PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Genome, Insect”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 685 records · Page 38Linked to original sources

A cellular Drosophila melanogaster protein with similarity to baculovirus F envelope fusion proteins.

Baculovirus F (fusion) proteins are found in the envelopes of budded virions. Recently a Drosophila melanogaster gene (CG4715) that encodes a protein with sequence similarity to baculovirus F proteins was discovered. To examine similarities and differences with baculovirus F proteins, we cloned the D. melanogaster cellular F (Dm-cF) protein gene and analyzed Dm-cF expression and localization. The predicted Dm-cF protein sequence lacks a furin cleavage site, and transiently expressed Dm-cF showed no protein cleavage and no detectable membrane fusion activity. In cell localization studies, transiently expressed Dm-cF was localized to intracellular organelles in D. melanogaster S2 cells, unlike baculovirus F proteins, which localize to cellular plasma membranes. Using reverse transcriptase PCR and Western blot analysis to examine Dm-cF expression in animals, we detected Dm-cF expression in both larval and adult D. melanogaster cells. However, Dm-cF expression was detected only in third instar larvae and adults, suggesting that Dm-cF expression may be developmentally regulated. We also identified genes related to Dm-cF in the genomes of two other Drosophila species, Drosophila yakuba and Drosophila pseudoobscura, and the mosquito Anopheles gambiae. These observations suggest that f genes may be present in the genomes of many insects. Conservation within and between 22 baculovirus and 4 insect F proteins was examined in detail. These studies demonstrate that Dm-cF is expressed in D. melanogaster and suggest that if baculovirus f genes are derived from a host cellular f gene, the function appears to have changed substantially upon adaptation to the baculovirus infection cycle.

Amino Acid Sequence↗

The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2- N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein.

UDP-GlcNAc:alpha-6-D-mannoside [GlcNAc to Man alpha 1-6] beta-1,2-N-acetylglucosaminyltransferase II (GlcNAc-T II, EC 2.4.1.143) is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complex N-glycans. A 1.2-kb probe from a rat liver cDNA encoding GlcNAc-T II was used to screen a human genomic DNA library in lambda EMBL3. Southern analysis of restriction endonuclease digests of positive phage clones identified two hybridizing fragments (3.0 and 3.5 kb) which were subcloned into pBlueScript. The inserts of the resulting plasmids (pHG30 and pHG36) are over-lapping clones containing 5.5 kb of genomic DNA. The pHG30 insert (3.0 kb) contains a 1341-bp open reading frame encoding a 447-amino-acid protein, 250 bp of G + C-rich 5'-upstream sequence and 1.4 kb of 3'-downstream sequence. The pHG36 insert (3.5 kb) contains 2.75 kb of 5'-upstream sequence and 750 bp of the 5'-end of the open reading frame. The protein sequence showed the domain structure typical of all previously cloned glycosyltransferases, i.e. a short 9-residue putative cytoplasmic N-terminal domain, a 20-residue hydrophobic non-cleavable putative signal-anchor domain and a 418-residue C-terminal catalytic domain. Northern analysis of human tissues showed a major message at 3 kb and minor signals at 2 and 4.5 kb. There is no sequence similarity to any previously cloned glycosyltransferases including human UDP-GlcNAc:alpha-3-D-mannoside [GlcNAc to Man alpha 1-3] beta-1,2-N-acetylglucosaminyltransferase I (GlcNAc-T I) which has 445 amino acids with a 418-residue C-terminal catalytic domain. The human GlcNAc-T I and II genes (MGAT1 and MGAT2) map to chromosome bands 5q35 and 14q21, respectively, by fluorescence in situ hybridization. The entire coding regions of human GlcNAc-T I and II are each on a single exon. There is 92% identity between the amino acid sequences of the catalytic domains of human and rat GlcNAc-T II. Southern analysis of restriction enzyme digests of human genomic DNA indicates that there is only a single copy of the MGAT2 gene. The full-length coding region of GlcNAc-T II has been expressed in the baculovirus/Sf9 insect cell system, the recombinant enzyme has been purified to near homogeneity with a specific activity of about 20 mumol.min-1.mg-1 and the product synthesized by the recombinant enzyme has been identified by high-resolution 1H-NMR spectroscopy and mass spectrometry.

Amino Acid Sequence↗

Contrasting patterns of DNA sequence arrangement in Apis mellifera (honeybee) and Musca domestica (housefly).

We have examined the organization of the repeated and single copy DNA sequences in the genomes of two insects, the honeybee (Apis mellifera) and the housefly (Musca domestica). Analysis of the reassociation kinetics of honeybee DNA fragments 330 and 2,200 nucleotides long shows that approximately 90% of both size fragments is composed entirely of non-repeated sequences. Thus honeybee DNA contains few or no repeated sequences interspersed with nonrepeated sequences at a distance of less than a few thousand nucleotides. On the other hand, the reassociation kinetics of housefly DNA fragments 250 and 2,000 nucleotides long indicates that less than 15% of the longer fragments are composed entirely of single copy sequences. A large fraction of the housefly DNA therefore contains repeated sequences spaced less than a few thousand nucleotides apart. Reassociated repetitive DNA from the housefly was treated with S1 nuclease and sized on agarose A-50. The S1 resistant sequences have a bimodal distribution of lengths. Thirty-three percent is greater than 1,500 nucleotide pairs, and 67% has an average size about 300 nucleotide pairs. The genome of the housefly appears to have at least 70% of its DNA arranged as short repeats interspersed with single copy sequences in a pattern qualitatively similar to that of most eukaryotic genomes.

Animals↗

Genomic imprinting in the mealybugs.

The coccid insects (Hemiptera; Sternorrhyncha; Aphidiformes; Coccoidea; Pseudococcidae) are well suited to study not only the mechanisms of genomic imprinting but also facultative heterochromatization, a phenomenon well exemplified by inactivation of the X chromosome in female mammals. Coccids show sex-specific heterochromatization of an entire set of chromosomes and transcriptional silencing of all the paternally contributed chromosomes in males. Thus, genomic imprinting and the resultant differential regulation operate on 50% of the genome in contrast to the single X chromosome in female mammals. A significant insight into the phenomenon of genomic imprinting has come from very elegant cytological analysis of the coccid system. Recently, efforts have been made to dissect out at the molecular level the phenomenon of genomic imprinting in these insects. The present review summarizes both of these aspects. In light of the accruing experimental evidence for chromatin-based differences in the maternal and paternal genomes, it appears that the mealybug system may provide evidence for stable maintenance of chromatin code not only through mitosis but also through meiosis.

Animals↗

Ordered duplex RNA controls capsid architecture in an icosahedral animal virus.

Small spherical viruses are among the simplest replicating systems in biology, yet the factors affecting their assembly, stability and disassembly are still poorly understood. A molecular switch is required for the assembly of icosahedral virus particles containing more than 60 identical subunits because strict symmetry cannot be maintained in subunit packing. All previously reported viruses with this type of structure use a portion of the capsid protein to regulate interactions between chemically equivalent but structurally distinct interfaces. We have investigated the T = 3 quasiequivalent nodaviruses, which are small non-enveloped viruses with a single-stranded RNA genome that infect insects, mice and fish. They undergo a well-characterized series of steps in assembly and maturation, which in some respects are similar to the picornaviruses, despite their different capsid architecture. Here we report the X-ray structure of Flock House virus at 3.0 A resolution, which reveals an ordered RNA duplex of 20 nucleotides and a protein segment that control the subunit interactions in this animal virus. The RNA interacts with a helical protein domain of the subunit that lies inside the capsid shell. One of the helices that binds the RNA is part of a 44-amino-acid polypeptide which is autocatalytically cleaved from the initial subunit translation product after virion assembly. The structure indicates that RNA associated with the cleaved polypeptide may be important in the infection process.

Amino Acid Sequence↗

Identification and functional validation of glutathione S-transferase genes involved in detoxification of sulfoxaflor, afidopyropen and lambda-cyhalothrin in Aphis glycines.

BACKGROUND: Glutathione S-transferases (GSTs) play important roles in the detoxification of insecticides in insects. However, genome-wide identification and functional characterization of the GST gene family in the soybean aphid Aphis glycines have not been performed. RESULTS: A total of 17 AgGST genes were identified in the A. glycines genome and classified into five classes. Phylogenetic analysis and chromosomal mapping showed that delta and epsilon class genes experienced significant expansion. Exposure to LC₅₀ concentrations of sulfoxaflor, afidopyropen and lambda-cyhalothrin strongly induced several AgGST genes with AgGSTd5, AgGSTd6 and AgGSTe2 displaying the highest expression levels. RNA interference of AgGSTd5 significantly increased aphid mortality following exposure to all three insecticides. Knockdown of AgGSTd6 significantly elevated mortality under sulfoxaflor, while knockdown of AgGSTe2 significantly increased mortality under both sulfoxaflor and lambda-cyhalothrin. In contrast, silencing of AgGSTt1 and AgGSTt2 showed no significant effect on aphid mortality under the tested insecticides. CONCLUSION: This study provides comprehensive characterization of the GST gene family in A. glycines and demonstrates that AgGSTd5 plays a central role in the detoxification of sulfoxaflor, afidopyropen and lambda-cyhalothrin, while AgGSTd6 and AgGSTe2 contribute to tolerance against specific insecticides among the three compounds. These genes represent promising molecular targets for monitoring insecticide detoxification responses and for the development of strategies based on GST inhibitors to enhance insecticide efficacy in integrated pest management. © 2026 Society of Chemical Industry.

Animals↗

Behavioral mutants of Drosophila melanogaster. III. Isolation and mapping of mutations by direct visual observations of behavioral phenotypes.

Sex-linked behavioral mutants were induced in Drosophila melanogaster with ethyl methanesulfonate (EMS) and isolated by direct visual observation of abnormal phenotypes. The four behavioral phenotypes used were flight-reduction, hyperactivity, hypoactivity and stress-sensitivity, and are easily discernable in either single or small populations of mutant flies. In one screen, forty-two behavioral mutants were recovered from strains derived from 800 mutagen-treated X chromosomes In a second screen, 139 behavioral mutants were obtained from 2369 X chromosomes. The high rate at which behavioral mutants were recovered in the second screen, when compared to new visibles (28) and new temperature-sensitive lethals (124), suggests that the isolation of behavioral mutations on the autosomes of Drosophila and in the genomes of larger insects should be practical.

Animals↗

Localization of tandemly repeated DNA sequences in beetle chromosomes by fluorescent in situ hybridization.

In situ hybridization to chromosomes and nuclei of Tenebrio molitor shows the massive presence of a species-specific satellite DNA in all chromosomes and six sites of rDNA in mitotic chromosomes. These sites are located in two autosomal pairs and in the X and Y chromosomes. In a related species, Misolampus goudoti, in which two different families of highly repetitive DNA have been previously characterized, one family is located in centromeric regions of all chromosomes with the exception of chromosome Y, while the other repeated DNA family is present both in centromeric and distal regions of all chromosomes. rRNA genes in this species are present in a medium-sized autosomal pair only. These results show that molecular cytogenetics can be applied to coleopteran chromosomes and open the way for a physical mapping of DNA sequences in these organisms. The results also provide insights into the type of meiotic association of the X and Y chromosomes in Coleoptera and the distribution of repeated DNAs within the genome of these insects.

Animals↗

Potato cysteine proteinase inhibitor gene family: molecular cloning, characterisation and immunocytochemical localisation studies.

Potato cysteine proteinase inhibitors (PCPIs) represent a distinct group of proteins as they show no homology to any other known cysteine proteinase inhibitor superfamilies, but they all belong to the Kunitz-type soybean trypsin inhibitor family. cDNA clones for five PCPIs have been isolated and sequenced. Amino acid substitutions occurring in the limited regions forming loops on the surface of these proteins suggest a further classification of PCPIs into three subgroups. Accumulation of PCPI was observed in vacuoles of stems after treatment with jasmonic acid (JA) using immunocytochemical localisation, implying that these inhibitors are part of a potato defence mechanism against insects and pathogens. Genomic DNA analysis show that PCPIs form a multigene family and suggest that their genes do not possess any introns.

Amino Acid Sequence↗

Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae.

Plasma membrane localization of Ras requires posttranslational addition of farnesyl and palmitoyl lipid moieties to a C-terminal CaaX motif (C is cysteine, a is any aliphatic residue, X is the carboxy terminal residue). To better understand the relationship between posttranslational processing and the subcellular localization of Ras, a yeast genetic screen was undertaken based on the loss of function of a palmitoylation-dependent RAS2 allele. Mutations were identified in an uncharacterized open reading frame (YLR246w) that we have designated ERF2 and a previously described suppressor of hyperactive Ras, SHR5. ERF2 encodes a 41-kDa protein with four predicted transmembrane (TM) segments and a motif consisting of the amino acids Asp-His-His-Cys (DHHC) within a cysteine-rich domain (CRD), called DHHC-CRD. Mutations within the DHHC-CRD abolish Erf2 function. Subcellular fractionation and immunolocalization experiments reveal that Erf2 tagged with a triply iterated hemagglutinin epitope is an integral membrane protein that colocalizes with the yeast endoplasmic reticulum marker Kar2. Strains lacking ERF2 are viable, but they have a synthetic growth defect in the absence of RAS2 and partially suppress the heat shock sensitivity resulting from expression of the hyperactive RAS2(V19) allele. Ras2 proteins expressed in an erf2Delta strain have a reduced level of palmitoylation and are partially mislocalized to the vacuole. Based on these observations, we propose that Erf2 is a component of a previously uncharacterized Ras subcellular localization pathway. Putative members of an Erf2 family of proteins have been uncovered in yeast, plant, worm, insect, and mammalian genome databases, suggesting that Erf2 plays a role in Ras localization in all eucaryotes.

Acyltransferases↗

Numerous gene rearrangements in the mitochondrial genome of the wallaby louse, Heterodoxus macropus (Phthiraptera).

The complete arrangement of genes in the mitochondrial (mt) genome is known for 12 species of insects, and part of the gene arrangement in the mt genome is known for over 300 other species of insects. The arrangement of genes in the mt genome is very conserved in insects studied, since all of the protein-coding and rRNA genes and most of the tRNA genes are arranged in the same way. We sequenced the entire mt genome of the wallaby louse, Heterodoxus macropus, which is 14,670 bp long and has the 37 genes typical of animals and some noncoding regions. The largest noncoding region is 73 bp long (93% A+T), and the second largest is 47 bp long (92% A+T). Both of these noncoding regions seem to be able to form stem-loop structures. The arrangement of genes in the mt genome of this louse is unlike that of any other animal studied. All tRNA genes have moved and/or inverted relative to the ancestral gene arrangement of insects, which is present in the fruit fly Drosophila yakuba. At least nine protein-coding genes (atp6, atp8, cox2, cob, nad1-nad3, nad5, and nad6) have moved; moreover, four of these genes (atp6, atp8, nad1, and nad3) have inverted. The large number of gene rearrangements in the mt genome of H. macropus is unprecedented for an arthropod.

Adenine↗

Cloning and characterisation of a procorticotrophin-releasing hormone in the IZD-MB-0503 immunocyte line from the insect Mamestra brassicae.

The cloning and characterisation of a procorticotrophin-releasing hormone (proCRH) and the related CRH fragment in the IZD-MB-0503 cell line from the leptidopteran Mamestra brassicae were performed. PCR amplification of the genomic DNA reveals a fragment of 276 bp, while inverse PCR shows the presence of a gene consisting of 1153 bp. The comparison of the insect genomic proCRH gene with proCRH cDNA obtained by RACE shows the presence of three introns. There was a 61% identity with the corresponding coding sequence in Tilapia mossambica, and a 65.2% identity with the human proCRH coding sequence.

Amino Acid Sequence↗

Genomic sequence of Spodoptera frugiperda Ascovirus 1a, an enveloped, double-stranded DNA insect virus that manipulates apoptosis for viral reproduction.

Ascoviruses (family Ascoviridae) are double-stranded DNA viruses with circular genomes that attack lepidopterans, where they produce large, enveloped virions, 150 by 400 nm, and cause a chronic, fatal disease with a cytopathology resembling that of apoptosis. After infection, host cell DNA is degraded, the nucleus fragments, and the cell then cleaves into large virion-containing vesicles. These vesicles and virions circulate in the hemolymph, where they are acquired by parasitic wasps during oviposition and subsequently transmitted to new hosts. To develop a better understanding of ascovirus biology, we sequenced the genome of the type species Spodoptera frugiperda ascovirus 1a (SfAV-1a). The genome consisted of 156,922 bp, with a G+C ratio of 49.2%, and contained 123 putative open reading frames coding for a variety of enzymes and virion structural proteins, of which tentative functions were assigned to 44. Among the most interesting enzymes, due to their potential role in apoptosis and viral vesicle formation, were a caspase, a cathepsin B, several kinases, E3 ubiquitin ligases, and especially several enzymes involved in lipid metabolism, including a fatty acid elongase, a sphingomyelinase, a phosphate acyltransferase, and a patatin-like phospholipase. Comparison of SfAV-1a proteins with those of other viruses showed that 10% were orthologs of Chilo iridescent virus proteins, the highest correspondence with any virus, providing further evidence that ascoviruses evolved from a lepidopteran iridovirus. The SfAV-1a genome sequence will facilitate the determination of how ascoviruses manipulate apoptosis to generate the novel virion-containing vesicles characteristic of these viruses and enable study of their origin and evolution.

Animals↗

Self-assembly of the JC virus major capsid protein, VP1, expressed in insect cells.

The major capsid protein of human polyomavirus JC virus, VP1, has been cloned into a baculovirus genome and expressed in insect cells. The VP1 protein was expressed in the cytoplasm and transported into the nucleus. It was then purified by a sucrose cushion and CsCI density gradient centrifugation to near homogeneity. Electron microscopy showed that isolated recombinant VP1 protein self-assembled into a capsid-like structure similar to the natural empty capsid. Both chelator (EDTA) and reducing agent (DTT) are required to disrupt the capsid structure into the pentameric capsomeres, as demonstrated by haemagglutination assay and electron microscopy. These results suggest that JC virus VP1 can be transported into the nucleus and self-assembled to form capsid-like particles without the involvement of the viral minor capsid proteins, VP2 and VP3. In addition, metal ions and disulphide bonds appear to be important in maintaining the integrity of the viral capsid structure.

Amino Acid Sequence↗

Structural genomics sheds light on protein functions and remote homologs across the insect tree of life.

Protein structure bridges the sequence-function relationship, enabling deep exploration of biological processes across diverse organisms. Insects, the most diverse animal lineage, accounting for over 50% of all described animal species, provide an exceptional system for exploring sequence-structure-function relationships. Here, we reconstructed a comprehensive and well-resolved phylogeny of 4854 insects, spanning all orders. Leveraging this framework, we created an atlas of 13.29 million predicted protein structures from 824 representative species, including 11.63 million newly predicted structures. Structural clustering revealed that proteins with divergent sequences but similar structures could be effectively grouped together. Structural similarity searches against proteins with well-characterized functions yielded annotations for 7.61 million insect proteins, including up to 14% of previously unannotated proteins. We further identified 750 million remote homologs between insect proteins, many of which trace back to ancient branches of the insect phylogeny. Remarkably, despite extensive sequence divergence, cGAS-like receptors (cGLRs) were structurally conserved across all 824 insects. Experimental assays demonstrated that these structurally identified cGLRs play a crucial role in antiviral defense in the yellow fever mosquito. Our findings highlight the significance of structural genomics for understanding protein function and evolution across the tree of life.

Animals↗

Long repeats in a huge genome: microsatellite loci in the grasshopper Chorthippus biguttulus.

It is commonly believed that both the average length and the frequency of microsatellites correlate with genome size. We have estimated the frequency and the average length for 69 perfect dinucleotide microsatellites in an insect with an exceptionally large genome: Chorthippus biguttulus (Orthoptera, Acrididae). Dinucleotide microsatellites are not more frequent in C. biguttulus, but repeat arrays are 1.4 to 2 times longer than in other insect species. The average repeat number in C. biguttulus lies in the range of higher vertebrates. Natural populations are highly variable. At least 30 alleles per locus were found and the expected heterozygosity is above 0.95 at all three loci studied. In contrast, the observed heterozygosity is much lower (< or = 0.51), which could be caused by long null alleles.

Alleles↗

Insect-mediated transmission of mixed and reassorted cucumovirus genomic RNAs.

Transmissions of virus using the aphid Myzus persicae were performed using plants co-infected with two cucumoviruses, tomato aspermy virus (V-TAV) and cucumber mosaic virus (M-CMV). Five of the aphid-transmitted progeny viruses (3.7%) induced symptoms distinct from those induced by either parental virus. Northern blot hybridization analysis of encapsidated RNAs from these novel progeny demonstrated that all of the RNA profiles were characteristic of pseudo-recombinants, i.e. viruses with reassorted genomic RNAs. The two larger RNAs, 1 and 2, originated from V-TAV, whereas RNA 3 was derived from M-CMV. A more sensitive RNase protection assay analysis of both unencapsidated and encapsidated RNAs revealed the presence of minor populations of V-TAV-derived RNA 3 in all of these novel progeny, and of M-CMV-derived RNA 1 (and presumably RNA 2) in one of the progeny. A bias against the encapsidation of the minor populations of RNAs by the M-CMV coat protein was observed, suggesting that there is specificity or competition with regard to the encapsidation of cucumoviral RNAs in vivo. This study demonstrates that insect vectors can mediate the establishment of pseudorecombinants with mixed populations of RNA 3.

Animals↗