Role of curdlan sulfate in the binding of HIV-1 gp120 to CD4 molecules and the production of gp120-mediated TNF-alpha

N Takeda-Hirokawa; L P Neoh; H Akimoto; H Kaneko; T Hishikawa; I Sekigawa; H Hashimoto; S Hirose; T Murakami; N Yamamoto; T Mimura; Y Kaneko

doi:10.1111/j.1348-0421.1997.tb01920.x

Role of curdlan sulfate in the binding of HIV-1 gp120 to CD4 molecules and the production of gp120-mediated TNF-alpha

Microbiol Immunol. 1997;41(9):741-5. doi: 10.1111/j.1348-0421.1997.tb01920.x.

Authors

N Takeda-Hirokawa¹, L P Neoh, H Akimoto, H Kaneko, T Hishikawa, I Sekigawa, H Hashimoto, S Hirose, T Murakami, N Yamamoto, T Mimura, Y Kaneko

Affiliation

¹ Department of Internal Medicine and Rheumatology, Juntendo University School of Medicine, Tokyo, Japan.

PMID: 9343827
DOI: 10.1111/j.1348-0421.1997.tb01920.x

Abstract

To clarify the mechanism by which curdlan sulfate (CRDS) inhibits human immunodeficiency virus (HIV)-1 infection, we examined its influence on the binding of gp120 to CD4 molecules on T cells and macrophages, as well as on the production of TNF-alpha by gp120-stimulated macrophages (which promotes HIV-1 replication). CRDS treatment of cells not only inhibited the binding of HIV-1 gp120 to CD4+ cells, but also inhibited TNF-alpha production induced by gp120. Inhibition of HIV-1 infection by CRDS may be related to these two actions.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Anti-HIV Agents / pharmacology*
CD4 Antigens / metabolism*
Depression, Chemical
Gene Expression Regulation / drug effects
Glucans / pharmacology*
HIV Envelope Protein gp120 / metabolism*
HIV-1 / drug effects*
HIV-1 / metabolism
Humans
Macrophages / metabolism*
Protein Binding / drug effects
T-Lymphocytes / metabolism*
Tumor Necrosis Factor-alpha / biosynthesis*
Tumor Necrosis Factor-alpha / genetics
beta-Glucans*

Substances

Anti-HIV Agents
CD4 Antigens
Glucans
HIV Envelope Protein gp120
Tumor Necrosis Factor-alpha
beta-Glucans
curdlan sulfate