Novel anti-CD4 monoclonal antibodies separate human immunodeficiency virus infection and fusion of CD4+ cells from virus binding
Human immunodeficiency virus (HIV) binds to cells via an interaction between CD4 and the virus envelope glycoprotein, gp120. Previous studies have localized the high affinity binding site for gp120 to the first domain of CD4, and monoclonal antibodies (mAbs) reactive with this region compete with gp...
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| Veröffentlicht in: | The Journal of experimental medicine 1990-10, Vol.172 (4), p.1233-1242 |
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| container_title | The Journal of experimental medicine |
| container_volume | 172 |
| creator | HEALEY, D DIANDA, L MOORE, J. P MCDOUGAL, J. S MOORE, M. J ESTESS, P BUCK, D KWONG, P. D BEVERLEY, P. C. L SATTENTAU, Q. J |
| description | Human immunodeficiency virus (HIV) binds to cells via an interaction between CD4 and the virus envelope glycoprotein, gp120. Previous studies have localized the high affinity binding site for gp120 to the first domain of CD4, and monoclonal antibodies (mAbs) reactive with this region compete with gp120 binding and thereby block virus infectivity and syncytium formation. Despite a detailed understanding of the binding of gp120 to CD4, little is known of subsequent events leading to membrane fusion and virus entry. We describe two new mAbs reactive with the third domain of CD4 that inhibit steps subsequent to virus binding critical for HIV infectivity and cell fusion. Binding of recombinant gp120 or virus to CD4 is not inhibited by these antibodies, whereas infection and syncytium formation by a number of HIV isolates are blocked. These findings demonstrate that in addition to virus binding, CD4 may have an active role in membrane fusion. |
| doi_str_mv | 10.1084/jem.172.4.1233 |
| format | Article |
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P ; MCDOUGAL, J. S ; MOORE, M. J ; ESTESS, P ; BUCK, D ; KWONG, P. D ; BEVERLEY, P. C. L ; SATTENTAU, Q. J</creator><creatorcontrib>HEALEY, D ; DIANDA, L ; MOORE, J. P ; MCDOUGAL, J. S ; MOORE, M. J ; ESTESS, P ; BUCK, D ; KWONG, P. D ; BEVERLEY, P. C. L ; SATTENTAU, Q. J</creatorcontrib><description>Human immunodeficiency virus (HIV) binds to cells via an interaction between CD4 and the virus envelope glycoprotein, gp120. Previous studies have localized the high affinity binding site for gp120 to the first domain of CD4, and monoclonal antibodies (mAbs) reactive with this region compete with gp120 binding and thereby block virus infectivity and syncytium formation. Despite a detailed understanding of the binding of gp120 to CD4, little is known of subsequent events leading to membrane fusion and virus entry. We describe two new mAbs reactive with the third domain of CD4 that inhibit steps subsequent to virus binding critical for HIV infectivity and cell fusion. Binding of recombinant gp120 or virus to CD4 is not inhibited by these antibodies, whereas infection and syncytium formation by a number of HIV isolates are blocked. These findings demonstrate that in addition to virus binding, CD4 may have an active role in membrane fusion.</description><identifier>ISSN: 0022-1007</identifier><identifier>EISSN: 1540-9538</identifier><identifier>DOI: 10.1084/jem.172.4.1233</identifier><identifier>PMID: 1698911</identifier><identifier>CODEN: JEMEAV</identifier><language>eng</language><publisher>New York, NY: Rockefeller University Press</publisher><subject>AIDS/HIV ; Animals ; Antibodies, Monoclonal - immunology ; Binding Sites ; Biological and medical sciences ; CD4 Antigens - immunology ; CD4 Antigens - physiology ; CD4-Positive T-Lymphocytes - microbiology ; Cell Fusion ; Epitopes - analysis ; Fundamental and applied biological sciences. 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Despite a detailed understanding of the binding of gp120 to CD4, little is known of subsequent events leading to membrane fusion and virus entry. We describe two new mAbs reactive with the third domain of CD4 that inhibit steps subsequent to virus binding critical for HIV infectivity and cell fusion. Binding of recombinant gp120 or virus to CD4 is not inhibited by these antibodies, whereas infection and syncytium formation by a number of HIV isolates are blocked. These findings demonstrate that in addition to virus binding, CD4 may have an active role in membrane fusion.</description><subject>AIDS/HIV</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>CD4 Antigens - immunology</subject><subject>CD4 Antigens - physiology</subject><subject>CD4-Positive T-Lymphocytes - microbiology</subject><subject>Cell Fusion</subject><subject>Epitopes - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HIV Envelope Protein gp120 - metabolism</subject><subject>HIV Infections - prevention & control</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Microbiology</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>Virology</subject><issn>0022-1007</issn><issn>1540-9538</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkb1vFDEQxS1EFI5AS4fkBhq0G3-u7QYpOj6lKDRQW16vnTha24e9e1I6_vT4dCcC1VjzfvM8owfAG4x6jCS7vHexx4L0rMeE0mdggzlDneJUPgcbhAjpMELiBXhZ6z1CmDE-nINzPCipMN6APzd572Zo0hK67ScGY07ZzjmZY2_MU3AVVrczxSwO3q3RJBhiXFOenA82uGQf4D6UtcKQvLNLyKmNTtCv9fDMHjbfD9C6ea7QlxxP9BjSFNLtK3DmzVzd61O9AL--fP65_dZd__j6fXt13Vkm8dKNzkk7IasGKgfMBCXcWEqkEGJUfCSScMuIZdRIrwQXTHKsKKfUTlgYL-gF-Hj03a1jdJN1aSlm1rsSoikPOpug_1dSuNO3ea8JlpIr0gzenwxK_r26uugY6uEqk1xeq5YIsbYGamB_BG3JtRbn_36CkT5kpltmumWmmT5k1gbe_rvaE34MqenvTrqp1sy-mGRDfcLUMLTzFX0EZm-hgA</recordid><startdate>19901001</startdate><enddate>19901001</enddate><creator>HEALEY, D</creator><creator>DIANDA, L</creator><creator>MOORE, J. 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Psychology</topic><topic>HIV Envelope Protein gp120 - metabolism</topic><topic>HIV Infections - prevention & control</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Microbiology</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HEALEY, D</creatorcontrib><creatorcontrib>DIANDA, L</creatorcontrib><creatorcontrib>MOORE, J. P</creatorcontrib><creatorcontrib>MCDOUGAL, J. S</creatorcontrib><creatorcontrib>MOORE, M. J</creatorcontrib><creatorcontrib>ESTESS, P</creatorcontrib><creatorcontrib>BUCK, D</creatorcontrib><creatorcontrib>KWONG, P. D</creatorcontrib><creatorcontrib>BEVERLEY, P. C. L</creatorcontrib><creatorcontrib>SATTENTAU, Q. 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J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel anti-CD4 monoclonal antibodies separate human immunodeficiency virus infection and fusion of CD4+ cells from virus binding</atitle><jtitle>The Journal of experimental medicine</jtitle><addtitle>J Exp Med</addtitle><date>1990-10-01</date><risdate>1990</risdate><volume>172</volume><issue>4</issue><spage>1233</spage><epage>1242</epage><pages>1233-1242</pages><issn>0022-1007</issn><eissn>1540-9538</eissn><coden>JEMEAV</coden><abstract>Human immunodeficiency virus (HIV) binds to cells via an interaction between CD4 and the virus envelope glycoprotein, gp120. Previous studies have localized the high affinity binding site for gp120 to the first domain of CD4, and monoclonal antibodies (mAbs) reactive with this region compete with gp120 binding and thereby block virus infectivity and syncytium formation. Despite a detailed understanding of the binding of gp120 to CD4, little is known of subsequent events leading to membrane fusion and virus entry. We describe two new mAbs reactive with the third domain of CD4 that inhibit steps subsequent to virus binding critical for HIV infectivity and cell fusion. Binding of recombinant gp120 or virus to CD4 is not inhibited by these antibodies, whereas infection and syncytium formation by a number of HIV isolates are blocked. These findings demonstrate that in addition to virus binding, CD4 may have an active role in membrane fusion.</abstract><cop>New York, NY</cop><pub>Rockefeller University Press</pub><pmid>1698911</pmid><doi>10.1084/jem.172.4.1233</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of experimental medicine, 1990-10, Vol.172 (4), p.1233-1242 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | AIDS/HIV Animals Antibodies, Monoclonal - immunology Binding Sites Biological and medical sciences CD4 Antigens - immunology CD4 Antigens - physiology CD4-Positive T-Lymphocytes - microbiology Cell Fusion Epitopes - analysis Fundamental and applied biological sciences. Psychology HIV Envelope Protein gp120 - metabolism HIV Infections - prevention & control Mice Mice, Inbred BALB C Microbiology Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Virology |
| title | Novel anti-CD4 monoclonal antibodies separate human immunodeficiency virus infection and fusion of CD4+ cells from virus binding |
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