Specific Interaction of CCR5 Amino-Terminal Domain Peptides Containing Sulfotyrosines with HIV-1 Envelope Glycoprotein gp120
The HIV-1 envelope glycoprotein gp120 interacts consecutively with CD4 and the CCR5 coreceptor to mediate the entry of certain HIV-1 strains into target cells. Acidic residues and sulfotyrosines in the amino-terminal domain (Nt) of CCR5 are crucial for viral fusion and entry. We tested the binding o...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2000-05, Vol.97 (11), p.5762-5767 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Cormier, Emmanuel G. Persuh, Marjan Daniah A. D. Thompson Lin, Steven W. Sakmar, Thomas P. Olson, William C. Dragic, Tatjana |
| description | The HIV-1 envelope glycoprotein gp120 interacts consecutively with CD4 and the CCR5 coreceptor to mediate the entry of certain HIV-1 strains into target cells. Acidic residues and sulfotyrosines in the amino-terminal domain (Nt) of CCR5 are crucial for viral fusion and entry. We tested the binding of a panel of CCR5 Nt peptides to different soluble gp120/CD4 complexes and anti-CCR5 mAbs. The tyrosine residues in the peptides were sulfated, phosphorylated, or unmodified. None of the gp120/CD4 complexes associated with peptides containing unmodified or phosphorylated tyrosines. The gp120/CD4 complexes containing envelope glycoproteins from isolates that use CCR5 as a coreceptor associated with Nt peptides containing sulfotyrosines but not with peptides containing sulfotyrosines in scrambled Nt sequences. Finally, only peptides containing sulfotyrosines inhibited the entry of an R5 isolate. Our data show that proper posttranslational modification of the CCR5 Nt is required for gp120 binding and viral entry. More importantly, the Nt domain determines the specificity of the interaction between CCR5 and gp120s from isolates that use this coreceptor. |
| doi_str_mv | 10.1073/pnas.97.11.5762 |
| format | Article |
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The gp120/CD4 complexes containing envelope glycoproteins from isolates that use CCR5 as a coreceptor associated with Nt peptides containing sulfotyrosines but not with peptides containing sulfotyrosines in scrambled Nt sequences. Finally, only peptides containing sulfotyrosines inhibited the entry of an R5 isolate. Our data show that proper posttranslational modification of the CCR5 Nt is required for gp120 binding and viral entry. More importantly, the Nt domain determines the specificity of the interaction between CCR5 and gp120s from isolates that use this coreceptor.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.97.11.5762</identifier><identifier>PMID: 10823934</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Amino acids ; Antibodies, Monoclonal - pharmacology ; Biological Sciences ; CCR5 protein ; CD4 antigen ; CD4 Antigens - chemistry ; CD4 Antigens - metabolism ; Cell Line ; Cell lines ; Drug interactions ; Epitopes ; Epitopes - metabolism ; glycoprotein gp120 ; Glycoproteins ; HeLa Cells ; HIV 1 ; HIV Envelope Protein gp120 - chemistry ; HIV Envelope Protein gp120 - metabolism ; HIV-1 - metabolism ; Human immunodeficiency virus 1 ; Human T-lymphotropic virus 1 - metabolism ; Humans ; Leukemia Virus, Murine - metabolism ; Macromolecular Substances ; Molecular Sequence Data ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Peptide Fragments - pharmacology ; Protein Binding - drug effects ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Receptors, CCR5 - chemistry ; Receptors, CCR5 - metabolism ; Sensors ; Sulfates ; Sulfation ; Surface Plasmon Resonance ; Tyrosine - analogs & derivatives ; Tyrosine - physiology</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2000-05, Vol.97 (11), p.5762-5767</ispartof><rights>Copyright 1993-2000 National Academy of Sciences of the United States of America</rights><rights>Copyright © 2000, The National Academy of Sciences 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c493t-193312094e4707bb6d1638e42df2a9165ab73636fbf65aa5e9d019ffe2e0fc863</citedby><cites>FETCH-LOGICAL-c493t-193312094e4707bb6d1638e42df2a9165ab73636fbf65aa5e9d019ffe2e0fc863</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/97/11.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/122530$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/122530$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10823934$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cormier, Emmanuel G.</creatorcontrib><creatorcontrib>Persuh, Marjan</creatorcontrib><creatorcontrib>Daniah A. D. Thompson</creatorcontrib><creatorcontrib>Lin, Steven W.</creatorcontrib><creatorcontrib>Sakmar, Thomas P.</creatorcontrib><creatorcontrib>Olson, William C.</creatorcontrib><creatorcontrib>Dragic, Tatjana</creatorcontrib><title>Specific Interaction of CCR5 Amino-Terminal Domain Peptides Containing Sulfotyrosines with HIV-1 Envelope Glycoprotein gp120</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The HIV-1 envelope glycoprotein gp120 interacts consecutively with CD4 and the CCR5 coreceptor to mediate the entry of certain HIV-1 strains into target cells. Acidic residues and sulfotyrosines in the amino-terminal domain (Nt) of CCR5 are crucial for viral fusion and entry. We tested the binding of a panel of CCR5 Nt peptides to different soluble gp120/CD4 complexes and anti-CCR5 mAbs. The tyrosine residues in the peptides were sulfated, phosphorylated, or unmodified. None of the gp120/CD4 complexes associated with peptides containing unmodified or phosphorylated tyrosines. The gp120/CD4 complexes containing envelope glycoproteins from isolates that use CCR5 as a coreceptor associated with Nt peptides containing sulfotyrosines but not with peptides containing sulfotyrosines in scrambled Nt sequences. Finally, only peptides containing sulfotyrosines inhibited the entry of an R5 isolate. Our data show that proper posttranslational modification of the CCR5 Nt is required for gp120 binding and viral entry. More importantly, the Nt domain determines the specificity of the interaction between CCR5 and gp120s from isolates that use this coreceptor.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Antibodies, Monoclonal - pharmacology</subject><subject>Biological Sciences</subject><subject>CCR5 protein</subject><subject>CD4 antigen</subject><subject>CD4 Antigens - chemistry</subject><subject>CD4 Antigens - metabolism</subject><subject>Cell Line</subject><subject>Cell lines</subject><subject>Drug interactions</subject><subject>Epitopes</subject><subject>Epitopes - metabolism</subject><subject>glycoprotein gp120</subject><subject>Glycoproteins</subject><subject>HeLa Cells</subject><subject>HIV 1</subject><subject>HIV Envelope Protein gp120 - chemistry</subject><subject>HIV Envelope Protein gp120 - metabolism</subject><subject>HIV-1 - metabolism</subject><subject>Human immunodeficiency virus 1</subject><subject>Human T-lymphotropic virus 1 - metabolism</subject><subject>Humans</subject><subject>Leukemia Virus, Murine - metabolism</subject><subject>Macromolecular Substances</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptide Fragments - pharmacology</subject><subject>Protein Binding - drug effects</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Structure, Tertiary</subject><subject>Receptors, CCR5 - chemistry</subject><subject>Receptors, CCR5 - metabolism</subject><subject>Sensors</subject><subject>Sulfates</subject><subject>Sulfation</subject><subject>Surface Plasmon Resonance</subject><subject>Tyrosine - analogs & derivatives</subject><subject>Tyrosine - physiology</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EosvCmQMS8glO2fojiWOJSxVKu1IlEC1cLScZb10ldoidwkr88Xi1C10kJE5j-f3m2TMPoZeUrCgR_HR0OqykWFG6KkTJHqEFJZJmZS7JY7QghImsyll-gp6FcEcIkUVFnqITSirGJc8X6Of1CK01tsVrF2HSbbTeYW9wXX8u8Nlgnc9uYEpV9_i9H7R1-BOM0XYQcO1dTBfWbfD13Bsft5MP1iXlu423-HL9NaP43N1D70fAF_229ePkIySPzUgZeY6eGN0HeHGoS_Tlw_lNfZldfbxY12dXWZtLHjMqOU-0zCEXRDRN2dGSV5CzzjAtaVnoRvCSl6Yx6awLkB2h0hhgQExblXyJ3u19x7kZoGvBxUn3apzsoKet8tqqvxVnb9XG3ytaFWnLS_Tm0D75bzOEqAYbWuh77cDPQQlKWVVI8l-QioIJnmZaotM92KaFhQnMn79QonbBql2wSgpFqdoFmzpeH49wxO-TTMDbA7Dr_C0_OCgz932EH_HI6t9kAl7tgbsQ_fTwFGMFJ_wXHUfB5g</recordid><startdate>20000523</startdate><enddate>20000523</enddate><creator>Cormier, Emmanuel G.</creator><creator>Persuh, Marjan</creator><creator>Daniah A. D. Thompson</creator><creator>Lin, Steven W.</creator><creator>Sakmar, Thomas P.</creator><creator>Olson, William C.</creator><creator>Dragic, Tatjana</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>The National Academy of Sciences</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>7U9</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000523</creationdate><title>Specific Interaction of CCR5 Amino-Terminal Domain Peptides Containing Sulfotyrosines with HIV-1 Envelope Glycoprotein gp120</title><author>Cormier, Emmanuel G. ; Persuh, Marjan ; Daniah A. D. Thompson ; Lin, Steven W. ; Sakmar, Thomas P. ; Olson, William C. ; Dragic, Tatjana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c493t-193312094e4707bb6d1638e42df2a9165ab73636fbf65aa5e9d019ffe2e0fc863</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Antibodies, Monoclonal - pharmacology</topic><topic>Biological Sciences</topic><topic>CCR5 protein</topic><topic>CD4 antigen</topic><topic>CD4 Antigens - chemistry</topic><topic>CD4 Antigens - metabolism</topic><topic>Cell Line</topic><topic>Cell lines</topic><topic>Drug interactions</topic><topic>Epitopes</topic><topic>Epitopes - metabolism</topic><topic>glycoprotein gp120</topic><topic>Glycoproteins</topic><topic>HeLa Cells</topic><topic>HIV 1</topic><topic>HIV Envelope Protein gp120 - chemistry</topic><topic>HIV Envelope Protein gp120 - metabolism</topic><topic>HIV-1 - metabolism</topic><topic>Human immunodeficiency virus 1</topic><topic>Human T-lymphotropic virus 1 - metabolism</topic><topic>Humans</topic><topic>Leukemia Virus, Murine - metabolism</topic><topic>Macromolecular Substances</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - metabolism</topic><topic>Peptide Fragments - pharmacology</topic><topic>Protein Binding - drug effects</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein Structure, Tertiary</topic><topic>Receptors, CCR5 - chemistry</topic><topic>Receptors, CCR5 - metabolism</topic><topic>Sensors</topic><topic>Sulfates</topic><topic>Sulfation</topic><topic>Surface Plasmon Resonance</topic><topic>Tyrosine - analogs & derivatives</topic><topic>Tyrosine - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cormier, Emmanuel G.</creatorcontrib><creatorcontrib>Persuh, Marjan</creatorcontrib><creatorcontrib>Daniah A. D. Thompson</creatorcontrib><creatorcontrib>Lin, Steven W.</creatorcontrib><creatorcontrib>Sakmar, Thomas P.</creatorcontrib><creatorcontrib>Olson, William C.</creatorcontrib><creatorcontrib>Dragic, Tatjana</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cormier, Emmanuel G.</au><au>Persuh, Marjan</au><au>Daniah A. D. Thompson</au><au>Lin, Steven W.</au><au>Sakmar, Thomas P.</au><au>Olson, William C.</au><au>Dragic, Tatjana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Specific Interaction of CCR5 Amino-Terminal Domain Peptides Containing Sulfotyrosines with HIV-1 Envelope Glycoprotein gp120</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2000-05-23</date><risdate>2000</risdate><volume>97</volume><issue>11</issue><spage>5762</spage><epage>5767</epage><pages>5762-5767</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The HIV-1 envelope glycoprotein gp120 interacts consecutively with CD4 and the CCR5 coreceptor to mediate the entry of certain HIV-1 strains into target cells. Acidic residues and sulfotyrosines in the amino-terminal domain (Nt) of CCR5 are crucial for viral fusion and entry. We tested the binding of a panel of CCR5 Nt peptides to different soluble gp120/CD4 complexes and anti-CCR5 mAbs. The tyrosine residues in the peptides were sulfated, phosphorylated, or unmodified. None of the gp120/CD4 complexes associated with peptides containing unmodified or phosphorylated tyrosines. The gp120/CD4 complexes containing envelope glycoproteins from isolates that use CCR5 as a coreceptor associated with Nt peptides containing sulfotyrosines but not with peptides containing sulfotyrosines in scrambled Nt sequences. Finally, only peptides containing sulfotyrosines inhibited the entry of an R5 isolate. Our data show that proper posttranslational modification of the CCR5 Nt is required for gp120 binding and viral entry. More importantly, the Nt domain determines the specificity of the interaction between CCR5 and gp120s from isolates that use this coreceptor.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>10823934</pmid><doi>10.1073/pnas.97.11.5762</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Antibodies, Monoclonal - pharmacology Biological Sciences CCR5 protein CD4 antigen CD4 Antigens - chemistry CD4 Antigens - metabolism Cell Line Cell lines Drug interactions Epitopes Epitopes - metabolism glycoprotein gp120 Glycoproteins HeLa Cells HIV 1 HIV Envelope Protein gp120 - chemistry HIV Envelope Protein gp120 - metabolism HIV-1 - metabolism Human immunodeficiency virus 1 Human T-lymphotropic virus 1 - metabolism Humans Leukemia Virus, Murine - metabolism Macromolecular Substances Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - metabolism Peptide Fragments - pharmacology Protein Binding - drug effects Protein Processing, Post-Translational Protein Structure, Tertiary Receptors, CCR5 - chemistry Receptors, CCR5 - metabolism Sensors Sulfates Sulfation Surface Plasmon Resonance Tyrosine - analogs & derivatives Tyrosine - physiology |
| title | Specific Interaction of CCR5 Amino-Terminal Domain Peptides Containing Sulfotyrosines with HIV-1 Envelope Glycoprotein gp120 |
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