|
||
Journal of Experimental Medicine, Vol 169, 185-196, Copyright © 1989 by Rockefeller University Press
ARTICLES |
RA Ezekowitz, M Kuhlman, JE Groopman and RA Byrn
Division of Hematology/Oncology, Harvard Medical School, Boston, Massachusetts.
In vitro infection by the human immunodeficiency virus (HIV) of CD4+ H9 lymphoblasts is inhibited by a mannose-binding protein (MBP) purified from human serum. In addition, MBP is able to selectively bind to HIV- infected H9 cells and HIV-infected cells from the monocyte cell line U937. These results indicate MBP most likely recognizes high mannose glycans known to be present on gp120 in the domain that is recognized by CD4 and thereby inhibits viral entry to susceptible cells. In support of this contention, recombinant gp120 binds directly to MBP; the binding is saturable, mannan inhibitable, removed by N-glycanase treatment, and dependent on divalent cations.
This article has been cited by other articles:
| TABLE OF CONTENTS |
|