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

Fingerprint

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.
@article{5a3458f1d50c40db902ba143c43261bb,
title = "Peptidoglycan Recognition Proteins Involved in 1,3-β -D-Glucan-dependent Prophenoloxidase Activation System of Insect",
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.",
author = "Lee, {Mi Hee} and Tsukasa Osaki and Lee, {Joo Young} and Baek, {Min Ji} and Rong Zhang and Park, {Ji Won} and Kawabata, {Shun Ichiro} and Kenneth S{\"o}derh{\"a}ll and Lee, {Bok Luel}",
year = "2004",
month = "1",
day = "30",
doi = "10.1074/jbc.M309821200",
language = "English",
volume = "279",
pages = "3218--3227",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "5",

}

TY - JOUR

T1 - Peptidoglycan Recognition Proteins Involved in 1,3-β -D-Glucan-dependent Prophenoloxidase Activation System of Insect

AU - Lee, Mi Hee

AU - Osaki, Tsukasa

AU - Lee, Joo Young

AU - Baek, Min Ji

AU - Zhang, Rong

AU - Park, Ji Won

AU - Kawabata, Shun Ichiro

AU - Söderhäll, Kenneth

AU - Lee, Bok Luel

PY - 2004/1/30

Y1 - 2004/1/30

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0942265564&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0942265564&partnerID=8YFLogxK

U2 - 10.1074/jbc.M309821200

DO - 10.1074/jbc.M309821200

M3 - Article

C2 - 14583608

AN - SCOPUS:0942265564

VL - 279

SP - 3218

EP - 3227

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 5

ER -