In Vivoandin VitroInteractions of theBombyx moriChymotrypsin Inhibitor b1 withEscherichia coli

He, Ningjia; Aso, Yoichi; Fujii, Hiroshi; Banno, Yutaka; Yamamoto, Kohji

doi:10.1271/bbb.68.835

Cited by 14 publications

(6 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The activation of prophenoloxidase (proPO) is catalyzed by serine proteases, which are suppressed by CI‐13a, CI‐13b and CI‐13c (Aso et al ., 1994). It is speculated that CI‐b1 is a mediator that scavenges intruding bacteria (He et al ., 2004). CI‐8 in the hemolymph can inhibit the activity of proteases in digestive juices, and there are proteinaceous factors involved in the uptake of CI‐8 into the midgut through the membranes (Shirai et al ., 1997; Ueno et al , 2006).…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of the immune response of the silkworm infected by Escherichia coli and Bacillus bombyseptieus

et al. 2012

View full text Add to dashboard Cite

The silkworm, Bombyx mori, is an economically important insect with a 5 000‐year history of domestication. During evolution, the silkworm has developed highly effective defenses against invasion and parasitization by microorganisms. In this study, two microorganisms Escherichia coli and Bacillus bombyseptieus were orally infected to silkworm larvae. After infection with E. coli and B. bombyseptieus for 24 h, we investigated the polypeptide changes in the hemolymph, midgut and integument using two‐dimensional gel electrophoresis and matrix‐assisted laser desorption ionization time of flight mass spectrometry. Forty‐seven differentially expressed proteins were identified in these tissues. They belonged to a variety of functional classes, including immune proteins, metabolic proteins and structural proteins. Compared with controls, E. coli‐infected silkworms showed 21 up‐regulated proteins, 25 down‐regulated proteins and lost one protein. After infection with B. bombyseptieus, silkworms showed 15 up‐regulated proteins, 27 down‐regulated proteins, lost three proteins and retained two proteins unchanged. We speculate that all these proteins may play a role in the silkworm immune response, although it is unclear why and how the two kinds of bacteria can so markedly alter expression of these proteins. These results offer valuable insights for measuring the proteomic responses of the silkworm innate immune mechanism.

show abstract

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of the immune response of the silkworm infected by Escherichia coli and Bacillus bombyseptieus

et al. 2012

View full text Add to dashboard Cite

show abstract

“…The larvae of the silkmoth were exposed to UV‐B at 50 mJ/cm 2 and, at 8 h post‐treatment, fat bodies were dissected on ice from larvae and stored at −80 °C until use. Injection of bacteria ( E. coli ) corresponding to 4 × 10 7 cells per silkmoth larva was performed in accordance with a previously published method (He et al ., 2004).…”

Section: Methodsmentioning

confidence: 99%

Characterization of an omega-class glutathione S-transferase in the stress response of the silkmoth

Yamamoto

Teshiba

Shigeoka

et al. 2011

Insect Molecular Biology

View full text Add to dashboard Cite

The glutathione S-transferase (GST) superfamily is involved in detoxification of various xenobiotics. Using real-time PCR, mRNA encoding an omega-class GST of Bombyx mori (bmGSTO) was shown to be induced after exposure to various environmental stresses. A soluble form of recombinant protein (rbmGSTO) was functionally overexpressed in Escherichia coli cells and purified to homogeneity. Cys 38 and Pro 39 were found to be highly conserved in omega-class GSTs, and their roles were investigated by site-directed mutagenesis/kinetic analysis. Mutations of Cys 38 and Pro 39 residues affected the catalytic efficiency of enzymes, indicating that the presence of Cys 38 and Pro 39 residues is important for bmGSTO activity. Thus, bmGSTO could contribute to increasing the environmental stress resistance of lepidopteran insects.

show abstract

“…CI-13 of kunitz family exists in the active ingredient of phenoloxidase precursor activation [28]. CI-b1 of kunitz family binds to LPS and scavenge intruding bacteria through interacting with lipopolysaccharides (LPS) [29]. CI-8 of serpin family has receptor protein in the midgut and shows inhibitory activity to protease in the digestive juice [24].…”

Section: Introductionmentioning

confidence: 99%

Genome-Wide Identification and Immune Response Analysis of Serine Protease Inhibitor Genes in the Silkworm, Bombyx mori

et al. 2012

View full text Add to dashboard Cite

In most insect species, a variety of serine protease inhibitors (SPIs) have been found in multiple tissues, including integument, gonad, salivary gland, and hemolymph, and are required for preventing unwanted proteolysis. These SPIs belong to different families and have distinct inhibitory mechanisms. Herein, we predicted and characterized potential SPI genes based on the genome sequences of silkworm, Bombyx mori. As a result, a total of eighty SPI genes were identified in B. mori. These SPI genes contain 10 kinds of SPI domains, including serpin, Kunitz_BPTI, Kazal, TIL, amfpi, Bowman-Birk, Antistasin, WAP, Pacifastin, and alpha-macroglobulin. Sixty-three SPIs contain single SPI domain while the others have at least two inhibitor units. Some SPIs also contain non-inhibitor domains for protein-protein interactions, including EGF, ADAM_spacer, spondin_N, reeler, TSP_1 and other modules. Microarray analysis showed that fourteen SPI genes from lineage-specific TIL family and Group F of serpin family had enriched expression in the silk gland. The roles of SPIs in resisting pathogens were investigated in silkworms when they were infected by four pathogens. Microarray and qRT-PCR experiments revealed obvious up-regulation of 8, 4, 3 and 3 SPI genes after infection with Escherichia coli, Bacillus bombysepticus, Beauveria bassiana or B. mori nuclear polyhedrosis virus (BmNPV), respectively. On the contrary, 4, 11, 7 and 9 SPI genes were down-regulated after infection with E. coli, B. bombysepticus, B. bassiana or BmNPV, respectively. These results suggested that these SPI genes may be involved in resistance to pathogenic microorganisms. These findings may provide valuable information for further clarifying the roles of SPIs in the development, immune defence, and efficient synthesis of silk gland protein.

show abstract

In Vivoandin VitroInteractions of theBombyx moriChymotrypsin Inhibitor b1 withEscherichia coli

Cited by 14 publications

References 23 publications

Proteomic analysis of the immune response of the silkworm infected by Escherichia coli and Bacillus bombyseptieus

Proteomic analysis of the immune response of the silkworm infected by Escherichia coli and Bacillus bombyseptieus

Characterization of an omega-class glutathione S-transferase in the stress response of the silkmoth

Genome-Wide Identification and Immune Response Analysis of Serine Protease Inhibitor Genes in the Silkworm, Bombyx mori

Contact Info

Product

Resources

About