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G J Gram1, J E Hansen

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The human immunodeficiency virus (HIV) envelope glycoprotein gp120 has numerous N-glycosylation sites, making up half its mass. This glycosylation is crucial for viral infection by facilitating binding to CD4 molecules.

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Area of Science:

  • Virology
  • Glycobiology
  • Immunology

Background:

  • The human immunodeficiency virus (HIV) causes AIDS.
  • HIV's envelope glycoprotein, gp120, is heavily glycosylated.
  • N-glycosylation sites are critical for viral structure and function.

Purpose of the Study:

  • To investigate the role of N-glycosylation in HIV gp120.
  • To understand the contribution of glycosylation to gp120's molecular mass.
  • To explore the significance of gp120 glycosylation in viral entry.

Main Methods:

  • Analysis of gp120 amino acid sequence for N-glycosylation sites (Asn-X-Ser/Thr, X≠Pro).
  • Quantification of glycosylation contribution to gp120 molecular mass.
  • Review of literature on gp120-CD4 binding and viral fusion.

Main Results:

  • Approximately 24 potential N-glycosylation sites were identified in gp120.
  • All identified sites are utilized, contributing to about 50% of gp120's molecular mass.
  • gp120 binding to CD4 is an essential early step in HIV infection.

Conclusions:

  • HIV gp120 is extensively N-glycosylated, impacting its structure and function.
  • Glycosylation plays a significant role in the initial stages of HIV infection, including CD4 binding and cell fusion.