An immune-responsive Serpin regulates the melanization cascade in Drosophila

Ennio De Gregorio; Sung Jun Han; Won Jae Lee; Min Ji Baek; Tsukasa Osaki; Shun Ichiro Kawabata; Bok Leul Lee; Sadaaki Iwanaga; Bruno Lemaitre; Paul T. Brey

doi:10.1016/S1534-5807(02)00267-8

An immune-responsive Serpin regulates the melanization cascade in Drosophila

Ennio De Gregorio, Sung Jun Han, Won Jae Lee, Min Ji Baek, Tsukasa Osaki, Shun Ichiro Kawabata, Bok Leul Lee, Sadaaki Iwanaga, Bruno Lemaitre, Paul T. Brey

Biology, Faculty of Science

Research output: Contribution to journal › Article › peer-review

130 Citations (Scopus)

Abstract

In arthropods, the melanization reaction is associated with multiple host defense mechanism leading to the sequestration and killing of invading microorganisms. Arthropod melanization is controlled by a cascade of serine proteases that ultimately activates the enzyme prophenoloxidase (PPO), which, in turn, catalyzes the synthesis of melanin. Here we report the biochemical and genetic characterization of a Drosophila serine protease inhibitor protein, Serpin-27A, which regulates the melanization cascade through the specific inhibition of the terminal protease prophenoloxidase-activating enzyme. Our data demonstrate that Serpin-27A is required to restrict the phenoloxidase activity to the site of injury or infection, preventing the insect from excessive melanization.

Original language	English
Pages (from-to)	581-592
Number of pages	12
Journal	Developmental Cell
Volume	3
Issue number	4
DOIs	https://doi.org/10.1016/S1534-5807(02)00267-8
Publication status	Published - Oct 1 2002

All Science Journal Classification (ASJC) codes

Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Developmental Biology
Cell Biology

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10.1016/S1534-5807(02)00267-8

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title = "An immune-responsive Serpin regulates the melanization cascade in Drosophila",

abstract = "In arthropods, the melanization reaction is associated with multiple host defense mechanism leading to the sequestration and killing of invading microorganisms. Arthropod melanization is controlled by a cascade of serine proteases that ultimately activates the enzyme prophenoloxidase (PPO), which, in turn, catalyzes the synthesis of melanin. Here we report the biochemical and genetic characterization of a Drosophila serine protease inhibitor protein, Serpin-27A, which regulates the melanization cascade through the specific inhibition of the terminal protease prophenoloxidase-activating enzyme. Our data demonstrate that Serpin-27A is required to restrict the phenoloxidase activity to the site of injury or infection, preventing the insect from excessive melanization.",

author = "{De Gregorio}, Ennio and Han, {Sung Jun} and Lee, {Won Jae} and Baek, {Min Ji} and Tsukasa Osaki and Kawabata, {Shun Ichiro} and Lee, {Bok Leul} and Sadaaki Iwanaga and Bruno Lemaitre and Brey, {Paul T.}",

note = "Funding Information: We thank Fran{\c c}ois Leulier, Nicolas Vodovar, Brigitte Maroni, Sylvie Perrot, and Charles Roth for assistance and stimulating discussions. E.D.G. was supported by a Human Frontier Science Program fellowship. The laboratory of B.L. was funded by the Association pour la Recherche contre le Cancer (ARC), the Fondation pour la Recherche M{\'e}dicale (FRM), and Programme Microbiologie (PRMMIP00). The laboratory of P.T.B. was supported by grants from the Institut Pasteur and the CNRS Programme International de Cooperation Scientifique N°907 France-Japon. S.-J.H. was the recipient of a French Government Doctoral Scholarship.",

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AU - De Gregorio, Ennio

AU - Han, Sung Jun

AU - Lee, Won Jae

AU - Baek, Min Ji

AU - Osaki, Tsukasa

AU - Kawabata, Shun Ichiro

AU - Lee, Bok Leul

AU - Iwanaga, Sadaaki

AU - Lemaitre, Bruno

AU - Brey, Paul T.

N1 - Funding Information: We thank François Leulier, Nicolas Vodovar, Brigitte Maroni, Sylvie Perrot, and Charles Roth for assistance and stimulating discussions. E.D.G. was supported by a Human Frontier Science Program fellowship. The laboratory of B.L. was funded by the Association pour la Recherche contre le Cancer (ARC), the Fondation pour la Recherche Médicale (FRM), and Programme Microbiologie (PRMMIP00). The laboratory of P.T.B. was supported by grants from the Institut Pasteur and the CNRS Programme International de Cooperation Scientifique N°907 France-Japon. S.-J.H. was the recipient of a French Government Doctoral Scholarship.

PY - 2002/10/1

Y1 - 2002/10/1

N2 - In arthropods, the melanization reaction is associated with multiple host defense mechanism leading to the sequestration and killing of invading microorganisms. Arthropod melanization is controlled by a cascade of serine proteases that ultimately activates the enzyme prophenoloxidase (PPO), which, in turn, catalyzes the synthesis of melanin. Here we report the biochemical and genetic characterization of a Drosophila serine protease inhibitor protein, Serpin-27A, which regulates the melanization cascade through the specific inhibition of the terminal protease prophenoloxidase-activating enzyme. Our data demonstrate that Serpin-27A is required to restrict the phenoloxidase activity to the site of injury or infection, preventing the insect from excessive melanization.

AB - In arthropods, the melanization reaction is associated with multiple host defense mechanism leading to the sequestration and killing of invading microorganisms. Arthropod melanization is controlled by a cascade of serine proteases that ultimately activates the enzyme prophenoloxidase (PPO), which, in turn, catalyzes the synthesis of melanin. Here we report the biochemical and genetic characterization of a Drosophila serine protease inhibitor protein, Serpin-27A, which regulates the melanization cascade through the specific inhibition of the terminal protease prophenoloxidase-activating enzyme. Our data demonstrate that Serpin-27A is required to restrict the phenoloxidase activity to the site of injury or infection, preventing the insect from excessive melanization.

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An immune-responsive Serpin regulates the melanization cascade in Drosophila

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