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Immunomodulatory properties of selectively processed prawn protein fractions assessed using human peripheral blood mononuclear cells

Summary Prawn muscles were treated with acetic acid and high‐pressure processing (600 MPa) separately to analyse their antigenicity and immunogenicity. The protein fractions were separated and isolated using preparative HPLC, and their antigenicity was analysed using Immunoglobulin G (IgG) ELISA kit...

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Published in:International journal of food science & technology 2020-02, Vol.55 (2), p.795-804
Main Authors: Faisal, Md, Dargahi, Narges, Vasiljevic, Todor, Donkor, Osaana N.
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description Summary Prawn muscles were treated with acetic acid and high‐pressure processing (600 MPa) separately to analyse their antigenicity and immunogenicity. The protein fractions were separated and isolated using preparative HPLC, and their antigenicity was analysed using Immunoglobulin G (IgG) ELISA kit. Out of thirty‐nine protein fractions, only four (A10, A11, B10 and C9) were detected with antigenic potentials. The immunogenicity of these protein fractions was analysed using human PBMCs, and supernatants were collected at multiple times from 0 to 144 h. The treated fractions (B10 and C9) analysed using Immunoglobulin E (IgE) ELISA kit showed significantly (P 
doi_str_mv 10.1111/ijfs.14331
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The protein fractions were separated and isolated using preparative HPLC, and their antigenicity was analysed using Immunoglobulin G (IgG) ELISA kit. Out of thirty‐nine protein fractions, only four (A10, A11, B10 and C9) were detected with antigenic potentials. The immunogenicity of these protein fractions was analysed using human PBMCs, and supernatants were collected at multiple times from 0 to 144 h. The treated fractions (B10 and C9) analysed using Immunoglobulin E (IgE) ELISA kit showed significantly (P &lt; 0.05) lower pro‐ and anti‐inflammatory cytokine production compared with control (A10). The allergenic fractions were characterised using an LC/MS/MS, which identified nine proteins. Among these, six proteins (tropomyosin, arginine kinase, haemocyanin, enolase, vitellogenin and 14‐3‐3 zeta) have been established as allergenic in prawn muscle and ovaries. Other three proteins (beta‐1,3‐glucan‐binding protein, translationally controlled tumour protein and farnesoic acid O‐methyltransferase short isoform protein) identified in this study need further investigation for their immunogenic properties. 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The protein fractions were separated and isolated using preparative HPLC, and their antigenicity was analysed using Immunoglobulin G (IgG) ELISA kit. Out of thirty‐nine protein fractions, only four (A10, A11, B10 and C9) were detected with antigenic potentials. The immunogenicity of these protein fractions was analysed using human PBMCs, and supernatants were collected at multiple times from 0 to 144 h. The treated fractions (B10 and C9) analysed using Immunoglobulin E (IgE) ELISA kit showed significantly (P &lt; 0.05) lower pro‐ and anti‐inflammatory cytokine production compared with control (A10). The allergenic fractions were characterised using an LC/MS/MS, which identified nine proteins. Among these, six proteins (tropomyosin, arginine kinase, haemocyanin, enolase, vitellogenin and 14‐3‐3 zeta) have been established as allergenic in prawn muscle and ovaries. Other three proteins (beta‐1,3‐glucan‐binding protein, translationally controlled tumour protein and farnesoic acid O‐methyltransferase short isoform protein) identified in this study need further investigation for their immunogenic properties. Immunomodulatory properties of selectively processed prawn protein fractions assessed using human peripheral blood mononuclear cells (PBMCs).</description><subject>Acetic acid</subject><subject>Antigenicity</subject><subject>Antigens</subject><subject>Arginine</subject><subject>Arginine kinase</subject><subject>Cytokines</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>Glucan</subject><subject>High-performance liquid chromatography</subject><subject>IgG antibody</subject><subject>Immunogenicity</subject><subject>Immunoglobulin E</subject><subject>Immunoglobulin G</subject><subject>Immunoglobulins</subject><subject>Immunomodulation</subject><subject>Inflammation</subject><subject>interleukin cytokine</subject><subject>Kinases</subject><subject>LC/MS/MS</subject><subject>Leukocytes (mononuclear)</subject><subject>Liquid chromatography</subject><subject>Methyltransferase</subject><subject>Muscles</subject><subject>Ovaries</subject><subject>PBMCs</subject><subject>Peripheral blood mononuclear cells</subject><subject>Phosphopyruvate hydratase</subject><subject>prawn allergy</subject><subject>Proteins</subject><subject>Tropomyosin</subject><subject>Tumors</subject><subject>Vitellogenin</subject><issn>0950-5423</issn><issn>1365-2621</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><recordid>eNp9kD1PwzAQhi0EEqWw8AsssSGl-CtpM6KKQhESAzBbjnOhrhw72AlVd344bsPMLXene-7rReiakhlNdme2TZxRwTk9QRPKizxjBaOnaELKnGS5YPwcXcS4JYQwPhcT9LNu28H51teDVb0Pe9wF30HoDUTsGxzBgu7NN9hjRUOMUKdI7dwh78E43ASVEO8iVql6BIZo3CfeDK1KGATTbSAoiyvrfY1b77wbtAUVsAZr4yU6a5SNcPXnp-hj9fC-fMpeXh_Xy_uXTKdbaaYEhfQSZWU956oqtCACNC1LXlW1yhdUVFooAqTU-YKVpBCqKBouCCsaxkTDp-hmnJsu_xog9nLrh-DSSsm4yBktF0mhKbodKR18jAEa2QXTqrCXlMiDyvKgsjyqnGA6wjtjYf8PKdfPq7ex5xc7s4Lp</recordid><startdate>202002</startdate><enddate>202002</enddate><creator>Faisal, Md</creator><creator>Dargahi, Narges</creator><creator>Vasiljevic, Todor</creator><creator>Donkor, Osaana N.</creator><general>Wiley Subscription Services, Inc</general><scope>24P</scope><scope>WIN</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>SOI</scope><orcidid>https://orcid.org/0000-0001-9565-9024</orcidid></search><sort><creationdate>202002</creationdate><title>Immunomodulatory properties of selectively processed prawn protein fractions assessed using human peripheral blood mononuclear cells</title><author>Faisal, Md ; 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Other three proteins (beta‐1,3‐glucan‐binding protein, translationally controlled tumour protein and farnesoic acid O‐methyltransferase short isoform protein) identified in this study need further investigation for their immunogenic properties. Immunomodulatory properties of selectively processed prawn protein fractions assessed using human peripheral blood mononuclear cells (PBMCs).</abstract><cop>Oxford</cop><pub>Wiley Subscription Services, Inc</pub><doi>10.1111/ijfs.14331</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-9565-9024</orcidid><oa>free_for_read</oa></addata></record>
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source Wiley-Blackwell Read & Publish Collection; Oxford Academic Journals (Open Access)
subjects Acetic acid
Antigenicity
Antigens
Arginine
Arginine kinase
Cytokines
Enzyme-linked immunosorbent assay
Glucan
High-performance liquid chromatography
IgG antibody
Immunogenicity
Immunoglobulin E
Immunoglobulin G
Immunoglobulins
Immunomodulation
Inflammation
interleukin cytokine
Kinases
LC/MS/MS
Leukocytes (mononuclear)
Liquid chromatography
Methyltransferase
Muscles
Ovaries
PBMCs
Peripheral blood mononuclear cells
Phosphopyruvate hydratase
prawn allergy
Proteins
Tropomyosin
Tumors
Vitellogenin
title Immunomodulatory properties of selectively processed prawn protein fractions assessed using human peripheral blood mononuclear cells
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