New insight in the interaction between the gp120 and the HIV receptor in human sperms

The human immunodeficiency virus (HIV) can infect some cell types which lack CD4. Galactosylceramide, a glycolipid present in the nervous system and colonic epithelial cells, has been implicated in the virus entry in these cells. Our data demonstrate that the HIV surface glycoprotein gp120 binds to the galactosyl-alkyl-acylglycerol (GalAAG), a glycolipid structurally related to galactosylceramide present on the surface membrane of the spermatozoa. In this paper, we review our previous data and further confirm the specificity of the interaction between this galactoglycerolipid and the gp120. Consistent with the structural similarity to galactosylceramide, the sperm GalAAG is capable of specifically binding the gp120. The specificity of the binding of antibodies antigalactosylceramide and the gp120 to the sperm extract and to the purified GalAAG fraction prepared from the same extract has been demonstrated utilizing an ELISA assay which favors sensitivity and specificity. Immunofluorescence and immunoelectron microscopy data show a different localization for the GalAAG and its sulfated form the seminolipid (SGalAAG). The GalAAG is preferentially localized in the equatorial segment and the middle piece of the sperm tail, while the seminolipid is widely distributed on the membrane of the spermatozoa. These data indicate that human sperm express on their surface membrane a glycolipid similar in structure to galactosylceramide, the receptor for HIV identified in the CD4 cells, that could function as a HIV receptor and possibly be implicated in its transmission.