Activation of pro-phenoloxidase by bacterial cell walls or β-1,3-glucans in plasma of the silkworm, Bombyx mori

Ashida, Masaaki; Ishizaki, Yuhko; Iwahana, Hidenori

doi:10.1016/0006-291x(83)91762-x

Cited by 157 publications

(69 citation statements)

References 16 publications

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“…Although we cannot exclude the possibility that the LPS also has a weak stimulatory effect in vivo that was not detected in our assay, our results indicate that peptidoglycan is the most active determinant of Gram-negative bacteria. This finding extends the results of previous studies showing that peptidoglycan but not LPS activates the prophenoloxidase cascade in the silkworm Bombyx mori 31,32 . Our study shows that the Imd pathway is activated by specific recognition of Gram-negative and Bacillus peptidoglycans, whereas the Toll pathway is more responsive to lysine-type peptidoglycans found in most Gram-positive bacteria.…”

Section: Discussionsupporting

confidence: 91%

The Drosophila immune system detects bacteria through specific peptidoglycan recognition

et al. 2003

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The Drosophila immune system discriminates between different classes of infectious microbes and responds with pathogen-specific defense reactions through selective activation of the Toll and the immune deficiency (Imd) signaling pathways. The Toll pathway mediates most defenses against Gram-positive bacteria and fungi, whereas the Imd pathway is required to resist infection by Gram-negative bacteria. The bacterial components recognized by these pathways remain to be defined. Here we report that Gram-negative diaminopimelic acid-type peptidoglycan is the most potent inducer of the Imd pathway and that the Toll pathway is predominantly activated by Gram-positive lysine-type peptidoglycan. Thus, the ability of Drosophila to discriminate between Gram-positive and Gram-negative bacteria relies on the recognition of specific forms of peptidoglycan.

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Section: Discussionsupporting

confidence: 91%

The Drosophila immune system detects bacteria through specific peptidoglycan recognition

et al. 2003

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“…In the arthropod proPO system, a threshold concentration of calcium is required for proPO activation (51)(52)(53), suggesting that calcium plays an important role in this process. However, the role(s) of calcium is still unclear.…”

Section: Discussionmentioning

confidence: 99%

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

Lee

Osaki

Lee

et al. 2004

Journal of Biological Chemistry

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“…It should be noted, however, that these authors never studied the activation of these enzymes, but only their activity once they had been activated. For the sake of clarity, it is important to visualize phenoloxidase within the context of the prophenoloxidase enzyme cascade [lo, 27, 281. Prophenoloxidase in arthropods is known to be activated by serine proteases which are initially activated by elicitors, such as microbial products (fi-l,3-glucan and peptidoglycan) [15,18,27,29,301 and denatured plasma proteins [27]. Furthermore, detergent, heat, [31, 321 and solvents [33, 341 can also cause activation of prophenoloxidase, but not by limited proteolysis.…”

Section: Discussionmentioning

confidence: 99%

Studies on prophenoloxidase activation in the mosquito Aedes aegypti L.

Ashida

Kinoshita

Brey

1990

European Journal of Biochemistry

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This study, the first of its kind in a mosquito vector species, demonstrates the feasibility of studying prophenoloxidase activation in an insect containing not more than a few microliters of hemolymph. Mosquito phenoloxidase was found to be in an inactive proenzyme form, prophenoloxidase. Mosquito prophenoloxidase required bivalent cation for its activation; Ca2+ was found to be the most efficient for activation. Concomitant amidase activity was also observed prior to phenoloxidase activity. Through Western blotting, using a cross-reactive silkworm antiprophenoloxidase antibody, our results strongly suggest that mosquito prophenoloxidase activation resulted from limited proteolysis. Protease inhibitor studies reinforced this contention showing the involvement of (a) serine protease(s) with trypsin-like activity in the activation of mosquito prophenoloxidase.

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Activation of pro-phenoloxidase by bacterial cell walls or β-1,3-glucans in plasma of the silkworm, Bombyx mori

Cited by 157 publications

References 16 publications

The Drosophila immune system detects bacteria through specific peptidoglycan recognition

The Drosophila immune system detects bacteria through specific peptidoglycan recognition

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

Studies on prophenoloxidase activation in the mosquito Aedes aegypti L.

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