Insect Biochemistry and Molecular Biology最新文献

{"title":"The powers and perils of bug editing","authors":"Helena Araujo","doi":"10.1016/j.ibmb.2024.104253","DOIUrl":"10.1016/j.ibmb.2024.104253","url":null,"abstract":"<div><div>Triatomine insects of the Hemiptera order are vectors of the neglected Chagas disease, that inflicts a great health burden in the Americas. Vector control has been recognized as a fundamental aspect to fight disease spread. However, besides the use of insecticides, no transgenic or gene editing tools have been developed for these insects, limiting the widespread use of biological control strategies. Here I present a personal account in trying to develop gene editing tools for triatomines. I highlight the major challenges we have faced, the efforts we have made to overcome these obstacles, and the hurdles that still lie ahead. I deliver no magic path to guide you through the perilous land of kissing bug gene editing but rather lay down a few rules we have learned that may help ease your journey.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"177 ","pages":"Article 104253"},"PeriodicalIF":3.2,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143178220","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":"Osmoregulation by sucrose isomerization in the phloem-feeding whitefly Bemisia tabaci involves members of the glycoside hydrolase family 13","authors":"Dor Wintraube ,&nbsp;Yonatan Sadeh ,&nbsp;Ofer Aidlin-Harari ,&nbsp;Yehudit Amor ,&nbsp;Shai Morin ,&nbsp;Osnat Malka","doi":"10.1016/j.ibmb.2025.104266","DOIUrl":"10.1016/j.ibmb.2025.104266","url":null,"abstract":"<div><div>A phloem-sap based diet requires unique enzymatic skills for regulating the osmotic pressure differences in the gut lumen between the sucrose-rich ingested sap and the body fluids, which can lead to desiccation and death. In the phloem-feeding whitefly <em>Bemisia tabaci</em>, members of the glycoside hydrolase family 13 (GH13) are likely to play a critical role in mitigating this risk by oligomerizing and isomerizing the products of sucrose hydrolysis. So far, however, the identities of the family members acting as sucrose isomerases (mainly isomerizing trehalulose) remain unknown. In this study, we focused on four putative sucrose isomerase coding genes of <em>B. tabaci</em> that belong to the GH13 family. The four coding genes were selected based on their phylogeny, expression patterns, and motif analyses. We used artificial diets of sucrose and dsRNA to knockdown the expression of each of the target genes and analyzed the sugar composition of the secreted honeydew. We found that in all cases, gene silencing resulted in a significant reduction of the fractions of trehalulose accompanied by an increase in the fractions of the trisaccharide melezitose, suggesting that the insects attempt to compensate for the inability to isomerize sucrose by synthesizing oligosaccharides. In addition, we found that the downregulation of the target genes also resulted in a significant increase in the mortality rates of the silenced insects and a significant delay in the development of their progeny. Taken together, these findings demonstrate the importance of the osmoregulation-by-isomerization strategy in <em>B. tabaci.</em></div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"178 ","pages":"Article 104266"},"PeriodicalIF":3.2,"publicationDate":"2025-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143073002","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":"Peroxiredoxin 6 is essential for the posttranslational activation of xanthine dehydrogenase in the uric acid synthesis of Bombyx mori","authors":"Tsuguru Fujii ,&nbsp;Masato Hino ,&nbsp;Toshiaki Fujimoto ,&nbsp;Kohei Kakino ,&nbsp;Yu Kaneko ,&nbsp;Hiroaki Abe ,&nbsp;Jae Man Lee ,&nbsp;Takahiro Kusakabe ,&nbsp;Toru Shimada","doi":"10.1016/j.ibmb.2025.104264","DOIUrl":"10.1016/j.ibmb.2025.104264","url":null,"abstract":"<div><div>We identified a novel mutant of <em>Bombyx mori</em>, designated as male-absent oily (genetic symbol: <em>om</em>). The larval integument of this mutant is translucent due to a lack of uric acid in the integument. This mutation is Z-linked, and as mutant females are infertile, it is impossible to obtain <em>om</em> homozygous males. Using positional cloning combined with RNA-seq analysis, we identified a 1-bp deletion in the <em>B. mori peroxiredoxin 6</em> (<em>BmPrx6</em>) gene. CRISPR/Cas9 knockout of <em>BmPrx6</em> resulted in a translucent larval integument, indicating <em>BmPrx6</em> as the causative gene for the <em>om</em> locus. Xanthine dehydrogenase (XDH)/xanthine oxidase (XO) is a key enzyme for uric acid synthesis. Injection of bovine XO into <em>om</em> mutants rescued the translucent phenotype, indicating that <em>om</em> is a mutant with defective XDH activity. To investigate XDH in <em>B. mori</em>, we generated a FLAG-tagged XDH gene using the CRISPR/Cas9 knock-in approach. Western blot analysis of XDH in <em>om</em> mutants revealed that <em>BmPrx6</em> is crucial for the posttranslational activation of XDH. The role of <em>BmPrx6</em> in regulating XDH activity is discussed.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"178 ","pages":"Article 104264"},"PeriodicalIF":3.2,"publicationDate":"2025-01-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143073004","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":"Bicarbonate, calcium ions, hydrogen peroxide and trypsin modulate activation of Anopheles gambiae sperm motility and protein tyrosine phosphorylation","authors":"Vincent O. Nyasembe ,&nbsp;Claire E. Schregardus ,&nbsp;Priscila Bascunan ,&nbsp;Catherine M. Steele ,&nbsp;Mark Q. Benedict ,&nbsp;Ellen M. Dotson","doi":"10.1016/j.ibmb.2025.104265","DOIUrl":"10.1016/j.ibmb.2025.104265","url":null,"abstract":"<div><div>With the increasing concern of potential loss of transgenic mosquitoes which are candidates as new tools for mosquito-borne disease control, methods for cryopreservation are actively under investigation. Methods to cryopreserve <em>Anopheles gambiae</em> sperm have recently been developed, but there are no artificial insemination or <em>in vitro</em> fertilization tools available. As a step to achieve this, we sought to identify a suitable medium for <em>in vitro</em> incubation of <em>An. gambiae</em> sperm and to tease out critical components that are involved in the sperm motility activation process. Using two cell viability assays, we identified the Biggers-Whitten-Whittingham (BWW) medium as suitable for <em>in vitro</em> incubation of <em>An. gambiae</em> sperm isolated from testes. We then modified the medium for motility assays by testing different HCO₃⁻ and Ca²⁺ concentrations. Our results show that there is an HCO₃⁻ and Ca²⁺ concentration-dependent activation of <em>An. gambiae</em> sperm motility. We further demonstrated that H₂O₂ can be produced by the testes <em>in vitro</em> and that the addition of 5.3 μM of H₂O₂ to the medium improves sperm motility and increases protein tyrosine phosphorylation in <em>An. gambiae</em>. Finally, we show a dose-dependent activation of sperm motility by the addition of trypsin to the medium and more than a 2-fold increase in sperm motility when modified BWW (mBWW) medium is supplemented with H₂O₂ and trypsin. Our <em>in vitro</em> results suggest that protein tyrosine phosphorylation, intracellular ionic influx, intrinsic production of H₂O₂ and trypsin-like proteases play a vital role in signal transduction that leads to the activation of <em>An. gambiae</em> sperm motility.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"178 ","pages":"Article 104265"},"PeriodicalIF":3.2,"publicationDate":"2025-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143062781","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":"BarH1 regulates the expression of conserved odorant-binding protein 22 from Dastarcus helophoroides","authors":"Rui-Nan Yang ,&nbsp;Dong-Zhen Li ,&nbsp;Ao Liu ,&nbsp;Yi Wei ,&nbsp;Rui-Lin Zhang ,&nbsp;Hazem Abdelnabby ,&nbsp;Man-Qun Wang","doi":"10.1016/j.ibmb.2025.104263","DOIUrl":"10.1016/j.ibmb.2025.104263","url":null,"abstract":"<div><div>Chemical signals are pivotal in establishing tritrophic interactions among host plants, herbivorous insects, and natural enemies. Previous studies have shown that evolutionarily conserved MaltOBPs in <em>Monochamus alternatus</em> and DhelOBPs in <em>Dastarcus helophoroides</em> contribute to the establishment of pine -pest - natural enemy tritrophic interactions by recognizing the same volatile emitted by the host during crucial developmental stages. We hypothesized that the transcriptional regulatory mechanisms of evolutionarily conserved OBPs respectively from pests and enemies are similar. In this study, we identified the promoter region of <em>DhelOBP22</em> through chromosome walking and discovered that transcription factor BarH1, which have been proved to regulate the expression of MaltOBP19 in <em>M. alternatus</em>, regulates the expression of DhelOBP22 by binding to its promoter region, as evidenced by dual-luciferase assays and electrophoretic mobility shift assay (EMSA). When the BarH1 gene was silenced using RNAi, the expression of DhelOBP22 was inhibited, leading to the disappearance of the attracted behavior of mated female <em>D. helophoroides</em> adults towards camphene. This study underscores that conserved transcriptional regulation mechanisms play a role in regulating the expression of evolutionarily conserved OBPs respectively from herbivores and natural enemies.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"178 ","pages":"Article 104263"},"PeriodicalIF":3.2,"publicationDate":"2025-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143062713","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":"Pioneering contributors to arthropod cuticle research","authors":"Subbaratnam Muthukrishnan","doi":"10.1016/j.ibmb.2024.104213","DOIUrl":"10.1016/j.ibmb.2024.104213","url":null,"abstract":"","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"175 ","pages":"Article 104213"},"PeriodicalIF":3.2,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142643311","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":"Lipophorin receptor knockdown reduces hatchability of kissing bug Rhodnius prolixus eggs","authors":"Alessa Macedo-Silva ,&nbsp;Thamara Rios ,&nbsp;Isabela Ramos ,&nbsp;David Majerowicz","doi":"10.1016/j.ibmb.2024.104221","DOIUrl":"10.1016/j.ibmb.2024.104221","url":null,"abstract":"<div><div>Lipophorin is the primary lipoprotein present in the hemolymph of insects, responsible for the lipids' transport between organs. It interacts with specific sites on cell membranes in an essential process for transferring lipids. The lipophorin receptor is the protein responsible for the interaction between lipophorin and cell membranes. In the kissing bug <em>Rhodnius prolixus</em>, much information on the interaction of lipophorin with organs is available. However, molecular data on the lipophorin receptor and its functions is still needed. Here, we explored lipophorin receptor gene expression and functions using a functional genomics approach. The <em>R. prolixus</em> genome encodes seven genes from the low-density lipoprotein receptor family, including a single ortholog of the lipophorin receptor. All organs analyzed (anterior and posterior midguts, fat body, ovaries, and flight muscle) expressed this gene. In the fat body, blood-feeding strongly reduced lipophorin receptor gene expression. Lipophorin receptor knockdown by RNA interference delayed egg laying and reduced the triacylglycerol in laid eggs without altering lipid stores in the fat body or lipid levels in the hemolymph. In the ovaries, lipophorin receptor knockdown reduces the expression of acetyl-CoA carboxylase and a fatty acid synthase while altered the gene expression profile in the fat body, causing an increase in the expression of carnitine palmitoyltransferase 1 and a reduction in Brummer lipase and vitellogenin 2. RNA interference treatment reduced the hatching of the eggs, causing the collapse and darkening of the laid eggs, in addition to the hatching of deformed first-stage nymphs. Furthermore, the structure of the chorion showed distortions in patterns and cracks and reduced hydrocarbon levels. These results show that the lipophorin receptor alone is not essential for lipid physiology in <em>R. prolixus</em>. However, this protein plays a fundamental role in the viability of eggs and, consequently, in insect reproduction.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"176 ","pages":"Article 104221"},"PeriodicalIF":3.2,"publicationDate":"2024-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142715097","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":"Structural characterization and proteomic profiling of oviposition secretions across three rice planthopper species","authors":"Jia-Bao Lu ,&nbsp;Peng-Peng Ren ,&nbsp;Ying Tian ,&nbsp;Yan-Yan Yang ,&nbsp;Qing-Kai Feng ,&nbsp;Xiao-Ya Zhang ,&nbsp;Fang He ,&nbsp;Hai-Jian Huang ,&nbsp;Jian-Ping Chen ,&nbsp;Jun-Min Li ,&nbsp;Chuan-Xi Zhang","doi":"10.1016/j.ibmb.2024.104220","DOIUrl":"10.1016/j.ibmb.2024.104220","url":null,"abstract":"<div><div>Insect oviposition secretions play crucial roles during the reproductive process, yet systematic studies on their structural characterization and protein compositions remain limited. This study investigated the oviposition secretions of three major rice pests: the brown planthopper (<em>Nilaparvata lugens</em>, BPH), small brown planthopper (<em>Laodelphax striatella</em>, SBPH), and white-backed planthopper (<em>Sogatella furcifera</em>, WBPH). Ultrastructural observation revealed differences in the oviposition secretions of them. The eggs of BPH and SBPH were adhered to rice tissue by abundant secretions, while WBPH eggs were embedded deeper within the leaf sheath with less secretions. Proteomic analysis identified 111, 98, and 66 oviposition secretion proteins (OSPs) in BPH, SBPH, and WBPH, respectively. 4 common protein subgroups were shared among them, along with varying numbers of shared subgroups between species pairs. Notably, the majority of OSPs were exclusively found in one species, indicating the existence of both similar and specialized functions unique to each planthopper species. The functions of 4 uncharacterized OSPs (Nl.chr07.0363, Nl.chr12.078, Nl.chr11.716, Nl.scaffold.0714) that were uniquely identified in the BPH were studied by maternal RNAi. Downregulation of each of these 4 protein-coding genes led to a significant decrease in egg production and hatchability. Moreover, knockdown of <em>Nl.chr12.078</em> or <em>Nl.chr07.0363</em> also disrupt the secretory function of the lateral oviduct. In conclusion, this study provides insights into the structural characteristics and protein components of the oviposition secretions of BPH, SBPH, and WBPH, which could serve as potential targets for RNAi-based pest control and lay a foundation for future studies on insect-plant interactions mediated by oviposition secretions.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"176 ","pages":"Article 104220"},"PeriodicalIF":3.2,"publicationDate":"2024-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142699016","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":"The immune function of thioester-containing proteins in typical invertebrate disease vectors","authors":"Qianqian Zhang ,&nbsp;Xia Zhou ,&nbsp;Tingting Feng ,&nbsp;Hao Tong ,&nbsp;Jun Wang ,&nbsp;Jianfeng Dai","doi":"10.1016/j.ibmb.2024.104218","DOIUrl":"10.1016/j.ibmb.2024.104218","url":null,"abstract":"<div><div>Disease vectors, such as arthropods, primarily rely on innate immunity to counteract pathogen invasions, typically through the recognition and binding of pathogen-associated molecular patterns (PAMPs) by the host's pattern recognition receptors (PRRs). As a conserved immune effector gene family from insects to mammals, the complement system may play an essential role in combating pathogenic microorganisms. In arthropods, the complement proteins are often referred to as thioester-containing proteins (TEPs) because thioester motifs are one of the essential functional domains of the first proteins characterized within the C3 and A₂M family. TEPs mainly function as specialized PRRs in sensing and binding to pathogens or their components. This paper presents a comprehensive review of the common domain and functions of TEPs in major disease vectors, in particular the specific decision-making ones expressed by <em>Arthropoda</em> (medical arthropods) and <em>Mollusca</em> (<em>Biomphalaria glabrata</em>) after pathogen infections. The relationship between the structure and antibacterial/antiviral activities of TEPs would further our understandings on the mechanisms governing the initiation of innate immune responses in typical disease vectors.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"176 ","pages":"Article 104218"},"PeriodicalIF":3.2,"publicationDate":"2024-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142694939","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":"Suppression of the H3K27me3 demethylase disrupts diapause formation in mosquito Culex pipiens","authors":"Xueyan Wei ,&nbsp;Prabin Dhungana ,&nbsp;Kaylah Callender ,&nbsp;Berhanu Zewde ,&nbsp;Fu Chen ,&nbsp;Sung Joon Kim ,&nbsp;Cheolho Sim","doi":"10.1016/j.ibmb.2024.104216","DOIUrl":"10.1016/j.ibmb.2024.104216","url":null,"abstract":"<div><div>Diapause (D) is a hormonally controlled alternative developmental pathway that allows mosquitoes to survive harsh winter conditions. Key characteristics of mosquito diapause include elevated lipid storage, enhanced stress and cold endurance, and extended longevity. These phenotypic changes are often associated with dynamic alterations in the transcriptome and epigenome. In our previous study, we identified significantly lower H3K27me2 levels in the fat body (FB) of diapausing <em>Culex pipiens</em>. However, the specific roles of the repressive H3K27 methylation marks in mosquito diapause have not been investigated. In the present study, we employed the effective histone lysine demethylase inhibitor GSK-J4 to assess the functions of H3K27me3 levels in the fat body on diapause initiation and phenotypes in <em>Cx. pipiens</em>. Results from solid-state NMR (ssNMR), Fourier-transform infrared spectroscopy (FTIR), and biochemical assays suggest that elevated H3K27me3 levels via GSK-J4 inhibition led to disrupted accumulation of lipids and glycogen in diapausing mosquitoes. GSK-J4 treatment also increased the mortality rate, resulting in lower survivability in treated mosquitoes. Together, these findings propose a crucial role for H3K27me3 in diapause formation, particularly related to energy metabolism. Our results provide a potential target for novel vector control strategies for this species.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"176 ","pages":"Article 104216"},"PeriodicalIF":3.2,"publicationDate":"2024-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142692272","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}