Recognition of human immunodeficiency virus glycoproteins by natural anti-carbohydrate antibodies in human serum

Biochem Biophys Res Commun. 1991 May 31;177(1):279-85. doi: 10.1016/0006-291x(91)91979-m.

Abstract

Anti-carbohydrate antibodies were isolated from Human immunodeficiency virus (HIV) negative human serum by affinity chromatography using yeast mannan followed by protein A. The purified mannan-binding IgG (MBIgG) bound to HIV glycoproteins gp 160, gp 120 and gp 41 in Western blot. Immunofluorescence revealed that MBIgG bound to HIV/IIIB-infected H9 cells but not to uninfected H9 cells, suggesting that carbohydrate structures recognized by MBIgG are specifically expressed on HIV-infected cells. MBIgG did not neutralize infectivity of HIV. These results show that normal human serum contains natural antibodies reactive to carbohydrate structures of HIV glycoproteins propagated in human cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies / immunology*
  • Antibodies / isolation & purification
  • Blotting, Western
  • Cell Line
  • Fluorescent Antibody Technique
  • Gene Products, env / immunology*
  • HIV / immunology*
  • HIV Envelope Protein gp120 / immunology*
  • HIV Envelope Protein gp160
  • HIV Envelope Protein gp41 / immunology*
  • HIV Seropositivity
  • Humans
  • Immunoglobulin G / immunology*
  • Immunoglobulin G / isolation & purification
  • Mannans / immunology*
  • Protein Precursors / immunology*
  • Reference Values
  • Viral Envelope Proteins / analysis
  • Viral Envelope Proteins / immunology*

Substances

  • Antibodies
  • Gene Products, env
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp160
  • HIV Envelope Protein gp41
  • Immunoglobulin G
  • Mannans
  • Protein Precursors
  • Viral Envelope Proteins