Complete amino acid sequence of the sarcoplasmic calcium‐binding protein (SCP‐I) from crayfish (Astacus leptodactilus)

Jáuregui-Adell, J.; Wnuk, W; Cox, Jos A.

doi:10.1016/0014-5793(89)80131-0

Cited by 19 publications

(5 citation statements)

References 22 publications

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“…When searched by the protein databases on the basis of the determined amino acid sequences of the 2 peptides, the 20-kDa allergen was found to be a member of the SCP family. The SCPs from 3 species of crustaceans, oriental shrimp Penaeus orientalis [26, 27], narrow-fingered crayfish Astacus leptodactylus [28] and red swamp crayfish Procambarus clarkii [29], have been elucidated for their amino acid sequences, as shown in figure 3. Peptides 1 and 2 obviously correspond to the segments 120–139 and 56–72 of the crustacean SCPs, respectively.…”

Section: Resultsmentioning

confidence: 99%

Sarcoplasmic Calcium-Binding Protein: Identification as a New Allergen of the Black Tiger Shrimp Penaeus monodon

Shiomi

Sato²,

Hamamoto³

et al. 2008

Int Arch Allergy Immunol

131

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Background: Tropomyosin and arginine kinase have been identified as crustacean allergens. During purification of arginine kinase from black tiger shrimp Penaeus monodon, we found a new allergen of 20-kDa. Methods: A 20-kDa allergen was purified from the abdominal muscle of black tiger shrimp by salting-out, anion-exchange HPLC and reverse-phase HPLC. Following digestion of the 20-kDa allergen with lysyl endopeptidase, peptide fragments were isolated by reverse-phase HPLC, and 2 of them were sequenced. The 20-kDa allergen, together with tropomyosin and arginine kinase purified from black tiger shrimp, was evaluated for IgE reactivity by ELISA. Five species of crustaceans (kuruma shrimp, American lobster, pink shrimp, king crab and snow crab) were surveyed for the 20-kDa allergen by immunoblotting. Results: The 20-kDa allergen was purified from black tiger shrimp and identified as a sarcoplasmic calcium-binding protein (SCP) based on the determined amino acid sequences of 2 enzymatic fragments. Of 16 sera from crustacean-allergic patients, 8 and 13 reacted to SCP and tropomyosin, respectively; the reactivity to arginine kinase was weakly recognized with 10 sera. In immunoblotting, an IgE-reactive 20-kDa protein was also detected in kuruma shrimp, American lobster and pink shrimp but not in 2 species of crab. Preadsorption of the sera with black tiger shrimp SCP abolished the IgE reactivity of the 20-kDa protein, suggesting the 20-kDa protein to be an SCP. Conclusions: SCP is a new crustacean allergen, and distribution of IgE-reactive SCP is probably limited to shrimp and crayfish.

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Section: Resultsmentioning

confidence: 99%

Sarcoplasmic Calcium-Binding Protein: Identification as a New Allergen of the Black Tiger Shrimp Penaeus monodon

Shiomi

Sato²,

Hamamoto³

et al. 2008

Int Arch Allergy Immunol

131

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“…For each PCR product, several clones (at least three clones) obtained by subcloning were found to have the same nucleotide sequence. In both species of shrimps, therefore, isoforms of the cloned SCP (correctly the SCP subunit) are absent or trace, although three different isoforms of SCP, two homodimers (αα and ββ) and one heterodimer (αβ) have been reported for oriental shrimp and narrow‐clawed crayfish …”

Section: Resultsmentioning

confidence: 99%

“…In both species of shrimps, therefore, isoforms of the cloned SCP (correctly the SCP subunit) are absent or trace, although three different isoforms of SCP, two homodimers (αα and ββ) and one heterodimer (αβ) have been reported for oriental shrimp 22,23 and narrow-clawed crayfish. 24 The determined nucleotide sequences of the full-length cDNAs coding for the black tiger shrimp SCP (1002 bp) and kuruma shrimp SCP (1007 bp) have been deposited in the DDBJ/EMBL/GenBank databases under the accession numbers AB703461 and AB703462,…”

Section: Cloning Of the Cdnas Encoding Shrimp Scpsmentioning

confidence: 99%

Molecular cloning and functional expression of allergenic sarcoplasmic calcium‐binding proteins from Penaeus shrimps

et al. 2012

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“…ADV17343.1), 33 Pontastacus lepto- dactylus (Genbank accession no. p05946.1), 34 S. paramamosain (Genbank accession no. AFJ80778.1), 7 Aedes aegypti (Genbank accession no.…”

Section: Ige Epitope Mapping Analysis Of Scy Pmentioning

confidence: 99%

Crystal Structure Analysis of Sarcoplasmic-Calcium-Binding Protein: An Allergen in Scylla paramamosain

Chen

Jin

et al. 2023

J. Agric. Food Chem.

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The structure of allergenic proteins provides important information about the binding of allergens to antibodies. In this study, the crystal structure of Scy p 4 with a resolution of 1.60 Å was obtained by X-ray diffraction. Epitope mapping of Scy p 4 revealed that linear epitopes are located on the surface of Scy p 4. Also, conformational epitopes are mostly located in the structural conservative region. Further structural comparison, surface electrostatic potential, and hydrogen bond force analysis showed that mutation of Asp 70 and Asp 18/20/70 would lead to calcium-binding capacity being lost and destruction of allergenicity. Furthermore, a comparative analysis of structure showed that sarcoplasmic-calcium-binding protein (SCP) had high sequence, secondary, and spatial structural identity in crustaceans, which may be an important factor leading to cross-reactivity among crustaceans. The structure of Scy p 4 provides a template for epitope evaluation and localization of SCPs, which will help to reveal cross-reactivity among species.

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Complete amino acid sequence of the sarcoplasmic calcium‐binding protein (SCP‐I) from crayfish (Astacus leptodactilus)

Cited by 19 publications

References 22 publications

Sarcoplasmic Calcium-Binding Protein: Identification as a New Allergen of the Black Tiger Shrimp <i>Penaeus monodon</i>

Sarcoplasmic Calcium-Binding Protein: Identification as a New Allergen of the Black Tiger Shrimp <i>Penaeus monodon</i>

Molecular cloning and functional expression of allergenic sarcoplasmic calcium‐binding proteins from Penaeus shrimps

Crystal Structure Analysis of Sarcoplasmic-Calcium-Binding Protein: An Allergen in Scylla paramamosain

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