Role of cell surface glycosaminoglycans of human T cells in human immunodeficiency virus type-1 (HIV-1) infection.

Abstract

To investigate the role of cell surface glycosaminoglycans (GAGs), including heparan sulfate (HS), on HIV-1 infection in human T cells, HIV-1 binding and infection were determined after treatment of T-cell lines and CD4+ T cells from normal peripheral blood mononuclear cells (PBMC) with GAG-degrading enzyme or a GAG metabolic sulfation inhibitor. Heparitinase I (hep I) and sodium chlorate prevented binding of HIV-1/IIIB to MT-4 cells as revealed by indirect immunofluorescence procedures, thereby inhibiting infection. Hep I was less effective in the binding inhibition of the macrophage-tropic strain HIV-1/SF162 than that of the T-cell line-tropic strain HIV-1/IIIB. The binding of HIV-1/SF162 was about 100-fold less dependent on cell surface HS than HIV-1/IIIB. Human HTLV-I positive T-cell lines expressed more HS than HTLV-I negative T-cell lines or normal CD4+ T cells when stained with anti-HS mAbs against either native or heparitinase-treated HS. With the exception of endo-beta-galactosidase (endo-beta-gal), GAG-degrading enzymes, including hep I, chondroitinase ABC (chon ABC), chondroitinase AC II (chon AC II) and keratanase, did not prevent the binding of HIV-1/IIIB to CD4+ T cells from normal PBMC. These results indicate that the cell surface HS of human T cells participates in HIV-1 infection by facilitating HIV-1/IIIB binding to MT-4 cells. In particular, the sulfation of HS chains is critical. Since the expression of cell surface HS varies among T cells, which are not consistently sensitive to hep I treatment in HIV-1 binding inhibition, other GAG-like molecules may also be involved.

• Authors: Y Ohshiro, T Murakami, K Matsuda, K Nishioka, K Yoshida, N Yamamoto
• Journal: Microbiology and immunology (Microbiol Immunol) Vol. 40 Issue 11 Pg. 827-35 ( 1996) ISSN: 0385-5600 [Print] Australia
• PMID: 8985938 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Chlorates
• Glycosaminoglycans
• Heparitin Sulfate
• Glycoside Hydrolases
• keratan-sulfate endo-1,4-beta-galactosidase
• beta-Galactosidase
• Chondroitin Lyases
• Polysaccharide-Lyases
• heparitinsulfate lyase
• sodium chlorate

Topics

• CD4-Positive T-Lymphocytes (chemistry, virology)
• Cell Line
• Cell Membrane (chemistry)
• Chlorates (pharmacology)
• Chondroitin Lyases (pharmacology)
• Fluorescent Antibody Technique, Indirect
• Glycosaminoglycans (physiology)
• Glycoside Hydrolases
• HIV-1 (physiology)
• Heparitin Sulfate (analysis, physiology)
• Humans
• Polysaccharide-Lyases (pharmacology)
• T-Lymphocytes (chemistry, virology)
• beta-Galactosidase (pharmacology)