Role of curdlan sulfate in the binding of HIV-1 gp120 to CD4 molecules and the production of gp120-mediated TNF-alpha.
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.
Takeda-Hirokawa
N
N
Department of Internal Medicine and Rheumatology, Juntendo University School of Medicine, Tokyo, Japan.
Neoh
L P
LP
Akimoto
H
H
Kaneko
H
H
Hishikawa
T
T
Sekigawa
I
I
Hashimoto
H
H
Hirose
S
S
Murakami
T
T
Yamamoto
N
N
Mimura
T
T
Kaneko
Y
Y
D019380:Anti-HIV Agents / Q000494:pharmacology*; D015704:CD4 Antigens / Q000378:metabolism*; D003864:Depression, Chemical; D005786:Gene Expression Regulation / Q000187:drug effects; D005936:Glucans / Q000494:pharmacology*; D015699:HIV Envelope Protein gp120 / Q000378:metabolism*; D015497:HIV-1 / Q000187:drug effects* / Q000378:metabolism; D006801:Humans; D008264:Macrophages / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D013601:T-Lymphocytes / Q000378:metabolism*; D014409:Tumor Necrosis Factor-alpha / Q000096:biosynthesis* / Q000235:genetics; D047071:beta-Glucans
D019380:Anti-HIV Agents; D015704:CD4 Antigens; D005936:Glucans; D015699:HIV Envelope Protein gp120; D014409:Tumor Necrosis Factor-alpha; D047071:beta-Glucans; C063130:curdlan sulfate