using controlled production procedures that yield defined molecules with known molecular, immunologic and biological characteristics [1]. Tiger prawn Penaeus monodon and blue swimming crab Portunus trituberculatus, are among the widely consumed shellfish in Malaysia. Our earlier study involving 131 atopic patients in Allergy Clinic, Kuala Lumpur Hospital demonstrated that patients in Malaysia suffering from allergic responses to shellfish including tiger prawn Penaeus monodon and blue swimming crab Portunus trituberculatus. Amongst the shellfish extracts tested, prawn elicited the highest frequency of positive reactivity in 39% of the patients. Further, crab was the second most common shellfish to elicit a positive reaction in 24% of the patients [3]. Our first phase study has successfully identified tropomyosin and arginine kinase as the major allergens in both species of shellfish. However, more information about the individual allergenic species-specific components is needed. Therefore, we continued our study to isolate and clone the tropomyosin and arginine kinase from these two species of shellfish, tiger prawn Penaeus monodon and blue swimming crab Portunus trituberculatus. Tropomyosin and arginine kinase were isolated from the total RNA (Ribonucleic Acid) obtained from both prawn and crab muscles followed by RT-PCR (Reverse Transcriptase-Polymerase Chain Reaction). The RT-PCR products were then cloned into the cloning vector, pJET 1.2 and transformed into Escherichia coli host. Transformants were screened for positive clones by PCR (Polymerase Chain Reaction) colony and sequenced. The 855 bp tropomyosins have been isolated and sequenced from both prawn and crab. Arginine kinases isolated and sequenced from prawn and crab were 1071 bp and 1074 bp, respectively (Figure 1). The GenBank BLAST search for the sequences showed high homology to the targeted proteins as shown in Table 1. Tropomyosin is a 34 to 38 kDa heat-stable protein that belongs to a highly conserved family of actin filament binding proteins, which plays a functional role in contractile activities in muscle cells [4]. Arginine kinase is a 40 to 42 kDa heat-labile protein that plays an important role in regenerating adenosine triphosphate (ATP) during bursts of cellular activity [5]. Tropomyosin and arginine kinase from the prawn and crab have been isolated and the full-length sequences were obtained. Current ongoing study focuses on sub-cloning and full-length expression of tropomyosin and arginine kinase in order to produce respective recombinant proteins, and subsequently investigate their physicochemical and allergenic characteristics.

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Crystal structure determination of Scylla paramamosain arginine kinase, an allergen that may cause cross-reactivity among invertebrates

Cited by 18 publications

References 37 publications

Crystal Structure of H227A Mutant of Arginine Kinase in Daphnia magna Suggests the Importance of Its Stability

Crystal Structure of H227A Mutant of Arginine Kinase in Daphnia magna Suggests the Importance of Its Stability

Shellfish Allergy: Unmet Needs in Diagnosis and Treatment

Isolation and Cloning of Tropomyosin and Arginine Kinase from Tiger Prawn Penaeus monodon and Blue Swimming Crab Portunus trituberculatus

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