Analysis of the linear epitope for Fc-binding on the mouse IgG Fc receptor (moFcγRI) by synthetic peptide
To identify the linear epitope for Fc-binding to the mouse immunoglobulin G (IgG) Fc receptor (moFcγRI), peptides derived from the membrane-distal extracellular domain (EC2) of moFcγRI, corresponding to the homologous region of human FcγRI (huFcγRI) and huFcγRII, were synthesized. Using a dot-blot a...
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| Veröffentlicht in: | Genetics and molecular research 2014-01, Vol.13 (2), p.4647-4653 |
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| creator | Wang, F Y Guo, J Q Zhang, G P |
| description | To identify the linear epitope for Fc-binding to the mouse immunoglobulin G (IgG) Fc receptor (moFcγRI), peptides derived from the membrane-distal extracellular domain (EC2) of moFcγRI, corresponding to the homologous region of human FcγRI (huFcγRI) and huFcγRII, were synthesized. Using a dot-blot assay, six peptides were tested. The results showed that the moRI3 peptide (CVFYRNGKSFQFS) could combine with mouse IgG efficiently. A competitive enzyme-linked immunosorbent assay (ELISA) showed that the IC50 value of the moRI3 peptide was 38.03 mM. The moRI3 peptide could inhibit the combination of mouse IgG to the transfected COS 7 cells significantly with an IC50 value of 72.68 mM. The IgG-binding region of moFcγRI was also localized in the C'-E loop of the EC2 domain as predicted according to huFcγRI and huFcγRII. We predicted that the minimum effective IgG-binding region of moFcγRI may be the peptide 153SFQFSS158. The linear epitope for immunoglobulin-binding to mouse FcγR is also described. Thus, we generated a peptide that targets a fundamental aspect of ligand recognition by this receptor class. |
| doi_str_mv | 10.4238/2014.June.18.7 |
| format | Article |
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Using a dot-blot assay, six peptides were tested. The results showed that the moRI3 peptide (CVFYRNGKSFQFS) could combine with mouse IgG efficiently. A competitive enzyme-linked immunosorbent assay (ELISA) showed that the IC50 value of the moRI3 peptide was 38.03 mM. The moRI3 peptide could inhibit the combination of mouse IgG to the transfected COS 7 cells significantly with an IC50 value of 72.68 mM. The IgG-binding region of moFcγRI was also localized in the C'-E loop of the EC2 domain as predicted according to huFcγRI and huFcγRII. We predicted that the minimum effective IgG-binding region of moFcγRI may be the peptide 153SFQFSS158. The linear epitope for immunoglobulin-binding to mouse FcγR is also described. Thus, we generated a peptide that targets a fundamental aspect of ligand recognition by this receptor class.</description><identifier>ISSN: 1676-5680</identifier><identifier>EISSN: 1676-5680</identifier><identifier>DOI: 10.4238/2014.June.18.7</identifier><identifier>PMID: 25036514</identifier><language>eng</language><publisher>Brazil</publisher><subject>Animals ; Cercopithecus aethiops ; COS Cells ; Epitope Mapping ; Epitopes - chemistry ; Epitopes - immunology ; Epitopes - metabolism ; Humans ; Immunoglobulin Fc Fragments - chemistry ; Immunoglobulin Fc Fragments - immunology ; Immunoglobulin Fc Fragments - metabolism ; Immunoglobulin G - metabolism ; Mice ; Peptide Fragments - chemical synthesis ; Peptide Fragments - immunology ; Peptide Fragments - metabolism ; Receptors, IgG - metabolism</subject><ispartof>Genetics and molecular research, 2014-01, Vol.13 (2), p.4647-4653</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-3bce3e0cfd20ec0dfd8472c60e9ba2edfb554bb7bcf1d3d0a1c1bca3ce4fae843</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25036514$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, F Y</creatorcontrib><creatorcontrib>Guo, J Q</creatorcontrib><creatorcontrib>Zhang, G P</creatorcontrib><title>Analysis of the linear epitope for Fc-binding on the mouse IgG Fc receptor (moFcγRI) by synthetic peptide</title><title>Genetics and molecular research</title><addtitle>Genet Mol Res</addtitle><description>To identify the linear epitope for Fc-binding to the mouse immunoglobulin G (IgG) Fc receptor (moFcγRI), peptides derived from the membrane-distal extracellular domain (EC2) of moFcγRI, corresponding to the homologous region of human FcγRI (huFcγRI) and huFcγRII, were synthesized. Using a dot-blot assay, six peptides were tested. The results showed that the moRI3 peptide (CVFYRNGKSFQFS) could combine with mouse IgG efficiently. A competitive enzyme-linked immunosorbent assay (ELISA) showed that the IC50 value of the moRI3 peptide was 38.03 mM. The moRI3 peptide could inhibit the combination of mouse IgG to the transfected COS 7 cells significantly with an IC50 value of 72.68 mM. The IgG-binding region of moFcγRI was also localized in the C'-E loop of the EC2 domain as predicted according to huFcγRI and huFcγRII. We predicted that the minimum effective IgG-binding region of moFcγRI may be the peptide 153SFQFSS158. The linear epitope for immunoglobulin-binding to mouse FcγR is also described. Thus, we generated a peptide that targets a fundamental aspect of ligand recognition by this receptor class.</description><subject>Animals</subject><subject>Cercopithecus aethiops</subject><subject>COS Cells</subject><subject>Epitope Mapping</subject><subject>Epitopes - chemistry</subject><subject>Epitopes - immunology</subject><subject>Epitopes - metabolism</subject><subject>Humans</subject><subject>Immunoglobulin Fc Fragments - chemistry</subject><subject>Immunoglobulin Fc Fragments - immunology</subject><subject>Immunoglobulin Fc Fragments - metabolism</subject><subject>Immunoglobulin G - metabolism</subject><subject>Mice</subject><subject>Peptide Fragments - chemical synthesis</subject><subject>Peptide Fragments - immunology</subject><subject>Peptide Fragments - metabolism</subject><subject>Receptors, IgG - metabolism</subject><issn>1676-5680</issn><issn>1676-5680</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctKA0EQRRtRTIxuXUov42LGfs0jyxBMjAQE0XXTj-rYYV5OTxb5Lv_Db3JiorhzVQX31KW4F6FrSmLBeH7HCBXx47aCmOZxdoKGNM3SKElzcvpnH6CLEDaEsETk5BwNWEJ4mlAxRJtppYpd8AHXDndvgAtfgWoxNL6rG8CubvHcRNpX1ldrXFffUFlvA-DletFruAUDTddz47Kem8-P5-Ut1jscdlWPdt7gppe9hUt05lQR4Oo4R-h1fv8ye4hWT4vlbLqKjOCii7g2wIEYZxkBQ6yzuciYSQlMtGJgnU4SoXWmjaOWW6KoodoobkA4BbngIzQ--DZt_b6F0MnSBwNFoSro_5Y0TUUf24Sw_9FEZIngjNIejQ-oaesQWnCyaX2p2p2kRO6rkPsq5L4KSXOZ9Qc3R--tLsH-4j_Z8y-Yo4bG</recordid><startdate>20140101</startdate><enddate>20140101</enddate><creator>Wang, F Y</creator><creator>Guo, J Q</creator><creator>Zhang, G P</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7T5</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20140101</creationdate><title>Analysis of the linear epitope for Fc-binding on the mouse IgG Fc receptor (moFcγRI) by synthetic peptide</title><author>Wang, F Y ; Guo, J Q ; Zhang, G P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-3bce3e0cfd20ec0dfd8472c60e9ba2edfb554bb7bcf1d3d0a1c1bca3ce4fae843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Animals</topic><topic>Cercopithecus aethiops</topic><topic>COS Cells</topic><topic>Epitope Mapping</topic><topic>Epitopes - chemistry</topic><topic>Epitopes - immunology</topic><topic>Epitopes - metabolism</topic><topic>Humans</topic><topic>Immunoglobulin Fc Fragments - chemistry</topic><topic>Immunoglobulin Fc Fragments - immunology</topic><topic>Immunoglobulin Fc Fragments - metabolism</topic><topic>Immunoglobulin G - metabolism</topic><topic>Mice</topic><topic>Peptide Fragments - chemical synthesis</topic><topic>Peptide Fragments - immunology</topic><topic>Peptide Fragments - metabolism</topic><topic>Receptors, IgG - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, F Y</creatorcontrib><creatorcontrib>Guo, J Q</creatorcontrib><creatorcontrib>Zhang, G P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Immunology Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Genetics and molecular research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, F Y</au><au>Guo, J Q</au><au>Zhang, G P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the linear epitope for Fc-binding on the mouse IgG Fc receptor (moFcγRI) by synthetic peptide</atitle><jtitle>Genetics and molecular research</jtitle><addtitle>Genet Mol Res</addtitle><date>2014-01-01</date><risdate>2014</risdate><volume>13</volume><issue>2</issue><spage>4647</spage><epage>4653</epage><pages>4647-4653</pages><issn>1676-5680</issn><eissn>1676-5680</eissn><abstract>To identify the linear epitope for Fc-binding to the mouse immunoglobulin G (IgG) Fc receptor (moFcγRI), peptides derived from the membrane-distal extracellular domain (EC2) of moFcγRI, corresponding to the homologous region of human FcγRI (huFcγRI) and huFcγRII, were synthesized. Using a dot-blot assay, six peptides were tested. The results showed that the moRI3 peptide (CVFYRNGKSFQFS) could combine with mouse IgG efficiently. A competitive enzyme-linked immunosorbent assay (ELISA) showed that the IC50 value of the moRI3 peptide was 38.03 mM. The moRI3 peptide could inhibit the combination of mouse IgG to the transfected COS 7 cells significantly with an IC50 value of 72.68 mM. The IgG-binding region of moFcγRI was also localized in the C'-E loop of the EC2 domain as predicted according to huFcγRI and huFcγRII. We predicted that the minimum effective IgG-binding region of moFcγRI may be the peptide 153SFQFSS158. The linear epitope for immunoglobulin-binding to mouse FcγR is also described. Thus, we generated a peptide that targets a fundamental aspect of ligand recognition by this receptor class.</abstract><cop>Brazil</cop><pmid>25036514</pmid><doi>10.4238/2014.June.18.7</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Cercopithecus aethiops COS Cells Epitope Mapping Epitopes - chemistry Epitopes - immunology Epitopes - metabolism Humans Immunoglobulin Fc Fragments - chemistry Immunoglobulin Fc Fragments - immunology Immunoglobulin Fc Fragments - metabolism Immunoglobulin G - metabolism Mice Peptide Fragments - chemical synthesis Peptide Fragments - immunology Peptide Fragments - metabolism Receptors, IgG - metabolism |
| title | Analysis of the linear epitope for Fc-binding on the mouse IgG Fc receptor (moFcγRI) by synthetic peptide |
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