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Conglutinin Binds The HIV‐1 Envelope Glycoprotein gpl60 and Inhibits its Interaction with Cell Membrane CD4
Author(s) -
ANDERSEN O.,
SØRENSEN A.M.,
SVEHAG S.E.,
FENOUILLET E.
Publication year - 1991
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1991.tb02494.x
Subject(s) - glycoprotein , biology , viral envelope , lectin , membrane glycoproteins , c type lectin , biochemistry , microbiology and biotechnology , binding site
The highly glycosylated envelope glycoprotein (gpl60) 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 gpl60 (rgpl60) 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 A‐acetyl‐D‐glucosamine. Deglycosylation of rgpl60 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.