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(Received for publication, July 21, 1997, and in revised form, September 25, 1997)
From the Department of Biology, Faculty of Science, Kyushu
University, Fukuoka 812-82, Japan
We identified a novel horseshoe crab
hemocyte-derived lectin, which we named tachylectin-4. It has more
potent hemagglutinating activity against human A-type erythrocytes than
a previously identified hemocyte lectin with an affinity to
N-acetylglucosamine, tachylectin-2. The purified
tachylectin-4 is an oligomeric glycoprotein of 470 kDa, composed of
subunits of 30 and 31.5 kDa. Ca2+ at 10 mM
enhanced the hemagglutinating activity 4-fold, and the activity was
inhibited by EDTA and o-phenanthroline.
L-Fucose and N-acetylneuraminic acid at 100 mM completely inhibited the activity of tachylectin-4. The
activity was also inhibited more strongly by bacterial S-type
lipopolysaccharides (LPS) but not by R-type LPS lacking O-antigen. The
most effective S-type LPS was from Escherichia coli
O111:B4, and the minimum concentration required for inhibiting
agglutination against human A-type erythrocytes (0.1 µg/ml) was
160-fold lower than those of S-type LPS from Salmonella minnesota. Therefore, colitose (3-deoxy-L-fucose), a
unique sugar present in the O-antigen of E. coli O111:B4
with structural similarity to L-fucose, is the most
probable candidate for a specific ligand of tachylectin-4.
A cDNA coding for tachylectin-4 was isolated from a hemocyte
cDNA library. The open reading frame of the 1344-base pair cDNA coded for the mature protein with 232 amino acids. There is no significant sequence similarity to any other known LPS-binding lectins,
whereas tachylectin-4 is homologous to the NH2-terminal domain with unknown functions of Xenopus laevis pentraxin
1.
Volume 272, Number 49,
Issue of December 5, 1997
pp. 30703-30708
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
A Newly Identified Horseshoe Crab Lectin with Binding Specificity
to O-antigen of Bacterial Lipopolysaccharides
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