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Conglutinin binds the HIV-1 envelope glycoprotein gp 160 and inhibits its interaction with cell membrane CD4
O Andersen1, A M Sørensen, S E Svehag
1Department of Medical Microbiology, Odense University, Denmark.
Insights
Bovine conglutinin, a C-type lectin, binds to the human immunodeficiency virus (HIV) envelope glycoprotein (gp160). This interaction may inhibit HIV-1 infection by blocking viral entry into CD4+ cells.
Area of Science:
- Virology
- Immunology
- Biochemistry
Background:
- The human immunodeficiency virus (HIV) envelope glycoprotein (gp160) mediates viral entry by binding to CD4 receptors on host cells.
- Lectins are proteins that bind carbohydrates, playing roles in cellular recognition and immune responses.
- Bovine conglutinin is a C-type lectin known to interact with glycoproteins.
Purpose of the Study:
- To investigate the interaction between bovine conglutinin and the HIV-1 envelope glycoprotein (gp160).
- To determine if bovine conglutinin can inhibit the binding of HIV-1 gp160 to the CD4 receptor.
Main Methods:
- Enzyme-linked immunosorbent assay (ELISA) was used to demonstrate specific binding between conglutinin and recombinant gp160 (rgp160).
- Flow cytometry (FACS) analysis was employed to assess the inhibition of rgp160-CD4 binding by conglutinin.
- The role of calcium ions and N-acetyl-D-glucosamine in the binding interaction was evaluated.
Main Results:
- Specific, calcium-dependent binding of bovine conglutinin to rgp160 was confirmed.
- Binding was inhibited by N-acetyl-D-glucosamine and abrogated by deglycosylation of rgp160.
- Conglutinin dose-dependently inhibited the binding of rgp160 to the CD4 receptor on CEM 13 cells.
Conclusions:
- Bovine conglutinin interacts with the HIV-1 envelope glycoprotein through its carbohydrate residues.
- Conglutinin's ability to inhibit rgp160-CD4 binding suggests a potential mechanism for blocking HIV-1 infection.
- These findings highlight bovine conglutinin as a potential therapeutic agent against HIV-1.
Abstract:
The highly glycosylated envelope glycoprotein (gp 160) of human immunodeficiency virus (HIV) interacts with the CD4 molecule present on the membrane of CD4+ cells and is involved in the pathobiology of HIV infection. Lectins bind glycoproteins through non-covalent interactions with specific hexose residues. The mammalian C-type lectin bovine conglutinin was examined for its ability to interact with recombinant gp160 (rgp160) produced in vaccinia virus-infected BHK21 cells. Specific binding of conglutinin to rgp160 was demonstrated by ELISA. The interaction of bovine conglutinin with rgp160 was calcium-dependent, which is characteristic of the binding of a C-type lectin to its ligand, and the binding was inhibited in a dose-dependent manner with N-acetyl-D-glucosamine. Deglycosylation of rgp160 abrogated the conglutinin binding. In addition, conglutinin exerted a dose-dependent inhibition of the binding of rgp160 to the CD4 receptor on CEM 13 cells, as demonstrated by FACS analyses. These results indicate that conglutinin may inhibit the infection with HIV-1 through its interaction with the viral envelope glycoprotein.
