Peptidoglycan Recognition Proteins Involved in 1,3-β -D-Glucan-dependent Prophenoloxidase Activation System of Insect

Mi Hee Lee, Tsukasa Osaki, Joo Young Lee, Min Ji Baek, Rong Zhang, Ji Won Park, Shun-Ichiro Kawabata, Kenneth Söderhäll, Bok Luel Lee

研究成果: ジャーナルへの寄稿記事

77 引用 (Scopus)

抄録

The prophenoloxidase (proPO) cascade is a major innate immune response in invertebrates, which is triggered into its active form by elicitors, such as lipopolysaccharide, peptidoglycan, and 1,3-β-D-glucan. A key question of the proPO system is how pattern recognition proteins recognize pathogenic microbes and subsequently activate the system. To investigate the biological function of 1,3-β-D-glucan pattern recognition protein in the proPO cascade system, we isolated eight different 1,3-β-D-glucan-binding proteins from the hemolymph of large beetle (Holotrichia diomphalia) larvae by using 1,3-β-D-glucan immobilized column. Among them, a 20- and 17-kDa protein (referred to as Hd-PGRP-1 and Hd-PGRP-2) show high sequence identity with the short forms of peptidoglycan recognition proteins (PGRPs-S) from human and Drosophila melanogaster. To be able to characterize the biochemical prop. erties of these two proteins, we expressed them in Drosophila S2 cells. Hd-PGRP-1 and Hd-PGRP-2 were found to specifically bind both 1, 3-β-D-glucan and peptidoglycan. By BIAcore analysis, the minimal 1,3-β-D-glucan structure required for binding to Hd-PGRP-1 was found to be laminaritetraose. Hd-PGRP-1 increased serine protease activity upon binding to 1,3-β-D-glucan and subsequently induced the phenoloxidase activity in the presence of both 1,3-β-D-glucan and Ca2+, but no phenoloxidase activity was elicited under the same conditions in the presence of peptidoglycan and Ca2+. These results demonstrate that Hd-PGRP-1 can serve as a receptor for 1,3-β-D-glucan in the insect proPO activation system.

元の言語英語
ページ(範囲)3218-3227
ページ数10
ジャーナルJournal of Biological Chemistry
279
発行部数5
DOI
出版物ステータス出版済み - 1 30 2004

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Insects
Chemical activation
Peptidoglycan
Monophenol Monooxygenase
Pattern recognition
Automated Pattern Recognition
Proteins
pro-phenoloxidase
polyglucosan
peptidoglycan recognition protein
Hemolymph
Beetles
Serine Proteases
Invertebrates
Drosophila melanogaster
Innate Immunity
Drosophila
Larva
Lipopolysaccharides

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Peptidoglycan Recognition Proteins Involved in 1,3-β -D-Glucan-dependent Prophenoloxidase Activation System of Insect. / Lee, Mi Hee; Osaki, Tsukasa; Lee, Joo Young; Baek, Min Ji; Zhang, Rong; Park, Ji Won; Kawabata, Shun-Ichiro; Söderhäll, Kenneth; Lee, Bok Luel.

:: Journal of Biological Chemistry, 巻 279, 番号 5, 30.01.2004, p. 3218-3227.

研究成果: ジャーナルへの寄稿記事

Lee, Mi Hee ; Osaki, Tsukasa ; Lee, Joo Young ; Baek, Min Ji ; Zhang, Rong ; Park, Ji Won ; Kawabata, Shun-Ichiro ; Söderhäll, Kenneth ; Lee, Bok Luel. / Peptidoglycan Recognition Proteins Involved in 1,3-β -D-Glucan-dependent Prophenoloxidase Activation System of Insect. :: Journal of Biological Chemistry. 2004 ; 巻 279, 番号 5. pp. 3218-3227.
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abstract = "The prophenoloxidase (proPO) cascade is a major innate immune response in invertebrates, which is triggered into its active form by elicitors, such as lipopolysaccharide, peptidoglycan, and 1,3-β-D-glucan. A key question of the proPO system is how pattern recognition proteins recognize pathogenic microbes and subsequently activate the system. To investigate the biological function of 1,3-β-D-glucan pattern recognition protein in the proPO cascade system, we isolated eight different 1,3-β-D-glucan-binding proteins from the hemolymph of large beetle (Holotrichia diomphalia) larvae by using 1,3-β-D-glucan immobilized column. Among them, a 20- and 17-kDa protein (referred to as Hd-PGRP-1 and Hd-PGRP-2) show high sequence identity with the short forms of peptidoglycan recognition proteins (PGRPs-S) from human and Drosophila melanogaster. To be able to characterize the biochemical prop. erties of these two proteins, we expressed them in Drosophila S2 cells. Hd-PGRP-1 and Hd-PGRP-2 were found to specifically bind both 1, 3-β-D-glucan and peptidoglycan. By BIAcore analysis, the minimal 1,3-β-D-glucan structure required for binding to Hd-PGRP-1 was found to be laminaritetraose. Hd-PGRP-1 increased serine protease activity upon binding to 1,3-β-D-glucan and subsequently induced the phenoloxidase activity in the presence of both 1,3-β-D-glucan and Ca2+, but no phenoloxidase activity was elicited under the same conditions in the presence of peptidoglycan and Ca2+. These results demonstrate that Hd-PGRP-1 can serve as a receptor for 1,3-β-D-glucan in the insect proPO activation system.",
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AU - Lee, Joo Young

AU - Baek, Min Ji

AU - Zhang, Rong

AU - Park, Ji Won

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AU - Söderhäll, Kenneth

AU - Lee, Bok Luel

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