Glycoglycerolipid from the membranes of Acholeplasma laidlawii binds to human immunodeficiency virus-1 (HIV-1) and accelerates its entry into cells.
We have reported previously that glycoglycerolipids derived from the membranes of Acholeplasma laidlawii, 3- O-[2'- O-(alpha-D-glucopyranosyl)-6'- O-acyl-alpha-glucopyranosyl]-1,2-di- O-acyl- sn-glycerols (GAGDGs) bind to human cell lines. In addition, the GAGDGs were found to augment HIV-1 infection in human cell lines. Here we show that GAGDG binds to HIV-1 and facilitates the entry of HIV-1 into cells. The binding ability of GAGDG to HIV-1 was blocked by anti-GAGDG serum. Binding assay with synthetic GAGDGs and related compounds showed that the presence of branching form of acyl chains at the C14 or C16 position, glucose, and the acyl chain binding to the glucose were critical for efficient binding. GAGDG efficiently augmented the entry of HIV-1 into cells in a single-cycle replication assay. These results indicate that GAGDG of A. laidlawii membranes participates in the facilitation of HIV-1 infection.
Shimizu
Takashi
T
Department of Bacteriology, Kurume University School of Medicine, 67 Asahi-machi, Kurume, Fukuoka 830-0011, Japan. takashi@med.kurume-u.ac.jp
Arai
Sumio
S
Imai
Hiroto
H
Oishi
Tohru
T
Hirama
Masahiro
M
Koito
Atsushi
A
Kida
Yutaka
Y
Kuwano
Koichi
K
D000128:Acholeplasma laidlawii / Q000737:chemistry* / Q000378:metabolism; D002460:Cell Line; D006017:Glycolipids / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D016655:HIV Core Protein p24 / Q000032:analysis; D015497:HIV-1 / Q000254:growth & development* / Q000378:metabolism*; D006801:Humans; D007106:Immune Sera; D013601:T-Lymphocytes / Q000821:virology; D014779:Virus Replication
D006017:Glycolipids; D016655:HIV Core Protein p24; D007106:Immune Sera; C015903:glycerolglycolipids