ABSTRACT
The expression of a molecule recognized by anti-galactosyl ceramide antibodies (MAb) O1 on the surface membrane of human spermatozoa was investigated by biochemical and immunochemical methods. Indirect immunofluorescence shows that this molecule is preferentially localized on the middle piece of the sperm tail. Immuno-thin-layer chromatography has identified it as a glycolipid related but not identical to galactosylceramide. Consistent with a structure similar to galactosylceramide, the sperm glycolipid is capable of binding gp120. An improved ELISA has been utilized to demonstrate the specificity of binding of the antibodies and gp120 to the isolated lipid fraction. Identity of the binding site of the two ligands to the glycolipid is suggested by competition assays. On the basis of preliminary biochemical analysis this glycolipid was tentatively classified as a galactosylalkylacylglycerolipid (GalAAG), the nonsulfated form of the seminolipid, a glycolipid known to be present in the testis and germ cells of mammals. These data indicate that human sperm express a glycolipid similar in structure to the receptor for HIV described on the CD4- neural and colonic epithelial cell lines, and moreover suggest that this glycolipid could also function as HIV receptor and possibly be implicated in its transmission.
Subject(s)
Glycolipids/metabolism , HIV Envelope Protein gp120/metabolism , HIV-1/chemistry , Spermatozoa/chemistry , Antibodies, Monoclonal , Enzyme-Linked Immunosorbent Assay , Fluorescent Antibody Technique, Indirect , Galactosylceramides/immunology , Galactosylceramides/metabolism , HIV Envelope Protein gp120/immunology , Humans , Male , Molecular Structure , Protein BindingABSTRACT
Sexual transmission is a major mode of spread of HIV-1 although the mechanisms involved remain to be elucidated. The role of spermatozoa as carriers of the HIV is supported by recent publications, while the expression of the CD4 on the membrane of the sperm has not yet been demonstrated. The data reported in this paper show that a glycolipid molecule, most likely the galactosyl-alkyl-acylglycerol, structurally similar to galactosylceramides, is present on the surface membrane of the spermatozoa. Consistent with a structure similar to galactosylceramide, the sperm glycolipid is capable of binding the gp120 as demonstrated utilizing an improved ELISA assay which favors sensitivity and specificity. Immunocytochemistry of testicular tissue shows the presence of this glycolipid on the membrane of immature germ cells, preferentially in the spermatogonia. These data indicate that human sperm express a glycolipid similar in structure to the receptor for HIV described on the CD4- neural and colonic epithelial cell lines, and moreover suggest that this glycolipid could also function as HIV receptor and possibly be implied in its transmission. The demonstration that this molecule is also expressed by the spermatogonia suggests its involvement in the interaction of the HIV with spermatogonia, as recently reported, and could explain the inhibition of spermatogenesis observed in AIDS patients.
