Mapping the site on human IgG for binding of the MHC class I‐related receptor, FcRn
The analysis of the pharmacokinetics of wild‐type and mutated Fc fragments derived from human IgG1 indicates that Ile253, His310 and His435 play a central role in regulating serum half‐life in mice. Reduced serum half‐life of the recombinant, mutated fragments correlates with decreased binding to th...
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| Veröffentlicht in: | European journal of immunology 1999-09, Vol.29 (9), p.2819-2825 |
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| container_title | European journal of immunology |
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| creator | Kim, Jin‐Kyoo Firan, Mihail Radu, Caius G. Kim, Cheol‐Hong Ghetie, Victor Ward, E. Sally |
| description | The analysis of the pharmacokinetics of wild‐type and mutated Fc fragments derived from human IgG1 indicates that Ile253, His310 and His435 play a central role in regulating serum half‐life in mice. Reduced serum half‐life of the recombinant, mutated fragments correlates with decreased binding to the MHC class I‐related neonatal Fc receptor, FcRn. In addition, the analysis of an Fc fragment in which His435 is mutated to Arg435 demonstrates that the sequence difference at this position between human IgG1 (His435) and IgG3 (Arg435) most likely accounts for the shorter serum half‐life of IgG3 relative to IgG1. In contrast to His310 and His435, the data indicate that His433 does not play a role in regulating the serum half‐life of human IgG1. Thus, the interaction site of mouse FcRn on human and mouse IgG1 involves the same conserved amino acids located at the CH2‐CH3 domain interface of the IgG molecule. The sequence similarities between mouse and human FcRn suggest that these studies have direct relevance to understanding the factors that govern the pharmacokinetics of therapeutic IgG. |
| doi_str_mv | 10.1002/(SICI)1521-4141(199909)29:09<2819::AID-IMMU2819>3.0.CO;2-6 |
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Sally</creator><creatorcontrib>Kim, Jin‐Kyoo ; Firan, Mihail ; Radu, Caius G. ; Kim, Cheol‐Hong ; Ghetie, Victor ; Ward, E. Sally</creatorcontrib><description>The analysis of the pharmacokinetics of wild‐type and mutated Fc fragments derived from human IgG1 indicates that Ile253, His310 and His435 play a central role in regulating serum half‐life in mice. Reduced serum half‐life of the recombinant, mutated fragments correlates with decreased binding to the MHC class I‐related neonatal Fc receptor, FcRn. In addition, the analysis of an Fc fragment in which His435 is mutated to Arg435 demonstrates that the sequence difference at this position between human IgG1 (His435) and IgG3 (Arg435) most likely accounts for the shorter serum half‐life of IgG3 relative to IgG1. In contrast to His310 and His435, the data indicate that His433 does not play a role in regulating the serum half‐life of human IgG1. Thus, the interaction site of mouse FcRn on human and mouse IgG1 involves the same conserved amino acids located at the CH2‐CH3 domain interface of the IgG molecule. The sequence similarities between mouse and human FcRn suggest that these studies have direct relevance to understanding the factors that govern the pharmacokinetics of therapeutic IgG.</description><identifier>ISSN: 0014-2980</identifier><identifier>EISSN: 1521-4141</identifier><identifier>DOI: 10.1002/(SICI)1521-4141(199909)29:09<2819::AID-IMMU2819>3.0.CO;2-6</identifier><identifier>PMID: 10508256</identifier><language>eng</language><publisher>Weinheim: WILEY‐VCH Verlag GmbH</publisher><subject>AFc receptors ; Animals ; Catabolism ; Epitope Mapping - methods ; Half-Life ; Histocompatibility Antigens Class I - immunology ; Histocompatibility Antigens Class I - metabolism ; Humans ; IgG ; Immunoglobulin G - chemistry ; Immunoglobulin G - metabolism ; immunoglobulin G1 ; Mice ; Models, Molecular ; Neonatal Fc receptor ; Receptors, Fc - immunology ; Receptors, Fc - metabolism ; Time Factors</subject><ispartof>European journal of immunology, 1999-09, Vol.29 (9), p.2819-2825</ispartof><rights>1999 WILEY‐VCH Verlag GmbH, Weinheim, Fed. 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Sally</creatorcontrib><title>Mapping the site on human IgG for binding of the MHC class I‐related receptor, FcRn</title><title>European journal of immunology</title><addtitle>Eur J Immunol</addtitle><description>The analysis of the pharmacokinetics of wild‐type and mutated Fc fragments derived from human IgG1 indicates that Ile253, His310 and His435 play a central role in regulating serum half‐life in mice. Reduced serum half‐life of the recombinant, mutated fragments correlates with decreased binding to the MHC class I‐related neonatal Fc receptor, FcRn. In addition, the analysis of an Fc fragment in which His435 is mutated to Arg435 demonstrates that the sequence difference at this position between human IgG1 (His435) and IgG3 (Arg435) most likely accounts for the shorter serum half‐life of IgG3 relative to IgG1. In contrast to His310 and His435, the data indicate that His433 does not play a role in regulating the serum half‐life of human IgG1. Thus, the interaction site of mouse FcRn on human and mouse IgG1 involves the same conserved amino acids located at the CH2‐CH3 domain interface of the IgG molecule. The sequence similarities between mouse and human FcRn suggest that these studies have direct relevance to understanding the factors that govern the pharmacokinetics of therapeutic IgG.</description><subject>AFc receptors</subject><subject>Animals</subject><subject>Catabolism</subject><subject>Epitope Mapping - methods</subject><subject>Half-Life</subject><subject>Histocompatibility Antigens Class I - immunology</subject><subject>Histocompatibility Antigens Class I - metabolism</subject><subject>Humans</subject><subject>IgG</subject><subject>Immunoglobulin G - chemistry</subject><subject>Immunoglobulin G - metabolism</subject><subject>immunoglobulin G1</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Neonatal Fc receptor</subject><subject>Receptors, Fc - immunology</subject><subject>Receptors, Fc - metabolism</subject><subject>Time Factors</subject><issn>0014-2980</issn><issn>1521-4141</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9u1DAQhy0EokvhFZBPqJXIMrbzx7MgpBJoG6mrlYC9cGCUOE4blE2CnRXqjUfgGXkSElIqJIR6sWXr82_G8zH2RsBSAMgXRx-yNDsWkRRBKEJxJBAR8FjiCvCV1AJXq5PsbZCt19vp9FotYZluXsogvscWt8_uswWACAOJGg7YI--_AADGET5kBwIi0DKKF2y7zvu-bi_5cGW5rwfLu5Zf7Xd5y7PLM151jhd1W05EV_2G1ucpN03uPc9-fv_hbJMPtuTOGtsPnXvOT8379jF7UOWNt09u9kO2PX33MT0PLjZnWXpyEZgwCTGwGhNIEowwKrBIUJda56CgklCGqkKwWkmDodEqFtKAtCpOSp0UqhBa2kodsmdzbu-6r3vrB9rV3timyVvb7T2N6VqPH70TFInCRGA4gp9m0LjOe2cr6l29y901CaDJDtFkh6Yx0zRmmu2QRJrW0QfRaIf-2CFFQOmGJMVj-NObLvbFzpZ_Rc86RuDzDHyrG3v9T-k7K_-n8O2d-gXvc6pw</recordid><startdate>199909</startdate><enddate>199909</enddate><creator>Kim, Jin‐Kyoo</creator><creator>Firan, Mihail</creator><creator>Radu, Caius G.</creator><creator>Kim, Cheol‐Hong</creator><creator>Ghetie, Victor</creator><creator>Ward, E. Sally</creator><general>WILEY‐VCH Verlag GmbH</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>199909</creationdate><title>Mapping the site on human IgG for binding of the MHC class I‐related receptor, FcRn</title><author>Kim, Jin‐Kyoo ; Firan, Mihail ; Radu, Caius G. ; Kim, Cheol‐Hong ; Ghetie, Victor ; Ward, E. Sally</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4749-e8970779595b9b798d88a030f20d43f90e832c94c83612c02e367d87b3b182ef3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>AFc receptors</topic><topic>Animals</topic><topic>Catabolism</topic><topic>Epitope Mapping - methods</topic><topic>Half-Life</topic><topic>Histocompatibility Antigens Class I - immunology</topic><topic>Histocompatibility Antigens Class I - metabolism</topic><topic>Humans</topic><topic>IgG</topic><topic>Immunoglobulin G - chemistry</topic><topic>Immunoglobulin G - metabolism</topic><topic>immunoglobulin G1</topic><topic>Mice</topic><topic>Models, Molecular</topic><topic>Neonatal Fc receptor</topic><topic>Receptors, Fc - immunology</topic><topic>Receptors, Fc - metabolism</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Jin‐Kyoo</creatorcontrib><creatorcontrib>Firan, Mihail</creatorcontrib><creatorcontrib>Radu, Caius G.</creatorcontrib><creatorcontrib>Kim, Cheol‐Hong</creatorcontrib><creatorcontrib>Ghetie, Victor</creatorcontrib><creatorcontrib>Ward, E. Sally</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Jin‐Kyoo</au><au>Firan, Mihail</au><au>Radu, Caius G.</au><au>Kim, Cheol‐Hong</au><au>Ghetie, Victor</au><au>Ward, E. Sally</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mapping the site on human IgG for binding of the MHC class I‐related receptor, FcRn</atitle><jtitle>European journal of immunology</jtitle><addtitle>Eur J Immunol</addtitle><date>1999-09</date><risdate>1999</risdate><volume>29</volume><issue>9</issue><spage>2819</spage><epage>2825</epage><pages>2819-2825</pages><issn>0014-2980</issn><eissn>1521-4141</eissn><abstract>The analysis of the pharmacokinetics of wild‐type and mutated Fc fragments derived from human IgG1 indicates that Ile253, His310 and His435 play a central role in regulating serum half‐life in mice. Reduced serum half‐life of the recombinant, mutated fragments correlates with decreased binding to the MHC class I‐related neonatal Fc receptor, FcRn. In addition, the analysis of an Fc fragment in which His435 is mutated to Arg435 demonstrates that the sequence difference at this position between human IgG1 (His435) and IgG3 (Arg435) most likely accounts for the shorter serum half‐life of IgG3 relative to IgG1. In contrast to His310 and His435, the data indicate that His433 does not play a role in regulating the serum half‐life of human IgG1. Thus, the interaction site of mouse FcRn on human and mouse IgG1 involves the same conserved amino acids located at the CH2‐CH3 domain interface of the IgG molecule. The sequence similarities between mouse and human FcRn suggest that these studies have direct relevance to understanding the factors that govern the pharmacokinetics of therapeutic IgG.</abstract><cop>Weinheim</cop><pub>WILEY‐VCH Verlag GmbH</pub><pmid>10508256</pmid><doi>10.1002/(SICI)1521-4141(199909)29:09<2819::AID-IMMU2819>3.0.CO;2-6</doi><tpages>7</tpages></addata></record> |
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| ispartof | European journal of immunology, 1999-09, Vol.29 (9), p.2819-2825 |
| issn | 0014-2980 1521-4141 |
| language | eng |
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| source | MEDLINE; Access via Wiley Online Library; EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection) |
| subjects | AFc receptors Animals Catabolism Epitope Mapping - methods Half-Life Histocompatibility Antigens Class I - immunology Histocompatibility Antigens Class I - metabolism Humans IgG Immunoglobulin G - chemistry Immunoglobulin G - metabolism immunoglobulin G1 Mice Models, Molecular Neonatal Fc receptor Receptors, Fc - immunology Receptors, Fc - metabolism Time Factors |
| title | Mapping the site on human IgG for binding of the MHC class I‐related receptor, FcRn |
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