Identification of an N-linked glycan in the V1-loop of HIV-1 gp120 influencing neutralization by anti-V3 antibodies and soluble CD4
Autor: | John-Erik Stig Hansen, Britt Jansson, Anna Hemming, Lennart Åkerblom, Gregers J. Gram, S. Olofsson, Anders Bolmstedt, J. O. Nielsen |
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Rok vydání: | 1994 |
Předmět: |
Glycan
Glycosylation Cell Survival HIV Antigens Protein Conformation medicine.drug_class viruses Molecular Sequence Data HIV Antibodies HIV Envelope Protein gp120 Biology Monoclonal antibody Neutralization Cell Line chemistry.chemical_compound Viral envelope N-linked glycosylation Neutralization Tests Polysaccharides Virology Concanavalin A medicine Humans Amino Acid Sequence chemistry.chemical_classification Infectivity Base Sequence Antibodies Monoclonal virus diseases General Medicine Molecular biology Peptide Fragments Recombinant Proteins carbohydrates (lipids) chemistry Mutagenesis CD4 Antigens HIV-1 biology.protein Glycoprotein |
Zdroj: | Archives of Virology. 139:253-261 |
ISSN: | 1432-8798 0304-8608 |
Popis: | Glycosylation is necessary for HIV-1 gp120 to attain a functional conformation, and individual N-linked glycans of gp120 are important, but not essential, for replication of HIV-1 in cell culture. We have constructed a mutant HIV-1 infectious clone lacking a signal for N-linked glycosylation in the V1-loop of HIV-1 gp120. Lack of an N-linked glycan was verified by a mobility enhancement of mutant gp120 in SDS-gel electrophoresis. The mutated virus showed no differences in either gp120 content per infectious unit or infectivity, indicating that the N-linked glycan was neither essential nor affecting viral infectivity in cell culture. We found that the mutated virus lacking an N-linked glycan in the V1-loop of gp120 was more resistant to neutralization by monoclonal antibodies to the V3-loop and neutralization by soluble recombinant CD4 (sCD4). Both viruses were equally well neutralized by ConA and a conformation dependent human antibody IAM-2G12. This suggests that the N-linked glycan in the V1-loop modulates the three-dimensional conformation of gp120, without changing the overall functional integrity of the molecule. |
Databáze: | OpenAIRE |
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