GC-MS-based metabonomic analysis of silkworm haemolymph reveals four-stage metabolic responses to nucleopolyhedrovirus infection.

Silkworm, Bombyx mori, an economically significant insect, plays a crucial role in silk production. However, silkworm breeding is highly susceptible to various pathogens, particularly the Bombyx mori nucleopolyhedrovirus (BmNPV), which poses a serious threat. Recent metabonomic studies have provided insights into the metabolic changes associated with BmNPV infection.

Integrating portable X-ray fluorescence site survey and ArcGIS models for rapid risk assessment and mitigation strategies at an abandoned arsenic mine site: a case study.

Australia's metalliferous abandoned mine sites (MAMSs), pose tangible threats to the environment and human health. To address these concerns, our study utilised state-of-the-art handheld XRF technology to conduct a real-time assessment of the Mole River arsenic mine site. The data revealed notably elevated levels of arsenic and manganese, with the southeast corner of the site identified as a contaminant hotspot.

The silk gland proteome of Stenopsyche angustata provides insights into the underwater silk secretion.

Caddisworms (Trichoptera) spin adhesive silks to construct a variety of underwater composite structures. Many studies have focused on the fibroin heavy chain of caddisworm silk and found that it contains heavy phosphorylation to maintain a stable secondary structure. Besides fibroins, recent studies have also identified some new silk proteins within caddisworm silk.

The tissue-specific expression of silkworm cuticle protein gene ASSCP2 is mediated by the Sox-2 transcription factor.

The silk gland of silkworm is a unique organ in which silk proteins are synthesized, secreted, and transformed into fibers. The anterior silk gland (ASG) is located at the end of the silk gland, and is thought to be involved in silk fibrosis. In our previous study, a cuticle protein, ASSCP2, was identified.

Identification and functional study of fhx-L1, a major silk component in Bombyx mori.

The silkworm cocoon was composed of fibroins, sericins, protease inhibitors, and proteins of unknown function. In this study, we focused on fhx-L1 (fibrohexamerin-like1), which was the homolog of fibroin fhx (fibrohexamerin). We identified 154 fhx family genes in 44 Lepidoptera insects, and seven fhx-Ls were found in Bombyx mori.

Multi-Omics Integration to Reveal the Mechanism of Sericin Inhibiting LPS-Induced Inflammation.

Sericin is a natural protein with high application potential, but the research on its efficacy is very limited. In this study, the anti-inflammatory mechanism of sericin protein was investigated. Firstly, the protein composition of sericin extracts was determined by Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS).

Insights into the structure and composition of mineralized hard cocoons constructed by the oriental moth, Monema (Cnidocampa) flavescens Walker.

Animals widely use minerals and organic components to construct biomaterials with excellent properties, such as teeth, bones, molluscan shells and eggshells. The larvae of the oriental moth, Monema (Cnidocampa) flavescens Walker, secrete silk proteins that combine closely with calcareous minerals to construct a hard cocoon, which is completely different from the mineral-free Bombyx mori cocoon. The cocoons of oriental moths are likely to be the hardest among the cocoons constructed by insect species.

Antimicrobial components in the cocoon silk of silkworm, Bombyx mori.

Silkworm spins silk fibers to make the cocoon to protect the pupa from predators and pathogenic microbes. To understand the defense mechanism of the cocoon, many antimicrobial proteins are currently identified. The functionality of these proteins is studied, including protease inhibitors and seroins.

Transcriptional Activation of Ecdysone-Responsive Genes Requires H3K27 Acetylation at Enhancers.

The steroid hormone ecdysone regulates insect development via its nuclear receptor (the EcR protein), which functions as a ligand-dependent transcription factor. The EcR regulates target gene expression by binding to ecdysone response elements (EcREs) in their promoter or enhancer regions. Its role in epigenetic regulation and, particularly, in histone acetylation remains to be clarified.

Identification and characterization of sericin5 reveals non-cocoon silk sericin components with high β-sheet content and adhesive strength.

Sericins are glue proteins on the surface of silk fibers. Four sericins have been characterized in silkworm, namely sericin1 (Ser1), sericin2 (Ser2), sericin3 (Ser3), and sericin4 (Ser4). In this study, we report a novel sericin, sericin5 (Ser5), which exists only in non-cocoon silk.

Chitin and cuticle proteins form the cuticular layer in the spinning duct of silkworm.

Chitin is found in the exoskeleton and peritrophic matrix of arthropods, but recent studies have also identified chitin in the spinning duct of silk-spinning arthropods. Here, we report the presence and function of chitin and cuticle proteins ASSCP1 and ASSCP2 in the spinning duct of silkworm. We show that chitin and these proteins are co-located in the cuticular layer of the spinning duct.

Fiber Formation and Mechanical Properties of Silk Are Regulated by Vacuolar-Type ATPase.

The mechanism of silk fiber formation in silkworms, , is of particular scientific interest because it is closely related to the mechanical properties of silk fibers. However, there are still substantial knowledge gaps in understanding the details of this mechanism. Studies have found a pH gradient in the silk gland of silkworms.

Identification of N-linked Glycoproteins in Silkworm Serum Using Con A Lectin Affinity Chromatography and Mass Spectrometry.

Glycosylation is one of the most common post-translational modifications to occur during protein biosynthesis, but remains poorly understood in insects. In this study, we collected serum proteins from two silkworm developmental stages, namely day 7 of the fifth instar larval stage and day 2 of the pupal stage. Results of SDS-PAGE and periodic acid-Schiff staining revealed that most serum proteins with high abundance were putative glycoproteins.

Haplotype-resolved genome of diploid ginger (Zingiber officinale) and its unique gingerol biosynthetic pathway.

Ginger (Zingiber officinale), the type species of Zingiberaceae, is one of the most widespread medicinal plants and spices. Here, we report a high-quality, chromosome-scale reference genome of ginger 'Zhugen', a traditionally cultivated ginger in Southwest China used as a fresh vegetable, assembled from PacBio long reads, Illumina short reads, and high-throughput chromosome conformation capture (Hi-C) reads. The ginger genome was phased into two haplotypes, haplotype 1 (1.

Adhesive property and mechanism of silkworm egg glue protein.

Egg glue proteins (EGPs) are produced by female insects, which can make the eggs firmly attached to the oviposition sites, not affected by wind and rain. Although EGPs are widespread in insects, they have been rarely characterized in molecular detail. Here, the full-length sequence and secondary structure of silkworm EGP is reported.

The mutation of SPI51, a protease inhibitor of silkworm, resulted in the change of antifungal activity during domestication.

Domestication of silkworm has led to alterations in various gene expression patterns. For instance, many protease inhibitors were significantly downregulated in the domestic silkworm cocoon compared to its wild progenitor. Considering that SPI51 is the most abundant protease inhibitor in silkworm cocoons, herein, we compared the gene structures and sequences of SPI51 from B.

Five Silkworm 30K Proteins Are Involved in the Cellular Immunity against Fungi.

Background: 30K proteins are a major group of nutrient storage proteins in the silkworm hemolymph. Previous studies have shown that 30K proteins are involved in the anti-fungal immunity; however, the molecular mechanism involved in this immunity remains unclear.

Methods: We investigated the transcriptional expression of five 30K proteins, including BmLP1, BmLP2, BmLP3, BmLP4, and BmLP7.

Antibacterial Mechanism of Silkworm Seroins.

Seroin 1 and seroin 2 are abundant in silkworm cocoon silk and show strong antibacterial activities, and thus are thought to protect cocoon silk from damage by bacteria. In this study, we characterized the expression pattern of silkworm seroin 3, and found that seroin 3 is synthesized in the female ovary and secreted into egg to play its roles. After being infected, seroin 1, 2, and 3 were significantly up-regulated in the silkworm.

Comparative Fecal Metabolomes of Silkworms Being Fed Mulberry Leaf and Artificial Diet.

Metabonomics accurately monitors the precise metabolic responses to various dietary patterns. Metabolic profiling allows simultaneous measurement of various fecal metabolites whose concentrations may be affected by food intake. In this study, we analyzed the fecal metabolomes of silkworm () larvae reared on fresh mulberry leaves and artificial diets.

Ultrafine and High-Strength Silk Fibers Secreted by Bimolter Silkworms.

Ultrafine fibers are widely employed because of their lightness, softness, and warmth retention. Although silkworm silk is one of the most applied natural silks, it is coarse and difficult to transform into ultrafine fibers. Thus, to obtain ultrafine high-performance silk fibers, we employed anti-juvenile hormones in this study to induce bimolter silkworms.

Synthesis, secretion, and antifungal mechanism of a phosphatidylethanolamine-binding protein from the silk gland of the silkworm Bombyx mori.

A silkworm cocoon contains several antimicrobial proteins such as protease inhibitors and seroins to provide protection for the enclosed pupa. In this study, we identified a new Bombyx mori phosphatidylethanolamine-binding protein (BmPEBP) with antimicrobial activity in the cocoon silk using semi-quantitative and quantitative RT-PCR, western blotting, and immunofluorescence. The results indicated that BmPEBP was synthesized in the middle silk gland and secreted into the sericin layer of the cocoon silk.