A newly identified horseshoe crab lectin with binding specificity to O- antigen of bacterial lipopolysaccharides

Tetsu Saito, Motoki Hatada, Sadaaki Iwanaga, Shun-Ichiro Kawabata

研究成果: ジャーナルへの寄稿記事

84 引用 (Scopus)

抄録

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 0111: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 0111: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.

元の言語英語
ページ(範囲)30703-30708
ページ数6
ジャーナルJournal of Biological Chemistry
272
発行部数49
DOI
出版物ステータス出版済み - 12 5 1997

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Horseshoe Crabs
O Antigens
Lectins
Lipopolysaccharides
Hemocytes
Fucose
Escherichia coli
Complementary DNA
Erythrocytes
Salmonella
Acetylglucosamine
Agglutination
Xenopus laevis
N-Acetylneuraminic Acid
Gene Library
Human Activities
Edetic Acid
Sugars
Base Pairing
Open Reading Frames

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

A newly identified horseshoe crab lectin with binding specificity to O- antigen of bacterial lipopolysaccharides. / Saito, Tetsu; Hatada, Motoki; Iwanaga, Sadaaki; Kawabata, Shun-Ichiro.

:: Journal of Biological Chemistry, 巻 272, 番号 49, 05.12.1997, p. 30703-30708.

研究成果: ジャーナルへの寄稿記事

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abstract = "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 0111: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 0111: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.",
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AB - 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 0111: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 0111: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.

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