Development of Resistance of Human Immunodeficiency Virus Type 1 to Dextran Sulfate Associated with the Emergence of Specific Mutations in the Envelope gp120 Glycoprotein
Polyanionic compounds are known to inhibit the binding of human immunodeficiency virus (HIV) to CD4 + cells and the subsequent fusion step between the virus and cells. We selected an HIV-1 strain resistant to dextran sulfate (DS) by cultivation of HIV-1 (NL4â3)-infected MT-4 cells in the presence...
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| Veröffentlicht in: | Molecular pharmacology 1997-07, Vol.52 (1), p.98-104 |
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| creator | Este, J A Schols, D De Vreese, K Van Laethem, K Vandamme, A M Desmyter, J De Clercq, E |
| description | Polyanionic compounds are known to inhibit the binding of human immunodeficiency virus (HIV) to CD4 + cells and the subsequent fusion step between the virus and cells. We selected an HIV-1 strain resistant to dextran sulfate
(DS) by cultivation of HIV-1 (NL4â3)-infected MT-4 cells in the presence of DS M
r 5000. DS did not inhibit the binding of DS-resistant virus to MT-4 cells or syncytium formation between MOLT cells and HUT-78
cells persistently infected with the DS-resistant virus. In addition, a monoclonal antibody with specificity for the V3 loop
of envelope gp120 glycoprotein did not recognize the DS-resistant HIV-1 gp120 V3 loop. The following mutations were found
in the gp120 molecule of the DS-resistant HIV-1 strain but not in the wild-type strain: S114N in the V1 loop region; S134N
in the V2 loop region; K269E, Q278H, and N293D in the V3 loop region; N323S in the C3 region; a deletion of five amino acids
(Phe-Asn-Ser-Thr-Trp) at positions 364â368 in the V4 loop; and R387I in the CD4 binding domain. Our results suggest that (i)
DS interacts with specific amino acid residues in the gp120 molecule, (ii) the virus is able to overcome the inhibitory effect
of DS on viral infectivity, (iii) cross-resistance developed against those polyanionic compounds that are structurally related
to DS, and (iv) the molecular determinants of HIV cell tropism, syncytium-inducing ability, coreceptor (fusin/CC-CKR5) utilization,
and polyanion resistance seem to be located in the env genome of HIV and specifically in the V3 loop domain. |
| doi_str_mv | 10.1124/mol.52.1.98 |
| format | Article |
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(DS) by cultivation of HIV-1 (NL4â3)-infected MT-4 cells in the presence of DS M
r 5000. DS did not inhibit the binding of DS-resistant virus to MT-4 cells or syncytium formation between MOLT cells and HUT-78
cells persistently infected with the DS-resistant virus. In addition, a monoclonal antibody with specificity for the V3 loop
of envelope gp120 glycoprotein did not recognize the DS-resistant HIV-1 gp120 V3 loop. The following mutations were found
in the gp120 molecule of the DS-resistant HIV-1 strain but not in the wild-type strain: S114N in the V1 loop region; S134N
in the V2 loop region; K269E, Q278H, and N293D in the V3 loop region; N323S in the C3 region; a deletion of five amino acids
(Phe-Asn-Ser-Thr-Trp) at positions 364â368 in the V4 loop; and R387I in the CD4 binding domain. Our results suggest that (i)
DS interacts with specific amino acid residues in the gp120 molecule, (ii) the virus is able to overcome the inhibitory effect
of DS on viral infectivity, (iii) cross-resistance developed against those polyanionic compounds that are structurally related
to DS, and (iv) the molecular determinants of HIV cell tropism, syncytium-inducing ability, coreceptor (fusin/CC-CKR5) utilization,
and polyanion resistance seem to be located in the env genome of HIV and specifically in the V3 loop domain.</description><identifier>ISSN: 0026-895X</identifier><identifier>EISSN: 1521-0111</identifier><identifier>DOI: 10.1124/mol.52.1.98</identifier><identifier>PMID: 9224818</identifier><language>eng</language><publisher>United States: American Society for Pharmacology and Experimental Therapeutics</publisher><subject>AIDS/HIV ; Amino Acid Sequence ; Anti-HIV Agents - pharmacology ; Base Sequence ; Dextran Sulfate - pharmacology ; Drug Resistance ; Fluorescent Antibody Technique ; Genes, env ; HIV Envelope Protein gp120 - drug effects ; HIV Envelope Protein gp120 - genetics ; HIV-1 - drug effects ; human immunodeficiency virus 1 ; Humans ; Molecular Sequence Data ; Mutation</subject><ispartof>Molecular pharmacology, 1997-07, Vol.52 (1), p.98-104</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c344t-c8cd8c649c3d03773ba29ae016d7b5c7adf678f7edc09645b9e5ba631c358b903</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9224818$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Este, J A</creatorcontrib><creatorcontrib>Schols, D</creatorcontrib><creatorcontrib>De Vreese, K</creatorcontrib><creatorcontrib>Van Laethem, K</creatorcontrib><creatorcontrib>Vandamme, A M</creatorcontrib><creatorcontrib>Desmyter, J</creatorcontrib><creatorcontrib>De Clercq, E</creatorcontrib><title>Development of Resistance of Human Immunodeficiency Virus Type 1 to Dextran Sulfate Associated with the Emergence of Specific Mutations in the Envelope gp120 Glycoprotein</title><title>Molecular pharmacology</title><addtitle>Mol Pharmacol</addtitle><description>Polyanionic compounds are known to inhibit the binding of human immunodeficiency virus (HIV) to CD4 + cells and the subsequent fusion step between the virus and cells. We selected an HIV-1 strain resistant to dextran sulfate
(DS) by cultivation of HIV-1 (NL4â3)-infected MT-4 cells in the presence of DS M
r 5000. DS did not inhibit the binding of DS-resistant virus to MT-4 cells or syncytium formation between MOLT cells and HUT-78
cells persistently infected with the DS-resistant virus. In addition, a monoclonal antibody with specificity for the V3 loop
of envelope gp120 glycoprotein did not recognize the DS-resistant HIV-1 gp120 V3 loop. The following mutations were found
in the gp120 molecule of the DS-resistant HIV-1 strain but not in the wild-type strain: S114N in the V1 loop region; S134N
in the V2 loop region; K269E, Q278H, and N293D in the V3 loop region; N323S in the C3 region; a deletion of five amino acids
(Phe-Asn-Ser-Thr-Trp) at positions 364â368 in the V4 loop; and R387I in the CD4 binding domain. Our results suggest that (i)
DS interacts with specific amino acid residues in the gp120 molecule, (ii) the virus is able to overcome the inhibitory effect
of DS on viral infectivity, (iii) cross-resistance developed against those polyanionic compounds that are structurally related
to DS, and (iv) the molecular determinants of HIV cell tropism, syncytium-inducing ability, coreceptor (fusin/CC-CKR5) utilization,
and polyanion resistance seem to be located in the env genome of HIV and specifically in the V3 loop domain.</description><subject>AIDS/HIV</subject><subject>Amino Acid Sequence</subject><subject>Anti-HIV Agents - pharmacology</subject><subject>Base Sequence</subject><subject>Dextran Sulfate - pharmacology</subject><subject>Drug Resistance</subject><subject>Fluorescent Antibody Technique</subject><subject>Genes, env</subject><subject>HIV Envelope Protein gp120 - drug effects</subject><subject>HIV Envelope Protein gp120 - genetics</subject><subject>HIV-1 - drug effects</subject><subject>human immunodeficiency virus 1</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><issn>0026-895X</issn><issn>1521-0111</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EKkvhxBnJB8QFZfHk0z5WbWkrFSHRgrhZjjPZGMV2sB1K_hK_kiy76pXTzGgePTPSS8hrYFuAvPxg_bit8i1sBX9CNlDlkDEAeEo2jOV1xkX1_Tl5EeMPxqCsODshJyLPSw58Q_5c4C8c_WTRJep7-gWjiUk5jfvperbK0RtrZ-c77I026PRCv5kwR3q_TEiBJk8v8HcKK3g3j71KSM9i9NqsXUcfTBpoGpBeWgw7PHrvJtRm1dFPc1LJeBepcQfM_XsH6W6CnNGrcdF-Cj6hcS_Js16NEV8d6yn5-vHy_vw6u_18dXN-dpvpoixTprnuuK5LoYuOFU1TtCoXChnUXdNWulFdXze8b7DTTNRl1QqsWlUXoIuKt4IVp-Tdwbve_TljTNKaqHEclUM_R9kIKFas_i8INeP1emsF3x9AHXyMAXs5BWNVWCQwuY9QrhHKKpcgxZ5-c9TOrcXukT1mtu7fHvaD2Q0PJqCcBhWs0n70u-VR8xcK56ca</recordid><startdate>19970701</startdate><enddate>19970701</enddate><creator>Este, J A</creator><creator>Schols, D</creator><creator>De Vreese, K</creator><creator>Van Laethem, K</creator><creator>Vandamme, A M</creator><creator>Desmyter, J</creator><creator>De Clercq, E</creator><general>American Society for Pharmacology and Experimental Therapeutics</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></search><sort><creationdate>19970701</creationdate><title>Development of Resistance of Human Immunodeficiency Virus Type 1 to Dextran Sulfate Associated with the Emergence of Specific Mutations in the Envelope gp120 Glycoprotein</title><author>Este, J A ; Schols, D ; De Vreese, K ; Van Laethem, K ; Vandamme, A M ; Desmyter, J ; De Clercq, E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c344t-c8cd8c649c3d03773ba29ae016d7b5c7adf678f7edc09645b9e5ba631c358b903</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>AIDS/HIV</topic><topic>Amino Acid Sequence</topic><topic>Anti-HIV Agents - pharmacology</topic><topic>Base Sequence</topic><topic>Dextran Sulfate - pharmacology</topic><topic>Drug Resistance</topic><topic>Fluorescent Antibody Technique</topic><topic>Genes, env</topic><topic>HIV Envelope Protein gp120 - drug effects</topic><topic>HIV Envelope Protein gp120 - genetics</topic><topic>HIV-1 - drug effects</topic><topic>human immunodeficiency virus 1</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Este, J A</creatorcontrib><creatorcontrib>Schols, D</creatorcontrib><creatorcontrib>De Vreese, K</creatorcontrib><creatorcontrib>Van Laethem, K</creatorcontrib><creatorcontrib>Vandamme, A M</creatorcontrib><creatorcontrib>Desmyter, J</creatorcontrib><creatorcontrib>De Clercq, E</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><jtitle>Molecular pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Este, J A</au><au>Schols, D</au><au>De Vreese, K</au><au>Van Laethem, K</au><au>Vandamme, A M</au><au>Desmyter, J</au><au>De Clercq, E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Development of Resistance of Human Immunodeficiency Virus Type 1 to Dextran Sulfate Associated with the Emergence of Specific Mutations in the Envelope gp120 Glycoprotein</atitle><jtitle>Molecular pharmacology</jtitle><addtitle>Mol Pharmacol</addtitle><date>1997-07-01</date><risdate>1997</risdate><volume>52</volume><issue>1</issue><spage>98</spage><epage>104</epage><pages>98-104</pages><issn>0026-895X</issn><eissn>1521-0111</eissn><abstract>Polyanionic compounds are known to inhibit the binding of human immunodeficiency virus (HIV) to CD4 + cells and the subsequent fusion step between the virus and cells. We selected an HIV-1 strain resistant to dextran sulfate
(DS) by cultivation of HIV-1 (NL4â3)-infected MT-4 cells in the presence of DS M
r 5000. DS did not inhibit the binding of DS-resistant virus to MT-4 cells or syncytium formation between MOLT cells and HUT-78
cells persistently infected with the DS-resistant virus. In addition, a monoclonal antibody with specificity for the V3 loop
of envelope gp120 glycoprotein did not recognize the DS-resistant HIV-1 gp120 V3 loop. The following mutations were found
in the gp120 molecule of the DS-resistant HIV-1 strain but not in the wild-type strain: S114N in the V1 loop region; S134N
in the V2 loop region; K269E, Q278H, and N293D in the V3 loop region; N323S in the C3 region; a deletion of five amino acids
(Phe-Asn-Ser-Thr-Trp) at positions 364â368 in the V4 loop; and R387I in the CD4 binding domain. Our results suggest that (i)
DS interacts with specific amino acid residues in the gp120 molecule, (ii) the virus is able to overcome the inhibitory effect
of DS on viral infectivity, (iii) cross-resistance developed against those polyanionic compounds that are structurally related
to DS, and (iv) the molecular determinants of HIV cell tropism, syncytium-inducing ability, coreceptor (fusin/CC-CKR5) utilization,
and polyanion resistance seem to be located in the env genome of HIV and specifically in the V3 loop domain.</abstract><cop>United States</cop><pub>American Society for Pharmacology and Experimental Therapeutics</pub><pmid>9224818</pmid><doi>10.1124/mol.52.1.98</doi><tpages>7</tpages></addata></record> |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | AIDS/HIV Amino Acid Sequence Anti-HIV Agents - pharmacology Base Sequence Dextran Sulfate - pharmacology Drug Resistance Fluorescent Antibody Technique Genes, env HIV Envelope Protein gp120 - drug effects HIV Envelope Protein gp120 - genetics HIV-1 - drug effects human immunodeficiency virus 1 Humans Molecular Sequence Data Mutation |
| title | Development of Resistance of Human Immunodeficiency Virus Type 1 to Dextran Sulfate Associated with the Emergence of Specific Mutations in the Envelope gp120 Glycoprotein |
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