Insect Biochemistry and Molecular Biology最新文献

{"title":"Genome editing in hymenoptera","authors":"Hamish A. Salvesen,&nbsp;Peter K. Dearden","doi":"10.1016/j.ibmb.2025.104300","DOIUrl":"10.1016/j.ibmb.2025.104300","url":null,"abstract":"<div><div>The application of genome editing tools in Hymenoptera has transformative potential for functional genetics and understanding their unique biology. Hymenoptera comprise one of the most diverse Orders of animals, and the development of methods for efficiently creating precise genome modifications could have applications in conservation, pest management and agriculture. To date, sex determination, DNA methylation, taste and smell sensory systems as well as phenotypic markers have been selected for gene editing investigations. From these data, insights into eusociality, the nature of haplodiploidy and the complex communication systems that Hymenoptera possess have provided an understanding of their evolutionary history that has led them to become so diverse and successful.</div><div>Insights from these functional genetics analyses have been supported by the ever-improving suite of CRIPSR tools and further expansion will allow more specific biological hypotheses to be tested and applications beyond the lab. Looking ahead, genome editing tools have potential for Hymenopteran applications in modifying biocontrol agents of agricultural pests and for use in managing invasive species through the development of technologies such as gene drives. This review provides accessibility to information regarding the status of Hymenopteran genome editing, intending to support the considered development of CRISPR tools in novel species as well as innovation and refinement of methods in species in which it has already been achieved.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"180 ","pages":"Article 104300"},"PeriodicalIF":3.2,"publicationDate":"2025-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143620319","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Functional analysis of the epsilon glutathione S-transferases in the adaptation of Spodoptera litura to xanthotoxin","authors":"Tianxiang Xiao ,&nbsp;Mengqing Deng ,&nbsp;Xiaodan Huang ,&nbsp;Wenxiu Wang ,&nbsp;Xiyue Xu ,&nbsp;Xinyu Zhao ,&nbsp;Jun Li ,&nbsp;Yingjie Jiang ,&nbsp;Bo Pan ,&nbsp;Ziyu He ,&nbsp;Zhiming Yang ,&nbsp;Zhongxiang Sun ,&nbsp;Kai Lu","doi":"10.1016/j.ibmb.2025.104299","DOIUrl":"10.1016/j.ibmb.2025.104299","url":null,"abstract":"<div><div>Through long-term coevolution with host plants, insects have evolved sophisticated detoxification systems to counteract plant secondary metabolites (PSMs). However, the precise mechanisms underlying these adaptations remain incompletely characterized. Our previous research identified epsilon glutathione <em>S</em>-transferases (GSTes) as critical mediators of xanthotoxin adaptation in <em>Spodoptera litura</em>, a model linear furanocoumarin. This study reveals that heterologous overexpression of five xanthotoxin-responsive GSTes in <em>Escherichia coli</em> significantly enhances bacterial tolerance to this PSM. Disk diffusion assays and metabolic studies demonstrated that both GSTe1 and GSTe16 mediate xanthotoxin adaptation via dual mechanisms involving antioxidant activity and catalytic metabolism. Fluorescent competitive binding experiments indicated that all five GSTes exhibit non-catalytic xanthotoxin sequestration capabilities. These <em>in vitro</em> observations were complemented by <em>in vivo</em> genetic manipulation of <em>GSTe16</em>, which exhibited the most potent defense activity against xanthotoxin. CRISPR/Cas9-mediated <em>GSTe16</em> knockout in <em>S. litura</em> significantly increased larval susceptibility to xanthotoxin, while transgenic <em>Drosophila melanogaster</em> overexpressing <em>GSTe16</em> showed enhanced tolerance to xanthotoxin. Furthermore, the endogenous biosynthesis of 20-hydroxyecdysone (20E) was provoked upon exposure to xanthotoxin, and 20E application enhanced the larval tolerance to xanthotoxin as well as the expression levels of <em>GSTe16</em>. Dual-luciferase reporter assays identified two functional <em>cis</em>-regulatory elements in the <em>GSTe16</em> promoter that facilitate transcriptional activation by the ecdysone receptor (EcR)/ultraspiracle (USP) heterodimer. Overall, this study elucidates the biochemical defense characteristics and transcriptional responses of GSTes to xanthotoxin in <em>S. litura</em>, providing novel insights into the counter-defense mechanisms of herbivorous insects against host plants.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"180 ","pages":"Article 104299"},"PeriodicalIF":3.2,"publicationDate":"2025-03-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143601209","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evolution of circadian clock and light-input pathway genes in Hemiptera","authors":"Vlastimil Smykal,&nbsp;Hisashi Tobita ,&nbsp;David Dolezel","doi":"10.1016/j.ibmb.2025.104298","DOIUrl":"10.1016/j.ibmb.2025.104298","url":null,"abstract":"<div><div>Circadian clocks are timekeeping mechanisms that help organisms anticipate periodic alterations of day and night. These clocks are widespread, and in the case of animals, they rely on genetically related components. At the molecular level, the animal circadian clock consists of several interconnected transcription-translation feedback loops. Although the clock setup is generally conserved, some important differences exist even among various insect groups. Therefore, we decided to identify <em>in silico</em> all major clock components and closely related genes in Hemiptera. Our analyses indicate several lineage-specific alterations of the clock setup in Hemiptera, derived from gene losses observed in the complete gene set identified in the outgroup, Thysanoptera, which thus presents the insect lineage with a complete clock setup. <em>Nilaparvata</em> and Fulgoroidea, in general, lost the (6–4)-photolyase, while all Hemiptera lost FBXL3, and several lineage-specific losses of dCRY and jetlag were identified. Importantly, we identified non-canonical splicing variants of <em>period</em> and <em>m-cry</em> genes, which might provide another regulatory mechanism for clock functioning. Lastly, we performed a detailed reconstruction of Hemiptera's light input pathway genetic repertoire and explored the horizontal gene transfer of cryptochrome-DASH from plant to <em>Bemisia</em>. Altogether, this inventory reveals important trends in clock gene evolution and provides a reference for clock research in Hemiptera, including several lineages of important pest species.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"180 ","pages":"Article 104298"},"PeriodicalIF":3.2,"publicationDate":"2025-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143584114","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pattern recognition, hemolymph protease-14 activation, and enhancement of lysozyme-mediated bacteria killing by soluble peptidoglycan recognition proteins in Manduca sexta","authors":"Chunxiang Hou ,&nbsp;Yang Wang ,&nbsp;Chao Xiong ,&nbsp;Udeshika Kariyawasam ,&nbsp;Tisheng Shan ,&nbsp;Michael R. Kanost ,&nbsp;Haobo Jiang","doi":"10.1016/j.ibmb.2025.104297","DOIUrl":"10.1016/j.ibmb.2025.104297","url":null,"abstract":"<div><div>Peptidoglycan recognition proteins (PGRPs) detect invading bacteria during insect immune responses, and some can damage bacterial cell walls. We previously produced <em>M. sexta</em> PGRPs 1–5, 12, and 13, and demonstrated that the PGRP repertoire in hemolymph preferentially detects <em>meso</em>-diaminopimelic acid-peptidoglycans (DAP-PGs). In this study, we found that adding DAP-PGs and PGRPs to larval hemolymph significantly enhanced prophenoloxidase activation beyond the sum of their individual effects. Lys-PG of <em>Micrococcus luteus</em> and PGRP4/5 also displayed the synergy, but Lys-PG of <em>Staphyloccous aureus</em> did not. Structural modeling and ligand docking supported the preferrential binding of DAP-PGs over Lys-PGs. DAP/Lys-PG, PGRP3s/3f/5/13N, and microbe binding protein activated hemolymph protease-14 (HP14), suggesting that these PGRPs initiate the serine protease system in the same way as PGRP1. Using fluorescein-labeled <em>M. luteus</em> peptidoglycan as a substrate, we detected increases in fluorescence signal caused by PGRP2, 4, 13N, 12e, and 3f, suggesting that these PGRPs have amidase activity for hydrolyzing peptidoglycan, which was enhanced by Zn²⁺ and decreased by EDTA. Spatial locations of the catalytic residues, Zn²⁺ ion, and scissile bond in the models of PGRP-peptidoglycan complexes explained some of the activity differences. PGRP2 and PGRP4 had the highest specific activity. Only PGRP4 (60 μg/ml) decreased <em>Bacillus megaterium</em> colony-forming units (CFU) compared to controls, whereas other PGRPs did not affect CFU numbers. A mixture of PGRP1−5 or 3s (2 μg/ml) and <em>Manduca</em> lysozyme (20 μg/ml) significantly reduced CFU compared to lysozyme alone, even for PGRPs without amidase activity. Scanning electron microscopy revealed that lysozyme caused structural damage to the bacterial cell walls, and when combined with PGRP2, this effect was enhanced. In summary, the soluble PGRPs preferentially recognize DAP-PGs, stimulate melanization via HP14, and enhance bacterial killing by lysozyme. Mechanisms for the amidase-independent bacterial killing by PGRPs and lysozyme require further exploration.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"180 ","pages":"Article 104297"},"PeriodicalIF":3.2,"publicationDate":"2025-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143584122","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Transcriptomic and proteomic analyses reveals the diverse venom composition of the spider Neoscona shillongensis","authors":"Wenhao Yin ,&nbsp;Yongming You ,&nbsp;Luke R. Tembrock ,&nbsp;Mengmeng Zhang ,&nbsp;Zhi Li ,&nbsp;Yulin Zheng ,&nbsp;Yu Zhao ,&nbsp;Zizhong Yang","doi":"10.1016/j.ibmb.2025.104289","DOIUrl":"10.1016/j.ibmb.2025.104289","url":null,"abstract":"<div><div><em>Neoscona shillongensis</em> (Araneidae), also known as the Shillong orb-weaving spider, is a species that constructs a typically shaped round web, is inactive during the daytime and comes out at dusk to forage, primarily preying on flying insects such as mosquitoes, flies, and moths. This spider serves as an important natural enemy of agricultural and forest pests. <em>Neoscona shillongensis</em> primarily uses its web to capture prey, but its venom also plays a crucial role in subduing and processing prey. To date, no research has been conducted on the composition of <em>N. shillongensis</em> venom. In This study, conducted high-throughput sequencing on the venom gland transcriptome and the venom gland extract proteome. A cDNA library of the venom gland tissue of <em>N. shillongensis</em> was constructed, yielding over 62 million reads, which were assembled into 90,481 sequences, predicting 171 toxin-like sequences, including 94 peptide toxins and 77 protein toxins. Furthermore, proteomic analyses of the venom gland extract samples identified 53 peptides and proteins, including 23 peptide toxins and 30 enzymes or proteins such as acetylcholinesterase, hyaluronidase, and astacin-like metalloproteases. The results revealed that the toxin composition of <em>N. shillongensis</em> is diverse and complex. This study provides essential baseline data for further research on the evolution and physiological activity of spider venom, as well as the potential development of pharmaceutical compounds therefrom.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"180 ","pages":"Article 104289"},"PeriodicalIF":3.2,"publicationDate":"2025-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143571886","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Membrane-bound sucrose hydrolase contributes to carbohydrate metabolism in Bombyx mori","authors":"Yanting Liang ,&nbsp;Yue Jin ,&nbsp;Yanyan Zhou,&nbsp;Jinsi Zhi,&nbsp;Huabing Wang","doi":"10.1016/j.ibmb.2025.104288","DOIUrl":"10.1016/j.ibmb.2025.104288","url":null,"abstract":"<div><div>Insects mainly rely on sucrase to hydrolyze sucrose into glucose and fructose, supplying carbon and energy for growth and development. Although soluble and membrane-associated sucrases have been identified in several insects, the physiological function of the membrane-bound sucrase remains unclear. Here, we performed a comprehensive analysis of the biochemical properties and physiological functions of the membrane-bound sucrase (BmSUH) in <em>Bombyx mori</em>. Immunofluorescence analysis revealed distinct localization patterns of BmSUH and another crucial sucrase, β-fructofuranosidase (BmSUC1) in the midgut. BmSUH was localized to the microvilli of columnar cells, while BmSUC1 was expressed in the cavities of goblet cells. In addition, the N-terminal transmembrane domain is crucial for membrane localization of BmSUH. We then verified that one of the positive selection sites, N326, is N-glycosylated and essential for the enzyme activity of BmSUH. CRISPR/Cas9-mediated knockout of BmSUH significantly reduced both membrane-associated and membrane-bound sucrase activity in the midgut, leading to decreased sucrose absorption from food. Transcriptome analysis further revealed the molecular mechanisms underlying the physiological function of BmSUH, with differentially expressed genes enriched in many pathways related to digestion, absorption, and metabolism of carbohydrates. These results highlight that BmSUH served as an essential sucrase involved in the digestive and metabolic processes. This study provides insight into the functional evolution of the membrane-bound sucrase and advances our understanding of sucrose utilization in lepidopteran insects.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"180 ","pages":"Article 104288"},"PeriodicalIF":3.2,"publicationDate":"2025-02-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143531036","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"N-alpha-acetyltransferase 40 modulates ecdysteroid action through chromatin accessibility changes near the promoters of 20-hydroxyecdysone response genes in Tribolium Castaneum TcA cells","authors":"Surjeet Kumar Arya,&nbsp;Subba Reddy Palli","doi":"10.1016/j.ibmb.2025.104285","DOIUrl":"10.1016/j.ibmb.2025.104285","url":null,"abstract":"<div><div>Changes in chromatin accessibility leading to altered gene expression play critical roles in cellular response to environmental signals. The function of N-alpha-acetyltransferase 40 (NAA40) in modulating chromatin accessibility and transcriptional regulation of 20-hydroxyecdysone (20E) response in <em>Tribolium castaneum</em> (TcA) cells was investigated. RNA interference (RNAi) was used to knockdown NAA40, and ATAC and RNA sequencing were used to examine changes in chromatin accessibility and gene expression in TcA cells exposed to 20E. ATAC-seq data revealed chromatin accessibility patterns between NAA40 knockdown and control cells exposed to 20E. Significant differences were detected in chromatin accessibility at transcription start sites (TSS) and promoter regions between dsNAA40 or dsGFP-treated cells exposed to 20E. Differential peak analysis identified many regions in the genome with altered chromatin accessibility upon NAA40 knockdown or 20E treatment, suggesting that NAA40 plays a critical role in 20E regulation of gene expression by modifying chromatin accessibility near the promoters of genes involved in 20E action. RNA sequence data analysis revealed changes in the expression of 20E response genes after NAA40 knockdown or 20E treatment. Comparison of ATAC-seq and RNA-seq data showed a correlation between chromatin accessibility and transcriptional changes of 20E response genes such as E74 and E75. Our results demonstrate that NAA40 affects chromatin dynamics and transcriptional regulation in modulating 20E response, increasing our understanding of the molecular mechanisms underlying the hormonal regulation of gene expression.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"179 ","pages":"Article 104285"},"PeriodicalIF":3.2,"publicationDate":"2025-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143476096","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A key amino acid substitution of vacuolar-type H+-ATPases A subunit (VATP-A) confers selective toxicity of a potential botanical insecticide, periplocoside P (PSP), in Mythimna separata and Spodoptera exigua","authors":"Xianxia Zhang ,&nbsp;Yayun Zuo ,&nbsp;Rui Liu ,&nbsp;Shuang Wen ,&nbsp;Yakun Pei ,&nbsp;Qin Zhao ,&nbsp;Baojun Shi ,&nbsp;Wenjun Wu ,&nbsp;Ding Li ,&nbsp;Zhaonong Hu","doi":"10.1016/j.ibmb.2025.104277","DOIUrl":"10.1016/j.ibmb.2025.104277","url":null,"abstract":"<div><div>Periplocosides, extracted from the root bark of <em>Periploca sepium</em>, are plant secondary compounds known to inhibit the V-ATPase enzyme in susceptible insect species, such as <em>Mythimna separata</em>. However, many species, including <em>Spodoptera exigua</em>, show resistance to these compounds. Previous studies identified the V-ATPase subunit A (VATP-A) in the midgut epithelium of <em>M. separata</em> as the putative target of periplocoside P (PSP), but the specific amino acids involved in this interaction remained unclear. In this study, we demonstrate the selective toxicity of PSP and its inhibition effect on V-ATPase. Molecular docking identified potential interactions between PSP and three amino acids (K85, R171, E199) in MsVATP-A, with <em>in vitro</em> binding assays revealing that K85 and R171 serve as the primary binding sites. Notably, sequence alignment revealed that R171 in sensitive species is substituted with K in resistant species. To investigate the functional implications of this substitution, we performed <em>in vitro</em> site-directed mutagenesis to exchange the corresponding amino acids between the VATP-A orthologs of <em>M. separata</em> and <em>S. exigua</em>. The R171K mutation in MsVATP-A reduced binding to PSP, while the K170R mutation in SeVATP-A enhanced it. Furthermore, <em>in vivo</em> genome editing in <em>Drosophila melanogaster</em>, a PSP-sensitive species, revealed that the R168K mutation conferred 15.78-fold resistance to PSP compared to the wild-type strain (<em>w</em>¹¹¹⁸). Our findings confirm the role of VATP-A as the target of PSP and elucidate the key amino acids influencing its insecticidal selectivity. This research enhances the understanding of the molecular interactions between natural compounds and insect targets, offering insights for the development of targeted pest control strategies.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"179 ","pages":"Article 104277"},"PeriodicalIF":3.2,"publicationDate":"2025-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143439591","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Modulation of peptidoglycan recognition protein expression alters begomovirus vectoring efficiency and fitness of Bemisia tabaci","authors":"Anupma Singh ,&nbsp;Rakesh V ,&nbsp;Yuvaraj Iyyappan ,&nbsp;Amalendu Ghosh","doi":"10.1016/j.ibmb.2025.104276","DOIUrl":"10.1016/j.ibmb.2025.104276","url":null,"abstract":"<div><div>Peptidoglycan recognition proteins (PGRPs) are evolutionarily conserved molecules. Their role in the immune response to invading pathogens makes them a natural target for viral defence study in a wide range of organisms. Silverleaf whitefly, <em>Bemisia tabaci</em> (Gennadius) (Hemiptera: Aleyrodidae) is one of the invasive insect pests and transmits begomoviruses in a circulative and persistent manner to vegetables, legumes, fibres and ornamentals. The virus entry, retention, circulation, and release process involve interactions with several proteins in <em>B. tabaci</em> and evade innate immunity to avoid the antiviral mechanisms. The present study investigated the role of <em>BtPGRP</em> in chilli leaf curl virus (ChiLCV, <em>Begomovirus capsica</em>) transmission by <em>B. tabaci</em>. Silencing of <em>BtPGRP</em> using double-stranded (ds) RNA led to the loss of innate immunity to ChiLCV resulting in increased virus titre in <em>B. tabaci</em>. Ds<em>BtPGRP</em> was orally administered to adults of <em>B. tabaci</em> at a concentration of 1, 3, and 5 μg/mL. The expression of <em>BtPGRP</em> was downregulated up to 4.67-fold. The virus titre in <em>B. tabaci</em> increased 90.05 times post-exposure to ds<em>BtPGRP</em> at 5 μg/mL. The test plants inoculated with ChiLCV by <em>dsBtPGRP</em>-exposed <em>B. tabaci</em> expressed severe curling symptoms with a higher virus load and transmission ratio than the control. Besides, the silencing of <em>BtPGRP</em> also induced up to 56.67% mortality in treated <em>B. tabaci</em>. The active site pocket of <em>BtPGRP</em> was found to interact directly with the ChiLCV-CP in computational analyses. Key residues of <em>BtPGRP</em>, including Tyr45, Asp84, His86, Trp87, and Asn119 exhibited critical interactions with the ChiLCV-CP. To our knowledge, this is the first report on the effect of <em>PGRP</em> silencing on ChiLCV acquisition and transmission efficiency and fitness of <em>B. tabaci</em> Asia II I.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"179 ","pages":"Article 104276"},"PeriodicalIF":3.2,"publicationDate":"2025-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143439594","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"What Drosophila can tell us about state-dependent peptidergic signaling in insects","authors":"Dick R. Nässel","doi":"10.1016/j.ibmb.2025.104275","DOIUrl":"10.1016/j.ibmb.2025.104275","url":null,"abstract":"<div><div>Plasticity in animal behavior and physiology is largely due to modulatory and regulatory signaling with neuropeptides and peptide hormones (collectively abbreviated NPHs). The NPHs constitute a very large and versatile group of signaling substances that partake at different regulatory levels in most daily activities of an organism. This review summarizes key principles in NPH actions in the brain and in interorgan signaling, with focus on <em>Drosophila</em>. NPHs are produced by neurons, neurosecretory cells (NSCs) and other endocrine cells in NPH-specific and stereotypic patterns. Most of the NPHs have multiple (pleiotropic) functions and target several different neuronal circuits and/or peripheral tissues. Such divergent NPH signaling ensures orchestration of behavior and physiology in state-dependent manners. Conversely, many neurons, circuits, NSCs, or other cells, are targeted by multiple NPHs. This convergent signaling commonly conveys various signals reporting changes in the external and internal environment to central neurons/circuits. As an example of wider functional convergence, 26 different <em>Drosophila</em> NPHs act at many different levels to regulate food search and feeding. Convergence is also seen in hormonal regulation of peripheral functions. For instance, multiple NPHs target renal tubules to ensure osmotic homeostasis. Interestingly, several of the same osmoregulatory NPHs also regulate feeding, metabolism and stress. However, for some NPHs the cellular distribution and functions suggests multiple unrelated functions that are restricted to specific circuits. Thus, NPH signaling follows distinct patterns for each specific NPH, but taken together they form overlapping networks that modulate behavior and physiology.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"179 ","pages":"Article 104275"},"PeriodicalIF":3.2,"publicationDate":"2025-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143432064","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}