author_facet Puri, Anu
Hug, Peter
Jernigan, Kristine
Barchi, Joseph
Kim, Hee-Yong
Hamilton, Jillon
Wiels, Joëlle
Murray, Gary J.
Brady, Roscoe O.
Blumenthal, Robert
Puri, Anu
Hug, Peter
Jernigan, Kristine
Barchi, Joseph
Kim, Hee-Yong
Hamilton, Jillon
Wiels, Joëlle
Murray, Gary J.
Brady, Roscoe O.
Blumenthal, Robert
author Puri, Anu
Hug, Peter
Jernigan, Kristine
Barchi, Joseph
Kim, Hee-Yong
Hamilton, Jillon
Wiels, Joëlle
Murray, Gary J.
Brady, Roscoe O.
Blumenthal, Robert
spellingShingle Puri, Anu
Hug, Peter
Jernigan, Kristine
Barchi, Joseph
Kim, Hee-Yong
Hamilton, Jillon
Wiels, Joëlle
Murray, Gary J.
Brady, Roscoe O.
Blumenthal, Robert
Proceedings of the National Academy of Sciences
The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
Multidisciplinary
author_sort puri, anu
spelling Puri, Anu Hug, Peter Jernigan, Kristine Barchi, Joseph Kim, Hee-Yong Hamilton, Jillon Wiels, Joëlle Murray, Gary J. Brady, Roscoe O. Blumenthal, Robert 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.95.24.14435 <jats:p>Previously, we showed that the addition of human erythrocyte glycosphingolipids (GSLs) to nonhuman CD4<jats:sup>+</jats:sup>or GSL-depleted human CD4<jats:sup>+</jats:sup>cells rendered those cells susceptible to HIV-1 envelope glycoprotein-mediated cell fusion. Individual components in the GSL mixture were isolated by fractionation on a silica-gel column and incorporated into the membranes of CD4<jats:sup>+</jats:sup>cells. GSL-supplemented target cells were then examined for their ability to fuse with TF228 cells expressing HIV-1<jats:sub>LAI</jats:sub>envelope glycoprotein. We found that one GSL fraction, fraction 3, exhibited the highest recovery of fusion after incorporation into CD4<jats:sup>+</jats:sup>nonhuman and GSL-depleted HeLa-CD4 cells and that fraction 3 contained a single GSL fraction. Fraction 3 was characterized by MS, NMR spectroscopy, enzymatic analysis, and immunostaining with an antiglobotriaosylceramide (Gb3) antibody and was found to be Gal(α1→4)Gal(β1→4)Glc-Cer (Gb3). The addition of fraction 3 or Gb3 to GSL-depleted HeLa-CD4 cells recovered fusion, but the addition of galactosylceramide, glucosylceramide, the monosialoganglioside, GM3, lactosylceramide, globoside, the disialoganglioside, GD3, or α-galactosidase A-digested fraction 3 had no effect. Our findings show that the neutral GSL, Gb3, is required for CD4/CXCR4-dependent HIV-1 fusion.</jats:p> The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein Proceedings of the National Academy of Sciences
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title The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_unstemmed The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_full The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_fullStr The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_full_unstemmed The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_short The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_sort the neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a cd4-dependent cxcr4-utilizing hiv type 1 envelope glycoprotein
topic Multidisciplinary
url http://dx.doi.org/10.1073/pnas.95.24.14435
publishDate 1998
physical 14435-14440
description <jats:p>Previously, we showed that the addition of human erythrocyte glycosphingolipids (GSLs) to nonhuman CD4<jats:sup>+</jats:sup>or GSL-depleted human CD4<jats:sup>+</jats:sup>cells rendered those cells susceptible to HIV-1 envelope glycoprotein-mediated cell fusion. Individual components in the GSL mixture were isolated by fractionation on a silica-gel column and incorporated into the membranes of CD4<jats:sup>+</jats:sup>cells. GSL-supplemented target cells were then examined for their ability to fuse with TF228 cells expressing HIV-1<jats:sub>LAI</jats:sub>envelope glycoprotein. We found that one GSL fraction, fraction 3, exhibited the highest recovery of fusion after incorporation into CD4<jats:sup>+</jats:sup>nonhuman and GSL-depleted HeLa-CD4 cells and that fraction 3 contained a single GSL fraction. Fraction 3 was characterized by MS, NMR spectroscopy, enzymatic analysis, and immunostaining with an antiglobotriaosylceramide (Gb3) antibody and was found to be Gal(α1→4)Gal(β1→4)Glc-Cer (Gb3). The addition of fraction 3 or Gb3 to GSL-depleted HeLa-CD4 cells recovered fusion, but the addition of galactosylceramide, glucosylceramide, the monosialoganglioside, GM3, lactosylceramide, globoside, the disialoganglioside, GD3, or α-galactosidase A-digested fraction 3 had no effect. Our findings show that the neutral GSL, Gb3, is required for CD4/CXCR4-dependent HIV-1 fusion.</jats:p>
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author Puri, Anu, Hug, Peter, Jernigan, Kristine, Barchi, Joseph, Kim, Hee-Yong, Hamilton, Jillon, Wiels, Joëlle, Murray, Gary J., Brady, Roscoe O., Blumenthal, Robert
author_facet Puri, Anu, Hug, Peter, Jernigan, Kristine, Barchi, Joseph, Kim, Hee-Yong, Hamilton, Jillon, Wiels, Joëlle, Murray, Gary J., Brady, Roscoe O., Blumenthal, Robert, Puri, Anu, Hug, Peter, Jernigan, Kristine, Barchi, Joseph, Kim, Hee-Yong, Hamilton, Jillon, Wiels, Joëlle, Murray, Gary J., Brady, Roscoe O., Blumenthal, Robert
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container_issue 24
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container_title Proceedings of the National Academy of Sciences
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description <jats:p>Previously, we showed that the addition of human erythrocyte glycosphingolipids (GSLs) to nonhuman CD4<jats:sup>+</jats:sup>or GSL-depleted human CD4<jats:sup>+</jats:sup>cells rendered those cells susceptible to HIV-1 envelope glycoprotein-mediated cell fusion. Individual components in the GSL mixture were isolated by fractionation on a silica-gel column and incorporated into the membranes of CD4<jats:sup>+</jats:sup>cells. GSL-supplemented target cells were then examined for their ability to fuse with TF228 cells expressing HIV-1<jats:sub>LAI</jats:sub>envelope glycoprotein. We found that one GSL fraction, fraction 3, exhibited the highest recovery of fusion after incorporation into CD4<jats:sup>+</jats:sup>nonhuman and GSL-depleted HeLa-CD4 cells and that fraction 3 contained a single GSL fraction. Fraction 3 was characterized by MS, NMR spectroscopy, enzymatic analysis, and immunostaining with an antiglobotriaosylceramide (Gb3) antibody and was found to be Gal(α1→4)Gal(β1→4)Glc-Cer (Gb3). The addition of fraction 3 or Gb3 to GSL-depleted HeLa-CD4 cells recovered fusion, but the addition of galactosylceramide, glucosylceramide, the monosialoganglioside, GM3, lactosylceramide, globoside, the disialoganglioside, GD3, or α-galactosidase A-digested fraction 3 had no effect. Our findings show that the neutral GSL, Gb3, is required for CD4/CXCR4-dependent HIV-1 fusion.</jats:p>
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imprint Proceedings of the National Academy of Sciences, 1998
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spelling Puri, Anu Hug, Peter Jernigan, Kristine Barchi, Joseph Kim, Hee-Yong Hamilton, Jillon Wiels, Joëlle Murray, Gary J. Brady, Roscoe O. Blumenthal, Robert 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.95.24.14435 <jats:p>Previously, we showed that the addition of human erythrocyte glycosphingolipids (GSLs) to nonhuman CD4<jats:sup>+</jats:sup>or GSL-depleted human CD4<jats:sup>+</jats:sup>cells rendered those cells susceptible to HIV-1 envelope glycoprotein-mediated cell fusion. Individual components in the GSL mixture were isolated by fractionation on a silica-gel column and incorporated into the membranes of CD4<jats:sup>+</jats:sup>cells. GSL-supplemented target cells were then examined for their ability to fuse with TF228 cells expressing HIV-1<jats:sub>LAI</jats:sub>envelope glycoprotein. We found that one GSL fraction, fraction 3, exhibited the highest recovery of fusion after incorporation into CD4<jats:sup>+</jats:sup>nonhuman and GSL-depleted HeLa-CD4 cells and that fraction 3 contained a single GSL fraction. Fraction 3 was characterized by MS, NMR spectroscopy, enzymatic analysis, and immunostaining with an antiglobotriaosylceramide (Gb3) antibody and was found to be Gal(α1→4)Gal(β1→4)Glc-Cer (Gb3). The addition of fraction 3 or Gb3 to GSL-depleted HeLa-CD4 cells recovered fusion, but the addition of galactosylceramide, glucosylceramide, the monosialoganglioside, GM3, lactosylceramide, globoside, the disialoganglioside, GD3, or α-galactosidase A-digested fraction 3 had no effect. Our findings show that the neutral GSL, Gb3, is required for CD4/CXCR4-dependent HIV-1 fusion.</jats:p> The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein Proceedings of the National Academy of Sciences
spellingShingle Puri, Anu, Hug, Peter, Jernigan, Kristine, Barchi, Joseph, Kim, Hee-Yong, Hamilton, Jillon, Wiels, Joëlle, Murray, Gary J., Brady, Roscoe O., Blumenthal, Robert, Proceedings of the National Academy of Sciences, The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein, Multidisciplinary
title The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_full The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_fullStr The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_full_unstemmed The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_short The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
title_sort the neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a cd4-dependent cxcr4-utilizing hiv type 1 envelope glycoprotein
title_unstemmed The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
topic Multidisciplinary
url http://dx.doi.org/10.1073/pnas.95.24.14435