The galactosyl ceramide/sulfatide receptor binding region of HIV-1 gp120 maps to amino acids 206-275
Our recent studies have indicated that galactosyl ceramide (GalCer) or sulfatide (sul) may serve as an alternate receptor for human immunodeficiency virus (HIV) in neural cells. In this paper, we describe the mapping of GalCer/sul binding region of HIV env glycoprotein gp120. Deglycosylated gp120 bi...
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| Veröffentlicht in: | AIDS research and human retroviruses 1993-02, Vol.9 (2), p.175-181 |
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| container_title | AIDS research and human retroviruses |
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| creator | SHAMA BHAT METTUS, R. V PREMKUMAR REDDY, E UGEN, K. E SRIKANTHAN, V WILLIAMS, W. V WEINER, D. B |
| description | Our recent studies have indicated that galactosyl ceramide (GalCer) or sulfatide (sul) may serve as an alternate receptor for human immunodeficiency virus (HIV) in neural cells. In this paper, we describe the mapping of GalCer/sul binding region of HIV env glycoprotein gp120. Deglycosylated gp120 binds to GalCer, suggesting that the amino acids of glycoprotein gp120 and not the carbohydrates are responsible for the observed binding. Specific regions of gp120 responsible for the binding were analyzed by using varying-length truncations of gp120 expressed in Escherichia coli and vaccinia virus. Purified recombinant gp120 containing amino acids 200-295 of gp120 bind to GalCer/sul, whereas recombinant env proteins that deleted this region did not bind. These recombinant proteins also bind to SK-N-MC-derived neuroblastoma cells, the binding of which is inhibited by anti-GalCer. In addition, 125I-labeled gp120 binding to GalCer is inhibited by these proteins. Studies using lysates containing truncated gp120 expressed in vaccinia virus also gave similar results. By eliminating the overlapping regions that do not bind, we conclude that the amino acids responsible for GalCer/sul binding reside between amino acids 206 and 275. The significance of this mapping is discussed in relation to the neurotropism of HIV. |
| doi_str_mv | 10.1089/aid.1993.9.175 |
| format | Article |
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V ; PREMKUMAR REDDY, E ; UGEN, K. E ; SRIKANTHAN, V ; WILLIAMS, W. V ; WEINER, D. B</creator><creatorcontrib>SHAMA BHAT ; METTUS, R. V ; PREMKUMAR REDDY, E ; UGEN, K. E ; SRIKANTHAN, V ; WILLIAMS, W. V ; WEINER, D. B</creatorcontrib><description>Our recent studies have indicated that galactosyl ceramide (GalCer) or sulfatide (sul) may serve as an alternate receptor for human immunodeficiency virus (HIV) in neural cells. In this paper, we describe the mapping of GalCer/sul binding region of HIV env glycoprotein gp120. Deglycosylated gp120 binds to GalCer, suggesting that the amino acids of glycoprotein gp120 and not the carbohydrates are responsible for the observed binding. Specific regions of gp120 responsible for the binding were analyzed by using varying-length truncations of gp120 expressed in Escherichia coli and vaccinia virus. Purified recombinant gp120 containing amino acids 200-295 of gp120 bind to GalCer/sul, whereas recombinant env proteins that deleted this region did not bind. These recombinant proteins also bind to SK-N-MC-derived neuroblastoma cells, the binding of which is inhibited by anti-GalCer. In addition, 125I-labeled gp120 binding to GalCer is inhibited by these proteins. Studies using lysates containing truncated gp120 expressed in vaccinia virus also gave similar results. By eliminating the overlapping regions that do not bind, we conclude that the amino acids responsible for GalCer/sul binding reside between amino acids 206 and 275. 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Psychology ; Galactosylceramides - metabolism ; Glycosylation ; HIV Envelope Protein gp120 - chemistry ; HIV Envelope Protein gp120 - genetics ; HIV Envelope Protein gp120 - metabolism ; HIV-1 - genetics ; HIV-1 - metabolism ; Humans ; Microbiology ; Molecular Sequence Data ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; Sulfoglycosphingolipids - metabolism ; Virology</subject><ispartof>AIDS research and human retroviruses, 1993-02, Vol.9 (2), p.175-181</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c319t-6869617fafebd3f5e677506d56daed4e380e71cad9a22734a6bb0ee6542686193</citedby><cites>FETCH-LOGICAL-c319t-6869617fafebd3f5e677506d56daed4e380e71cad9a22734a6bb0ee6542686193</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,3044,27931,27932</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4667586$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8457384$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SHAMA BHAT</creatorcontrib><creatorcontrib>METTUS, R. 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Specific regions of gp120 responsible for the binding were analyzed by using varying-length truncations of gp120 expressed in Escherichia coli and vaccinia virus. Purified recombinant gp120 containing amino acids 200-295 of gp120 bind to GalCer/sul, whereas recombinant env proteins that deleted this region did not bind. These recombinant proteins also bind to SK-N-MC-derived neuroblastoma cells, the binding of which is inhibited by anti-GalCer. In addition, 125I-labeled gp120 binding to GalCer is inhibited by these proteins. Studies using lysates containing truncated gp120 expressed in vaccinia virus also gave similar results. By eliminating the overlapping regions that do not bind, we conclude that the amino acids responsible for GalCer/sul binding reside between amino acids 206 and 275. The significance of this mapping is discussed in relation to the neurotropism of HIV.</description><subject>AIDS/HIV</subject><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Cells, Cultured</subject><subject>DNA, Viral - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactosylceramides - metabolism</subject><subject>Glycosylation</subject><subject>HIV Envelope Protein gp120 - chemistry</subject><subject>HIV Envelope Protein gp120 - genetics</subject><subject>HIV Envelope Protein gp120 - metabolism</subject><subject>HIV-1 - genetics</subject><subject>HIV-1 - metabolism</subject><subject>Humans</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>Sulfoglycosphingolipids - metabolism</subject><subject>Virology</subject><issn>0889-2229</issn><issn>1931-8405</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kDtvFTEQhS1EFC6Blg7JBaLbjd-PEkVAIkWiSWitWXv2YrQv7L1F_j2OcpVmZjRzzpHmI-QTZz1nzl9DTj33Xva-51a_IQfuJe-cYvotOTDnfCeE8O_I-1r_Msa8EPqSXDqlrXTqQNLDH6RHmCDua32aaMQCc054XU_TCHubaMGI274WOuQl5eXYFse8LnQd6e3d747T48YFozNsle4rbfal1ZhTpYKZTlj9gVyMMFX8eO5X5PHH94eb2-7-18-7m2_3XZTc751xxhtuRxhxSHLUaKzVzCRtEmBSKB1DyyMkD0JYqcAMA0M0WolmbX9fka8vuVtZ_52w7mHONeI0wYLrqQarjdRKqSbsX4SxrLUWHMNW8gzlKXAWnrGGhjU8Yw0-NKzN8PmcfBpmTK_yM8d2_3K-Q40wjQWWmOurTBljtTPyP0n2flY</recordid><startdate>19930201</startdate><enddate>19930201</enddate><creator>SHAMA BHAT</creator><creator>METTUS, R. 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Psychology</topic><topic>Galactosylceramides - metabolism</topic><topic>Glycosylation</topic><topic>HIV Envelope Protein gp120 - chemistry</topic><topic>HIV Envelope Protein gp120 - genetics</topic><topic>HIV Envelope Protein gp120 - metabolism</topic><topic>HIV-1 - genetics</topic><topic>HIV-1 - metabolism</topic><topic>Humans</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Sulfoglycosphingolipids - metabolism</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SHAMA BHAT</creatorcontrib><creatorcontrib>METTUS, R. V</creatorcontrib><creatorcontrib>PREMKUMAR REDDY, E</creatorcontrib><creatorcontrib>UGEN, K. E</creatorcontrib><creatorcontrib>SRIKANTHAN, V</creatorcontrib><creatorcontrib>WILLIAMS, W. V</creatorcontrib><creatorcontrib>WEINER, D. B</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>AIDS research and human retroviruses</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SHAMA BHAT</au><au>METTUS, R. V</au><au>PREMKUMAR REDDY, E</au><au>UGEN, K. E</au><au>SRIKANTHAN, V</au><au>WILLIAMS, W. V</au><au>WEINER, D. B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The galactosyl ceramide/sulfatide receptor binding region of HIV-1 gp120 maps to amino acids 206-275</atitle><jtitle>AIDS research and human retroviruses</jtitle><addtitle>AIDS Res Hum Retroviruses</addtitle><date>1993-02-01</date><risdate>1993</risdate><volume>9</volume><issue>2</issue><spage>175</spage><epage>181</epage><pages>175-181</pages><issn>0889-2229</issn><eissn>1931-8405</eissn><coden>ARHRE7</coden><abstract>Our recent studies have indicated that galactosyl ceramide (GalCer) or sulfatide (sul) may serve as an alternate receptor for human immunodeficiency virus (HIV) in neural cells. In this paper, we describe the mapping of GalCer/sul binding region of HIV env glycoprotein gp120. Deglycosylated gp120 binds to GalCer, suggesting that the amino acids of glycoprotein gp120 and not the carbohydrates are responsible for the observed binding. Specific regions of gp120 responsible for the binding were analyzed by using varying-length truncations of gp120 expressed in Escherichia coli and vaccinia virus. Purified recombinant gp120 containing amino acids 200-295 of gp120 bind to GalCer/sul, whereas recombinant env proteins that deleted this region did not bind. These recombinant proteins also bind to SK-N-MC-derived neuroblastoma cells, the binding of which is inhibited by anti-GalCer. In addition, 125I-labeled gp120 binding to GalCer is inhibited by these proteins. Studies using lysates containing truncated gp120 expressed in vaccinia virus also gave similar results. By eliminating the overlapping regions that do not bind, we conclude that the amino acids responsible for GalCer/sul binding reside between amino acids 206 and 275. 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| source | Mary Ann Liebert Online Subscription; MEDLINE |
| subjects | AIDS/HIV Amino Acid Sequence Base Sequence Binding Sites Biological and medical sciences Cells, Cultured DNA, Viral - genetics Fundamental and applied biological sciences. Psychology Galactosylceramides - metabolism Glycosylation HIV Envelope Protein gp120 - chemistry HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp120 - metabolism HIV-1 - genetics HIV-1 - metabolism Humans Microbiology Molecular Sequence Data Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Sulfoglycosphingolipids - metabolism Virology |
| title | The galactosyl ceramide/sulfatide receptor binding region of HIV-1 gp120 maps to amino acids 206-275 |
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