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J Biol Chem, Vol. 273, Issue 34, 22014-22020, August 21, 1998
-(1-3)-Glucan Immunomodulator, PGG-glucan, and Lactosylceramide of
Human Leukocytes
From Alpha-Beta Technology, Inc., Worcester, Massachusetts
01605
The immunomodulator Betafectin® PGG-glucan is a
homopolymer of glucose derived from yeast cell walls which has been
demonstrated to enhance leukocyte anti-infective activity in
vitro and in vivo, without the induction of
proinflammatory cytokines. We report here the purification of a
PGG-glucan-binding element from human leukocytes and its identification
as lactosylceramide, a major glycosphingolipid of neutrophils, which
includes the CDw17 epitope. The binding of radiolabeled PGG-glucan to
purified lactosylceramide was saturable, specific, and time- and
temperature-dependent. Lactosylceramides from human
leukocytes were fractionated by high performance liquid chromatography
in order to analyze the effect of ceramide structure on binding. A
variety of fatty acid chain lengths with varying degrees of
unsaturation were found to support binding to radiolabeled PGG-glucan.
However, DL-lactosylceramides containing dihydrosphingosine
did not bind. Radiolabeled PGG-glucan bound several other neutral
glycosphingolipids with a terminal galactose, including
galactosylceramide, globotriaosylceramide, and
gangliotetraosylceramide. The binding of radiolabeled PGG-glucan to lactosylceramide was not inhibited by glycogen, dextran, mannan, pustulan, laminarin, or a low molecular weight 
-(1-3)-glucan, but
was inhibited by high molecular weight -(1-3)-glucans and by a
monoclonal antibody to lactosylceramide. Although this
glycosphingolipid has been shown in numerous reports to bind various
microorganisms, this represents the first report of lactosylceramide
binding to a macromolecular carbohydrate.
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