Recognition of Human Cytomegalovirus by Human Primary Immunoglobulins Identifies an Innate Foundation to an Adaptive Immune Response
Most primates, including humans, are chronically infected with cospecifically evolved, potentially pathogenic CMV. Abs that bind a 10-aa linear epitope (antigenic determinant 2 site 1) within the extracellular domain of human CMV glycoprotein B neutralize viral infectivity. In this study, we show th...
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| Veröffentlicht in: | The Journal of immunology (1950) 2005-04, Vol.174 (8), p.4768-4778 |
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| container_title | The Journal of immunology (1950) |
| container_volume | 174 |
| creator | McLean, Gary R Olsen, Ole A Watt, Ian N Rathanaswami, P Leslie, Kevin B Babcook, John S Schrader, John W |
| description | Most primates, including humans, are chronically infected with cospecifically evolved, potentially pathogenic CMV. Abs that bind a 10-aa linear epitope (antigenic determinant 2 site 1) within the extracellular domain of human CMV glycoprotein B neutralize viral infectivity. In this study, we show that genes generated by recombinations involving two well-conserved human germline V elements (IGHV3-30 and IGKV3-11), and IGHJ4, encode primary Ig molecules that bind glycoprotein B at this key epitope. These particular V(H), J(H), and V(kappa) genes enable humans to generate through recombination and N nucleotide addition, a useful frequency of primary Igs that efficiently target this critical site on human CMV and thus confer an innate foundation for a specific adaptive response to this pathogen. |
| doi_str_mv | 10.4049/jimmunol.174.8.4768 |
| format | Article |
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Abs that bind a 10-aa linear epitope (antigenic determinant 2 site 1) within the extracellular domain of human CMV glycoprotein B neutralize viral infectivity. In this study, we show that genes generated by recombinations involving two well-conserved human germline V elements (IGHV3-30 and IGKV3-11), and IGHJ4, encode primary Ig molecules that bind glycoprotein B at this key epitope. 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Abs that bind a 10-aa linear epitope (antigenic determinant 2 site 1) within the extracellular domain of human CMV glycoprotein B neutralize viral infectivity. In this study, we show that genes generated by recombinations involving two well-conserved human germline V elements (IGHV3-30 and IGKV3-11), and IGHJ4, encode primary Ig molecules that bind glycoprotein B at this key epitope. These particular V(H), J(H), and V(kappa) genes enable humans to generate through recombination and N nucleotide addition, a useful frequency of primary Igs that efficiently target this critical site on human CMV and thus confer an innate foundation for a specific adaptive response to this pathogen.</description><subject>Adaptation, Physiological</subject><subject>Amino Acid Sequence</subject><subject>Antibodies, Viral - chemistry</subject><subject>Antibodies, Viral - genetics</subject><subject>Antibodies, Viral - metabolism</subject><subject>Antigens, Viral - genetics</subject><subject>Base Sequence</subject><subject>Codon - genetics</subject><subject>Cytomegalovirus - immunology</subject><subject>DNA, Complementary - genetics</subject><subject>Human cytomegalovirus</subject><subject>Humans</subject><subject>Immunity, Innate</subject><subject>Immunoglobulin Heavy Chains - genetics</subject><subject>Immunoglobulin Light Chains - genetics</subject><subject>Immunoglobulin Variable Region - genetics</subject><subject>Immunoglobulins - chemistry</subject><subject>Immunoglobulins - genetics</subject><subject>Immunoglobulins - metabolism</subject><subject>In Vitro Techniques</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - genetics</subject><subject>Peptide Fragments - immunology</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Viral Envelope Proteins - genetics</subject><subject>Viral Envelope Proteins - immunology</subject><issn>0022-1767</issn><issn>1550-6606</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFr3DAQhUVpaLZJf0Gh-NSevJ2xZMs-hiVpFgItITkL2R5tFGRpa9lZ9t4fXjve0t56Gpj53htmHmMfEdYCRPX12Xbd6INboxTrci1kUb5hK8xzSIsCirdsBZBlKcpCnrP3MT4DQAGZeMfOMS9RSMhW7Nc9NWHn7WCDT4JJbsdO-2RzHEJHO-3Ci-3HmNTH0-BHbzvdH5Pt6-qdC_XorI_JtiU_WGMpJhO19V4PlNyE0bf61XkIc_-q1fvBvtAip-Se4j74SJfszGgX6cOpXrDHm-uHzW169_3bdnN1lzYCcUiREzUSUACSkNNdJgPEQksuSJuKi5YENTW0JTembSE3lJdcSsqwAqiRX7DPi---Dz9HioPqbGzIOe0pjFEVUiLPpPwvOH284ryaQb6ATR9i7Mmo_fIhhaDmlNSflGaNKtWc0qT6dLIf647av5pTLBPwZQGe7O7pYHtSsdPOTTiqw-Hwj9VvfG-gFw</recordid><startdate>20050415</startdate><enddate>20050415</enddate><creator>McLean, Gary R</creator><creator>Olsen, Ole A</creator><creator>Watt, Ian N</creator><creator>Rathanaswami, P</creator><creator>Leslie, Kevin B</creator><creator>Babcook, John S</creator><creator>Schrader, John W</creator><general>Am Assoc Immnol</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20050415</creationdate><title>Recognition of Human Cytomegalovirus by Human Primary Immunoglobulins Identifies an Innate Foundation to an Adaptive Immune Response</title><author>McLean, Gary R ; Olsen, Ole A ; Watt, Ian N ; Rathanaswami, P ; Leslie, Kevin B ; Babcook, John S ; Schrader, John W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-13eec701401e47176f20116a734eaf934de4ecb0d83ffdd05fe58377e21900b13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adaptation, Physiological</topic><topic>Amino Acid Sequence</topic><topic>Antibodies, Viral - chemistry</topic><topic>Antibodies, Viral - genetics</topic><topic>Antibodies, Viral - metabolism</topic><topic>Antigens, Viral - genetics</topic><topic>Base Sequence</topic><topic>Codon - genetics</topic><topic>Cytomegalovirus - immunology</topic><topic>DNA, Complementary - genetics</topic><topic>Human cytomegalovirus</topic><topic>Humans</topic><topic>Immunity, Innate</topic><topic>Immunoglobulin Heavy Chains - genetics</topic><topic>Immunoglobulin Light Chains - genetics</topic><topic>Immunoglobulin Variable Region - genetics</topic><topic>Immunoglobulins - chemistry</topic><topic>Immunoglobulins - genetics</topic><topic>Immunoglobulins - metabolism</topic><topic>In Vitro Techniques</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments - genetics</topic><topic>Peptide Fragments - immunology</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Viral Envelope Proteins - genetics</topic><topic>Viral Envelope Proteins - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McLean, Gary R</creatorcontrib><creatorcontrib>Olsen, Ole A</creatorcontrib><creatorcontrib>Watt, Ian N</creatorcontrib><creatorcontrib>Rathanaswami, P</creatorcontrib><creatorcontrib>Leslie, Kevin B</creatorcontrib><creatorcontrib>Babcook, John S</creatorcontrib><creatorcontrib>Schrader, John W</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>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of immunology (1950)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McLean, Gary R</au><au>Olsen, Ole A</au><au>Watt, Ian N</au><au>Rathanaswami, P</au><au>Leslie, Kevin B</au><au>Babcook, John S</au><au>Schrader, John W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recognition of Human Cytomegalovirus by Human Primary Immunoglobulins Identifies an Innate Foundation to an Adaptive Immune Response</atitle><jtitle>The Journal of immunology (1950)</jtitle><addtitle>J Immunol</addtitle><date>2005-04-15</date><risdate>2005</risdate><volume>174</volume><issue>8</issue><spage>4768</spage><epage>4778</epage><pages>4768-4778</pages><issn>0022-1767</issn><eissn>1550-6606</eissn><abstract>Most primates, including humans, are chronically infected with cospecifically evolved, potentially pathogenic CMV. 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| source | MEDLINE; Free E-Journal (出版社公開部分のみ）; Alma/SFX Local Collection |
| subjects | Adaptation, Physiological Amino Acid Sequence Antibodies, Viral - chemistry Antibodies, Viral - genetics Antibodies, Viral - metabolism Antigens, Viral - genetics Base Sequence Codon - genetics Cytomegalovirus - immunology DNA, Complementary - genetics Human cytomegalovirus Humans Immunity, Innate Immunoglobulin Heavy Chains - genetics Immunoglobulin Light Chains - genetics Immunoglobulin Variable Region - genetics Immunoglobulins - chemistry Immunoglobulins - genetics Immunoglobulins - metabolism In Vitro Techniques Molecular Sequence Data Peptide Fragments - genetics Peptide Fragments - immunology Recombinant Proteins - genetics Recombinant Proteins - immunology Recombinant Proteins - metabolism Sequence Homology, Amino Acid Viral Envelope Proteins - genetics Viral Envelope Proteins - immunology |
| title | Recognition of Human Cytomegalovirus by Human Primary Immunoglobulins Identifies an Innate Foundation to an Adaptive Immune Response |
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