Identification and comparison of allergenicity of native and recombinant fish major allergen parvalbumins from Japanese flounder (<i>Paralichthys olivaceus</i>)

Sun, Lirui; Xu, Lili; Huang, Yuhao; Lin, Hong; Ahmed, Ifty; Liu, Zhenxing

doi:10.1039/c9fo01402k

Cited by 15 publications

(18 citation statements)

References 30 publications

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“…SCP is similar to parvalbumin, which is a major allergen of fish . Moreover, SCP belongs to the EF-hand calcium-binding protein family, which contain helix–loop–helix motifs that bind calcium ions (Ca 2+ ) .…”

Section: Discussionmentioning

confidence: 99%

“…12,15,27 SCP is similar to parvalbumin, which is a major allergen of fish. 31 Moreover, SCP belongs to the EF-hand calcium-binding protein family, which contain helix−loop−helix motifs that bind calcium ions (Ca 2+ ). 4 It has been demonstrated that the SCP of black-tiger-shrimp centered on conformational type IgE epitopes, which may partially be dependent on calcium binding.…”

Section: ■ Discussionmentioning

confidence: 99%

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Identification and Cross-reactivity Analysis of Sarcoplasmic-Calcium-Binding Protein: A Novel Allergen in Crassostrea angulata

Han

Huan

et al. 2020

J. Agric. Food Chem.

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Oysters are an important shellfish group known to cause food allergy; however, knowledge of their sensitization components and cross-reactivity is limited. This study aimed to identify a novel allergen in Crassostrea angulata and investigate its cross-reactivity. To this end, a 20 kDa protein was purified from oyster and confirmed to be a sarcoplasmic-calcium-binding protein (SCP) by LC-MS/MS. A 537 bp open reading frame was obtained from oyster SCP total RNA, which encoded 179 amino acids, and was expressed in Escherichia coli. According to the circular dichroism results, digestion assay, and inhibition ELISA, the recombinant SCP (rSCP) exhibited similar physicochemical properties and IgG-binding activity to native SCP. rSCP displayed stronger IgE-binding activity by immunological method. Moreover, a different intensity of cross-reactivity and sequence homology were demonstrated between shellfish species. Collectively, these findings provide novel insight into shellfish allergens, which can be used to aid in the in vitro diagnosis of oyster-sensitized patients.

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Section: Discussionmentioning

confidence: 99%

Section: ■ Discussionmentioning

confidence: 99%

Identification and Cross-reactivity Analysis of Sarcoplasmic-Calcium-Binding Protein: A Novel Allergen in Crassostrea angulata

Han

Huan

et al. 2020

J. Agric. Food Chem.

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“…iELISA was conducted according to the method described by Sun et al, 29 with slight modification. The inhibitor (Scy p 4 or IAA−Scy p 4) was diluted to different concentrations and then pre-incubated with the rabbit anti-Scy p 4 polyclonal antibody (dilution of 1:10 5 ) or the serum pool of crab-sensitized individuals.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Linear Epitopes Play an Important Role in the Immunoglobulin G (IgG)/Immunoglobulin E (IgE)-Binding Capacity of Scy p 4

Chen

Liu

et al. 2021

J. Agric. Food Chem.

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Sarcoplasmic calcium-binding protein is a stable allergen in Scylla paramamosain and named Scy p 4. To explore the importance of linear epitopes in the immunoglobulin G (IgG)/immunoglobulin E (IgE)-binding capacity of Scy p 4, chemical denaturants were used to destroy the structure. Scy p 4 was reduced with dithiothreitol and subsequently alkylated with iodoacetamide (IAA). Furthermore, the structural analysis indicated that IAA−Scy p 4 was an unstructured protein. The inhibition enzyme-linked immunosorbent assay showed that IAA−Scy p 4 could inhibit the binding of Scy p 4 to sensitize serum, with inhibition rates reached 55%. Moreover, the linear mimotopes of Scy p 4 were predicted in silico. Three linear epitopes were verified by serological tests and named L-Scy p 4-1 (AA 76−91 ), L-Scy p 4-2 (AA 111−125 ), and L-Scy p 4-3 (AA 137−146 ). Overall, these data provide an understanding of the relationship between the structure and allergenicity about Scy p 4, and the identified linear epitopes can be used for diagnosis and food processing of shellfish allergy.

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“…After running SDS-PAGE gels, protein bands were stained using Coomassie Brilliant Blue R-250 (Sigma, St Louis, MO, USA) to verify the target protein bands in the elution. Afterwards, western blotting was performed following the previously described procedure [ 25 ] to confirm the presence of recombinant Plychap001. Plychap001 bands from the unstained gels were transferred onto PVDF membranes, after which the primary rabbit anti-His IgG antibody (1:5000 dilution) and the secondary goat anti-rabbit antibody (1:8000 dilution) were successively incubated with the membranes.…”

Section: Methodsmentioning

confidence: 99%

A Single Catalytic Endolysin Domain Plychap001: Characterization and Application to Control Vibrio parahaemolyticus and Its Biofilm Directly

Wang

Cong

et al. 2022

Foods

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Endolysins are enzymes used by bacteriophages to cleave the host cell wall in the final stages of the lytic cycle. As such, they are considered promising antibacterial agents for controlling and combating multidrug-resistant (MDR) bacteria. However, the application of endolysins targeting Gram-negative bacteria is greatly hindered by the outer membrane on these bacteria. Lysqdvp001, an endolysin with modular structure, has been reported as one of the most efficient endolysins against the Gram-negative bacterium Vibrio parahaemolyticus. In this study, Plychap001, the truncated recombinant catalytic domain of Lysqdvp001, was demonstrated to exhibit a direct and efficient bactericidal activity against broad spectrum of V. parahaemolyticus strains. Plychap001 was shown to be highly stable and retain high bactericidal activity at high temperatures, over a wide pH range, and at high NaCl concentrations. Plychap001 also exhibited a synergistic lytic effect with EDTA. Additionally, Plychap001 was found to efficiently degrade and eliminate V. parahaemolyticus biofilms on polystyrene surfaces. Our study establishes Plychap001 as a promising method for controlling V. parahaemolyticus in the food industry.

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Identification and comparison of allergenicity of native and recombinant fish major allergen parvalbumins from Japanese flounder (Paralichthys olivaceus)

Abstract: Compared with native parvalbumin, recombinant β-parvalbumin based on the optimized DNA sequence can be used in fish allergen confirmation.

Cited by 15 publications

References 30 publications

Identification and Cross-reactivity Analysis of Sarcoplasmic-Calcium-Binding Protein: A Novel Allergen in Crassostrea angulata

Identification and Cross-reactivity Analysis of Sarcoplasmic-Calcium-Binding Protein: A Novel Allergen in Crassostrea angulata

Linear Epitopes Play an Important Role in the Immunoglobulin G (IgG)/Immunoglobulin E (IgE)-Binding Capacity of Scy p 4

A Single Catalytic Endolysin Domain Plychap001: Characterization and Application to Control Vibrio parahaemolyticus and Its Biofilm Directly

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