β-1,3-Glucan recognition protein-2 (βGRP-2) from Manduca sexta: an acute-phase protein that binds β-1,3-glucan and lipoteichoic acid to aggregate fungi and bacteria and stimulate prophenoloxidase activation

Jiang, Haobo; Ma, Congcong; Lu, Zhiqiang; Kanost, Michael R.

doi:10.1016/j.ibmb.2003.09.006

Cited by 123 publications

(107 citation statements)

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“…The analysis revealed that these sequences clustered in two distinct clades. One of them falls into three subclades (clades 1, 2, and 3) containing many proteins that had previously been found in insect hemolymph: Mse_BGRP1 and 2 (6,8), Bmo_BGRP and p50_GNBP (7,9), Pin_BGRP (5), and Ha_BGRP1 and 2a (the present study). The second cluster (clade 4) contains the H. armigera Glucanase-1 protein isolated from the midgut, and sequences from cDNA libraries made from midgut tissue of different Lepidoptera species.…”

Section: Glucanase-1 Is Conserved Among Lepidoptera and Other Insectmentioning

confidence: 51%

“…To further test whether the glucan-binding protein itself could be responsible for this ␤1,3-glucanase activity, its coding sequence fused to a C-terminal V5/(His) 6 tag was transiently expressed in High Five insect cells (Fig. 2C).…”

Section: Resultsmentioning

confidence: 99%

“…Gram-negative bacteria-binding proteins (GNBPs) and ␤1,3-glucan recognition proteins (␤GRPs) have been extensively studied as pattern recognition proteins in Lepidoptera (5)(6)(7)(8)(9)(10). These proteins are produced in the fat body and secreted into the hemolymph of the caterpillar.…”

mentioning

confidence: 99%

“…These proteins are produced in the fat body and secreted into the hemolymph of the caterpillar. Some are constitutively present (5,8), whereas others are induced upon microbial infection (6). Recognition of ␤1,3-glucans by these proteins appears to be due to two distinct ␤1,3-glucan-binding domains: a strongly binding N-terminal glucan recognition domain and a weakly binding C-terminal glucanase-like domain.…”

mentioning

confidence: 99%

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Immunity or Digestion

Pauchet

Freitak²,

Heidel‐Fischer

et al. 2009

Journal of Biological Chemistry

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The cell surfaces of microorganisms display distinct molecular patterns formed from lipopolysaccharides, peptidoglycans, or ␤1,3-glucans. Binding of these surfaces by pattern recognition proteins such as ␤1,3-glucan recognition proteins (␤GRPs) activates the immune response in arthropods. We identified a 40-kDa ␤1,3-glucan-binding protein with sequence similarity to previously characterized lepidopteran ␤GRPs from hemolymph, but unlike these it is secreted into the larval gut lumen and is an active ␤1,3-glucanase. This glucanase was not detected in hemolymph. Its mRNA is constitutively and predominantly expressed in the midgut and is induced there when larvae feed on a diet containing bacteria. Homologs of this predominantly midgut-expressed gene from many Lepidoptera possess key residues shown to be part of the active site of other glucanases, and form a cluster that is distinct from previously described ␤GRPs. In addition, this group includes proteins from insects such as the Anopheles gambiae GNBP subgroup B for which a catalytic role has not been previously suspected. The current domain classification does not distinguish between the catalytic and noncatalytic clades, and should be revised. The noncatalytic ␤GRPs may be evolutionarily derived from this newly described enzyme family that continues to function catalytically in digestion and/or pathogen defense.

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Section: Glucanase-1 Is Conserved Among Lepidoptera and Other Insectmentioning

confidence: 51%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Immunity or Digestion

Pauchet

Freitak²,

Heidel‐Fischer

et al. 2009

Journal of Biological Chemistry

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“…The major structural components of the fungal cell wall are -1,3-and -1,6-glucans, chitin, mannan, and glycoproteins, and insect hemolymph -glucan-binding proteins function in innate immune responses by binding to -glucans on the cell surface of invading fungi and initiating host defense reactions. [1][2][3] The silkworm Bombyx mori -1,3-glucan recognition protein has been shown to trigger the prophenoloxidase (proPO) cascade, a pathway in insects for defense against microbial infection, via binding to -1,3-glucan on the surface of invading pathogens. 4,5) Recently we found that B. mori 30-kDa lipoproteins (6G1 and 19G1), major plasma proteins of the fifth instar larvae and of pupae, [6][7][8] bind to -glucan, a fungal immune elicitor.…”

mentioning

confidence: 99%

Glucan-Binding Activity of Silkworm 30-kDa Apolipoprotein and Its Involvement in Defense against Fungal Infection

Ujita

Katsuno

Kawachi

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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Thermolysin Damages Animal Life Through Degradation of Plasma Proteins Enhanced by Rapid Cleavage of Serpins and Activation of Proteases

Kong

Lü

Guan

et al. 2014

Arch Insect Biochem Physiol

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Thermolysin, a metallopeptidase secreted by pathogenic microbes, is concluded as an important virulence factor due to cleaving purified host proteins in vitro. Using the silkworm Bombyx mori as a model system, we found that thermolysin injection into larvae induces the destruction of the coagulation response and the activation of hemolymph melanization, which results in larval death. Thermolysin triggers the rapid degradation of insect and mammalian plasma proteins at a level that is considerably greater than expected in vitro and/or in vivo. To more specifically explore the mechanism, thermolysin-induced changes to key proteins belonging to the insect melanization pathway were assessed as a window for observing plasma protein cleavage. The application of thermolysin induced the rapid cleavage of the melanization negative regulator serpin-3, but did not directly activate the melanization rate-limiting enzyme prophenoloxidase (PPO) or the terminal serine proteases responsible for PPO activation. Terminal serine proteases of melanization are activated indirectly after thermolysin exposure. We hypothesize that thermolysin induces the rapid degradation of serpins and the activation of proteases directly or indirectly, boosting uncontrolled plasma protein degradation in insects and mammalians.

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β-1,3-Glucan recognition protein-2 (βGRP-2) from Manduca sexta: an acute-phase protein that binds β-1,3-glucan and lipoteichoic acid to aggregate fungi and bacteria and stimulate prophenoloxidase activation

Cited by 123 publications

References 32 publications

Immunity or Digestion

Immunity or Digestion

Glucan-Binding Activity of Silkworm 30-kDa Apolipoprotein and Its Involvement in Defense against Fungal Infection

Thermolysin Damages Animal Life Through Degradation of Plasma Proteins Enhanced by Rapid Cleavage of Serpins and Activation of Proteases

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