Generation of recombinant, carbohydrate-free intercellular adhesion molecule-1 (ICAM-1) and ICAM-1 fragments in Escherichia coli and mapping of epitopes recognized by anti-ICAM-1 monoclonal antibodies
Intercellular adhesion molecule-1 (ICAM-1) has been shown to interact with the integrin leukocyte function associated antigen-1 (LFA-1) in a variety of cell-cell adhesion phenomena. Furthermore, it serves as a receptor for the majority of the Rhinoviruses and for Plasmodium falciparum-infected human...
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| Veröffentlicht in: | Immunology letters 1991-06, Vol.28 (3), p.237-243 |
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| creator | Mölgg, Martin Schwaeble, Wilhelm Johnson, Judith P. Dierich, Manfred P. |
| description | Intercellular adhesion molecule-1 (ICAM-1) has been shown to interact with the integrin leukocyte function associated antigen-1 (LFA-1) in a variety of cell-cell adhesion phenomena. Furthermore, it serves as a receptor for the majority of the Rhinoviruses and for
Plasmodium falciparum-infected human erythrocytes.
We generated recombinant, carbohydrate-free ICAM-1 and several ICAM-1 fragments by expression in
Escherichia coli using the fusion protein expression system pUEX1–3. In Western blot and dot blot analyses we tested mAbs (7F7, 8B9, P3.58-BA3, -BA11, -BA14, -BA19, -BA21, -BA23, -BA24, -BA26, CL203.4 and 84H10) and a polyclonal antiserum directed against native ICAM-1 for their reactivity with these constructs. We were able to localize the binding site for the mAbs P3.58-BA3, -BA11, -BA14, -BA19, -BA21, -BA23, -BA24 and -BA26 at domain 5, whereas the mAbs 7F7, 8B9, CL203.4 and 84H10 did not recognize the recombinant, carbohydrate-free ICAM-1. Our findings suggest the presence of an immunodominant epitope on domain 5 of ICAM-1. |
| doi_str_mv | 10.1016/0165-2478(91)90010-8 |
| format | Article |
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Plasmodium falciparum-infected human erythrocytes.
We generated recombinant, carbohydrate-free ICAM-1 and several ICAM-1 fragments by expression in
Escherichia coli using the fusion protein expression system pUEX1–3. In Western blot and dot blot analyses we tested mAbs (7F7, 8B9, P3.58-BA3, -BA11, -BA14, -BA19, -BA21, -BA23, -BA24, -BA26, CL203.4 and 84H10) and a polyclonal antiserum directed against native ICAM-1 for their reactivity with these constructs. We were able to localize the binding site for the mAbs P3.58-BA3, -BA11, -BA14, -BA19, -BA21, -BA23, -BA24 and -BA26 at domain 5, whereas the mAbs 7F7, 8B9, CL203.4 and 84H10 did not recognize the recombinant, carbohydrate-free ICAM-1. Our findings suggest the presence of an immunodominant epitope on domain 5 of ICAM-1.</description><identifier>ISSN: 0165-2478</identifier><identifier>EISSN: 1879-0542</identifier><identifier>DOI: 10.1016/0165-2478(91)90010-8</identifier><identifier>PMID: 1715847</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Animals ; Antibodies, Monoclonal - immunology ; Bacterial protein expression ; Blotting, Western ; Carbohydrates - deficiency ; Cell Adhesion Molecules - genetics ; Cell Adhesion Molecules - immunology ; Chromosome Mapping ; Electrophoresis, Polyacrylamide Gel ; Epitope mapping ; Epitopes - immunology ; Escherichia coli - genetics ; Fusion proteins ; Gene Expression ; ICAM-1 ; Mice ; Monoclonal ICAM-1 antibodies ; Peptide Fragments - genetics ; Recombinant Fusion Proteins ; Transfection - genetics</subject><ispartof>Immunology letters, 1991-06, Vol.28 (3), p.237-243</ispartof><rights>1991</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-4d3af865ae054be2885eced23e410395593c1549e1a0b94d404d84e6bb34a7a23</citedby><cites>FETCH-LOGICAL-c357t-4d3af865ae054be2885eced23e410395593c1549e1a0b94d404d84e6bb34a7a23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0165-2478(91)90010-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1715847$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mölgg, Martin</creatorcontrib><creatorcontrib>Schwaeble, Wilhelm</creatorcontrib><creatorcontrib>Johnson, Judith P.</creatorcontrib><creatorcontrib>Dierich, Manfred P.</creatorcontrib><title>Generation of recombinant, carbohydrate-free intercellular adhesion molecule-1 (ICAM-1) and ICAM-1 fragments in Escherichia coli and mapping of epitopes recognized by anti-ICAM-1 monoclonal antibodies</title><title>Immunology letters</title><addtitle>Immunol Lett</addtitle><description>Intercellular adhesion molecule-1 (ICAM-1) has been shown to interact with the integrin leukocyte function associated antigen-1 (LFA-1) in a variety of cell-cell adhesion phenomena. Furthermore, it serves as a receptor for the majority of the Rhinoviruses and for
Plasmodium falciparum-infected human erythrocytes.
We generated recombinant, carbohydrate-free ICAM-1 and several ICAM-1 fragments by expression in
Escherichia coli using the fusion protein expression system pUEX1–3. In Western blot and dot blot analyses we tested mAbs (7F7, 8B9, P3.58-BA3, -BA11, -BA14, -BA19, -BA21, -BA23, -BA24, -BA26, CL203.4 and 84H10) and a polyclonal antiserum directed against native ICAM-1 for their reactivity with these constructs. We were able to localize the binding site for the mAbs P3.58-BA3, -BA11, -BA14, -BA19, -BA21, -BA23, -BA24 and -BA26 at domain 5, whereas the mAbs 7F7, 8B9, CL203.4 and 84H10 did not recognize the recombinant, carbohydrate-free ICAM-1. Our findings suggest the presence of an immunodominant epitope on domain 5 of ICAM-1.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Bacterial protein expression</subject><subject>Blotting, Western</subject><subject>Carbohydrates - deficiency</subject><subject>Cell Adhesion Molecules - genetics</subject><subject>Cell Adhesion Molecules - immunology</subject><subject>Chromosome Mapping</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Epitope mapping</subject><subject>Epitopes - immunology</subject><subject>Escherichia coli - genetics</subject><subject>Fusion proteins</subject><subject>Gene Expression</subject><subject>ICAM-1</subject><subject>Mice</subject><subject>Monoclonal ICAM-1 antibodies</subject><subject>Peptide Fragments - genetics</subject><subject>Recombinant Fusion Proteins</subject><subject>Transfection - genetics</subject><issn>0165-2478</issn><issn>1879-0542</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UU1vFCEYJkZT1-o_0ISTaROpMAM7M5cmpqnVpI0XPRMG3tnFMDACY7L9hf4smZ2N3nogEJ6P9-NB6C2jV4yy7cdyBKl401507LKjlFHSPkMb1jYdoYJXz9HmH-UlepXSz8IRNa_P0BlrmGh5s0F_7sBDVNkGj8OAI-gw9tYrnz9grWIf9gdTYCBDBMDWZ4ganJudiliZPaRFOAYHenZAGL74evPpgbBLrLzB6xsPUe1G8DkVPb5Neg_R6r1VWAdnj8RRTZP1u6UDmGwOE6RjKztvH8Hg_lBY2ZKT3xh80C545Y7ffTAW0mv0YlAuwZvTfY5-fL79fvOF3H-7K7p7omvRZMJNrYZ2KxSUFfVQta0ADaaqgTNad0J0tWaCd8AU7TtuOOWm5bDt-5qrRlX1OXq_-k4x_JohZTnatKxEeQhzkk1FG84bVoh8JeoYUoowyCnaUcWDZFQuAcolHbmkIzsmjwHKtsjenfznfgTzX7QmVvDrFYcy5G8LUSZtwZcZbNlYlibYpwv8BV86rAY</recordid><startdate>19910601</startdate><enddate>19910601</enddate><creator>Mölgg, Martin</creator><creator>Schwaeble, Wilhelm</creator><creator>Johnson, Judith P.</creator><creator>Dierich, Manfred P.</creator><general>Elsevier B.V</general><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></search><sort><creationdate>19910601</creationdate><title>Generation of recombinant, carbohydrate-free intercellular adhesion molecule-1 (ICAM-1) and ICAM-1 fragments in Escherichia coli and mapping of epitopes recognized by anti-ICAM-1 monoclonal antibodies</title><author>Mölgg, Martin ; Schwaeble, Wilhelm ; Johnson, Judith P. ; Dierich, Manfred P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-4d3af865ae054be2885eced23e410395593c1549e1a0b94d404d84e6bb34a7a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Bacterial protein expression</topic><topic>Blotting, Western</topic><topic>Carbohydrates - deficiency</topic><topic>Cell Adhesion Molecules - genetics</topic><topic>Cell Adhesion Molecules - immunology</topic><topic>Chromosome Mapping</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Epitope mapping</topic><topic>Epitopes - immunology</topic><topic>Escherichia coli - genetics</topic><topic>Fusion proteins</topic><topic>Gene Expression</topic><topic>ICAM-1</topic><topic>Mice</topic><topic>Monoclonal ICAM-1 antibodies</topic><topic>Peptide Fragments - genetics</topic><topic>Recombinant Fusion Proteins</topic><topic>Transfection - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mölgg, Martin</creatorcontrib><creatorcontrib>Schwaeble, Wilhelm</creatorcontrib><creatorcontrib>Johnson, Judith P.</creatorcontrib><creatorcontrib>Dierich, Manfred 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><jtitle>Immunology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mölgg, Martin</au><au>Schwaeble, Wilhelm</au><au>Johnson, Judith P.</au><au>Dierich, Manfred P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Generation of recombinant, carbohydrate-free intercellular adhesion molecule-1 (ICAM-1) and ICAM-1 fragments in Escherichia coli and mapping of epitopes recognized by anti-ICAM-1 monoclonal antibodies</atitle><jtitle>Immunology letters</jtitle><addtitle>Immunol Lett</addtitle><date>1991-06-01</date><risdate>1991</risdate><volume>28</volume><issue>3</issue><spage>237</spage><epage>243</epage><pages>237-243</pages><issn>0165-2478</issn><eissn>1879-0542</eissn><abstract>Intercellular adhesion molecule-1 (ICAM-1) has been shown to interact with the integrin leukocyte function associated antigen-1 (LFA-1) in a variety of cell-cell adhesion phenomena. Furthermore, it serves as a receptor for the majority of the Rhinoviruses and for
Plasmodium falciparum-infected human erythrocytes.
We generated recombinant, carbohydrate-free ICAM-1 and several ICAM-1 fragments by expression in
Escherichia coli using the fusion protein expression system pUEX1–3. In Western blot and dot blot analyses we tested mAbs (7F7, 8B9, P3.58-BA3, -BA11, -BA14, -BA19, -BA21, -BA23, -BA24, -BA26, CL203.4 and 84H10) and a polyclonal antiserum directed against native ICAM-1 for their reactivity with these constructs. We were able to localize the binding site for the mAbs P3.58-BA3, -BA11, -BA14, -BA19, -BA21, -BA23, -BA24 and -BA26 at domain 5, whereas the mAbs 7F7, 8B9, CL203.4 and 84H10 did not recognize the recombinant, carbohydrate-free ICAM-1. Our findings suggest the presence of an immunodominant epitope on domain 5 of ICAM-1.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>1715847</pmid><doi>10.1016/0165-2478(91)90010-8</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Immunology letters, 1991-06, Vol.28 (3), p.237-243 |
| issn | 0165-2478 1879-0542 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Animals Antibodies, Monoclonal - immunology Bacterial protein expression Blotting, Western Carbohydrates - deficiency Cell Adhesion Molecules - genetics Cell Adhesion Molecules - immunology Chromosome Mapping Electrophoresis, Polyacrylamide Gel Epitope mapping Epitopes - immunology Escherichia coli - genetics Fusion proteins Gene Expression ICAM-1 Mice Monoclonal ICAM-1 antibodies Peptide Fragments - genetics Recombinant Fusion Proteins Transfection - genetics |
| title | Generation of recombinant, carbohydrate-free intercellular adhesion molecule-1 (ICAM-1) and ICAM-1 fragments in Escherichia coli and mapping of epitopes recognized by anti-ICAM-1 monoclonal antibodies |
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