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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 |
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creator | Faisal, Md Dargahi, Narges Vasiljevic, Todor Donkor, Osaana N. |
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 |
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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 < 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><identifier>ISSN: 0950-5423</identifier><identifier>EISSN: 1365-2621</identifier><identifier>DOI: 10.1111/ijfs.14331</identifier><language>eng</language><publisher>Oxford: Wiley Subscription Services, Inc</publisher><subject>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</subject><ispartof>International journal of food science & technology, 2020-02, Vol.55 (2), p.795-804</ispartof><rights>2019 The Authors. International Journal of Food Science & Technology published by John Wiley & Sons Ltd on behalf of Institute of Food, Science and Technology (IFSTTF).</rights><rights>International Journal of Food Science and Technology © 2020 Institute of Food Science and Technology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3741-a41e365129d73ab6c404ec1993bbda5814bc4a0e09c5829064a66f34026f224f3</citedby><cites>FETCH-LOGICAL-c3741-a41e365129d73ab6c404ec1993bbda5814bc4a0e09c5829064a66f34026f224f3</cites><orcidid>0000-0001-9565-9024</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Faisal, Md</creatorcontrib><creatorcontrib>Dargahi, Narges</creatorcontrib><creatorcontrib>Vasiljevic, Todor</creatorcontrib><creatorcontrib>Donkor, Osaana N.</creatorcontrib><title>Immunomodulatory properties of selectively processed prawn protein fractions assessed using human peripheral blood mononuclear cells</title><title>International journal of food science & technology</title><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 < 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 ; Dargahi, Narges ; Vasiljevic, Todor ; Donkor, Osaana N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3741-a41e365129d73ab6c404ec1993bbda5814bc4a0e09c5829064a66f34026f224f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Acetic acid</topic><topic>Antigenicity</topic><topic>Antigens</topic><topic>Arginine</topic><topic>Arginine kinase</topic><topic>Cytokines</topic><topic>Enzyme-linked immunosorbent assay</topic><topic>Glucan</topic><topic>High-performance liquid chromatography</topic><topic>IgG antibody</topic><topic>Immunogenicity</topic><topic>Immunoglobulin E</topic><topic>Immunoglobulin G</topic><topic>Immunoglobulins</topic><topic>Immunomodulation</topic><topic>Inflammation</topic><topic>interleukin cytokine</topic><topic>Kinases</topic><topic>LC/MS/MS</topic><topic>Leukocytes (mononuclear)</topic><topic>Liquid chromatography</topic><topic>Methyltransferase</topic><topic>Muscles</topic><topic>Ovaries</topic><topic>PBMCs</topic><topic>Peripheral blood mononuclear cells</topic><topic>Phosphopyruvate hydratase</topic><topic>prawn allergy</topic><topic>Proteins</topic><topic>Tropomyosin</topic><topic>Tumors</topic><topic>Vitellogenin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Faisal, Md</creatorcontrib><creatorcontrib>Dargahi, Narges</creatorcontrib><creatorcontrib>Vasiljevic, Todor</creatorcontrib><creatorcontrib>Donkor, Osaana N.</creatorcontrib><collection>Open Access: Wiley-Blackwell Open Access Journals</collection><collection>Wiley Online Library Journals</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><jtitle>International journal of food science & technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Faisal, Md</au><au>Dargahi, Narges</au><au>Vasiljevic, Todor</au><au>Donkor, Osaana N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immunomodulatory properties of selectively processed prawn protein fractions assessed using human peripheral blood mononuclear cells</atitle><jtitle>International journal of food science & technology</jtitle><date>2020-02</date><risdate>2020</risdate><volume>55</volume><issue>2</issue><spage>795</spage><epage>804</epage><pages>795-804</pages><issn>0950-5423</issn><eissn>1365-2621</eissn><abstract>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 < 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).</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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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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