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Molecular Pharmacology

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Research ArticleORIGINAL ARTICLE

Marked Depletion of Glycosylation Sites in HIV-1 gp120 under Selection Pressure by the Mannose-Specific Plant Lectins of Hippeastrum Hybrid and Galanthus nivalis

Jan Balzarini, Kristel Van Laethem, Sigrid Hatse, Matheus Froeyen, Els Van Damme, Anders Bolmstedt, Willy Peumans, Erik De Clercq and Dominique Schols
Molecular Pharmacology May 2005, 67 (5) 1556-1565; DOI: https://doi.org/10.1124/mol.104.005082
Jan Balzarini
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Kristel Van Laethem
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Sigrid Hatse
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Matheus Froeyen
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Els Van Damme
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Anders Bolmstedt
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Willy Peumans
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Erik De Clercq
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Dominique Schols
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Abstract

The plant lectins from Hippeastrum hybrid (HHA) and Galanthus nivalis (GNA) are 50,000-D tetramers showing specificity for α-(1,3) and/or α-(1,6)-mannose oligomers. They inhibit HIV-1 infection at a 50% effective concentration of 0.2 to 0.3 μg/ml. Escalating HHA or GNA concentrations (up to 500 μg/ml) led to the isolation of three HIV-1(IIIB) strains in CEM T cell cultures that were highly resistant to HHA and GNA, several other related mannose-specific plant lectins, and the monoclonal antibody 2G12, modestly resistant to the mannose-specific cyanovirin, which is derived from a blue-green alga, but fully susceptible to other HIV entry inhibitors as well as HIV reverse transcriptase inhibitors. These mutant virus strains were devoid of up to seven or eight of 22 glycosylation sites in the viral envelope glycoprotein gp120 because of mutations at the Asn or Thr/Ser sites of the N-glycosylation motifs. In one of the strains, a novel glycosylation site was created near a deleted glycosylation site. The affected glycosylation sites were predominantly clustered in regions of gp120 that are not involved in the direct interaction with either CD4, CCR5, CXCR4, or gp41. The mutant viruses containing the deleted glycosylation sites were markedly more infectious in CEM T-cell cultures than wild-type virus.

  • Received July 16, 2004.
  • Accepted February 17, 2005.
  • The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 67 (5)
Molecular Pharmacology
Vol. 67, Issue 5
1 May 2005
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Research ArticleORIGINAL ARTICLE

Marked Depletion of Glycosylation Sites in HIV-1 gp120 under Selection Pressure by the Mannose-Specific Plant Lectins of Hippeastrum Hybrid and Galanthus nivalis

Jan Balzarini, Kristel Van Laethem, Sigrid Hatse, Matheus Froeyen, Els Van Damme, Anders Bolmstedt, Willy Peumans, Erik De Clercq and Dominique Schols
Molecular Pharmacology May 1, 2005, 67 (5) 1556-1565; DOI: https://doi.org/10.1124/mol.104.005082

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Research ArticleORIGINAL ARTICLE

Marked Depletion of Glycosylation Sites in HIV-1 gp120 under Selection Pressure by the Mannose-Specific Plant Lectins of Hippeastrum Hybrid and Galanthus nivalis

Jan Balzarini, Kristel Van Laethem, Sigrid Hatse, Matheus Froeyen, Els Van Damme, Anders Bolmstedt, Willy Peumans, Erik De Clercq and Dominique Schols
Molecular Pharmacology May 1, 2005, 67 (5) 1556-1565; DOI: https://doi.org/10.1124/mol.104.005082
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