Loss of N-linked glycans in the V3-loop region of gp120 is correlated to an enhanced infectivity of HIV-1

We describe mutants of human immunodeficiency virus type-1 (HIV-1) strain NL4-3, which are lacking the thirteenth, fifteenth, or seventeenth sites for N-linked glycosylation (g13, g15, g17) of the envelope protein gp120. All three sites are located within the hypervariable V3 loop region of gp120. T...

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Bibliographic Details
Published in:Glycobiology (Oxford) 2001-01, Vol.11 (1), p.11-19
Main Authors: Polzer, S, Dittmar, M T, Schmitz, H, Meyer, B, Müller, H, Kräusslich, H G, Schreiber, M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
DNA Primers
Glycosylation
HeLa Cells
HIV Envelope Protein gp120 - chemistry
HIV Envelope Protein gp120 - genetics
HIV-1 - pathogenicity
Human immunodeficiency virus 1
Humans
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Peptide Fragments - chemistry
Peptide Fragments - genetics
Polysaccharides - chemistry
Tumor Cells, Cultured
Virulence - genetics
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Summary:We describe mutants of human immunodeficiency virus type-1 (HIV-1) strain NL4-3, which are lacking the thirteenth, fifteenth, or seventeenth sites for N-linked glycosylation (g13, g15, g17) of the envelope protein gp120. All three sites are located within the hypervariable V3 loop region of gp120. Those mutants lacking carbohydrates g15 or combinations of g15/g17 showed markedly higher infectivity for GHOST cells (human osteosarcoma cells) expressing CXCR4 (GHOST-X4), compared to the fully glycosylated NL4-3 wild type virus. In addition, these mutants could also infect cells which exhibits low background expression of CXCR4, corresponding to
ISSN:0959-6658
1460-2423
DOI:10.1093/glycob/11.1.11