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At least 595 records · Page 33Linked to original sources
PubMed2005

Tubulin glycylation and glutamylation deficiencies in unconventional insect axonemes.

Though the 9+2 axonemal organization has generally been conserved throughout metazoan evolution, insect spermatozoa possess a substantial variety in axoneme ultrastructure, displaying different axonemal patterns. Therefore, insects provide a wide range of models that may be useful for the study of the mechanisms of axoneme assembly. We have used antibodies specific for glutamylated, monoglycylated, and polyglycylated tubulin to investigate the tubulin isoform content expressed in the unorthodox sperm axonemes of four insect species belonging to both of the superorders Palaeoptera and Neoptera. Each one of these axonemal models exhibits distinctive structural features, either showing the typical radial organization endowed with a ninefold symmetry or consisting of an helical arrangement with up to 200 microtubular doublets, but in all cases these axonemes share the absence of a microtubule central pair. Our results showed that all these atypical patterns are characterized by a dramatic decrease in both tubulin glycylation and glutamylation levels or even lack of both polymodifications. These data provide the first examples of a simultaneous extreme reduction or even absence of both polymodifications in axonemal tubulin. Given the unrelated positions of the analyzed species in the insect phylogenetic tree, this common feature is probably not due to evolutionary relationships. Therefore, our findings support the hypothesis of the existence of a correlation between the low level of polymodifications and the lack of a microtubule central pair in these peculiar insect flagellar axonemes, similarly as was previously proposed for cilia of Tetrahymena glycylation site mutants.

Acylation↗
PubMed2001

Cannabinoid receptors are absent in insects.

The endocannabinoid system exerts an important neuromodulatory role in mammals. Knockout mice lacking cannabinoid (CB) receptors exhibit significant morbidity. The endocannabinoid system also appears to be phylogenetically ancient--it occurs in mammals, birds, amphibians, fish, sea urchins, leeches, mussels, and even the most primitive animal with a nerve network, the Hydra. The presence of CB receptors, however, has not been examined in terrestrial invertebrates (or any member of the Ecdysozoa). Surprisingly, we found no specific binding of the synthetic CB ligands [(3)H]CP55,940 and [(3)H]SR141716A in a panel of insects: Apis mellifera, Drosophila melanogaster, Gerris marginatus, Spodoptera frugiperda, and Zophobas atratus. A lack of functional CB receptors was confirmed by the inability of tetrahydrocannabinol (THC) and HU210 to activate G-proteins in insect tissues, utilizing a guanosine-5'-O-(3-[(35)]thio)-triphosphate (GTP gamma S) assay. No orthologs of human CB receptors were located in the Drosophila genome, nor did we find orthologs of fatty acid amide hydrolase. This loss of CB receptors appears to be unique in the field of comparative neurobiology. No other known mammalian neuroreceptor is understood to be missing in insects. We hypothesized that CB receptors were lost in insects because of a dearth of ligands; endogenous CB ligands are metabolites of arachidonic acid, and insects produce little or no arachidonic acid or endocannabinoid ligands, such as anandamide.

Amino Acid Sequence↗
PubMed2006

Phylogeny of a serotonin-immunoreactive neuron in the primary olfactory center of the insect brain.

Serotonin (5-hydroxytryptamine; 5HT) functions in insects as a neurotransmitter, neuromodulator, and neurohormone. In the sphinx moth Manduca sexta, each of the paired antennal lobes (ALs; the primary olfactory centers in the insect brain) has one 5HT-immunoreactive (5HT-ir) neuron that projects into the protocerebrum, crosses the posterior midline, and innervates the contralateral AL; this is referred to as the contralaterally projecting, serotonin-immunoreactive deutocerebral (CSD) neuron. These neurons are thought to function as centrifugal modulators of olfactory sensitivity. To examine the phylogenetic distribution of 5HT-ir neurons apparently homologous to the CSD neuron, we imaged 5HT-like immunoreactivity in the brains of 40 species of insects belonging to 38 families in nine orders. CSD neurons were found in other Lepidoptera, Trichoptera, Diptera, Coleoptera, and Neuroptera but not in the Hymenoptera. In the paraneopteran and polyneopteran species (insects that undergo incomplete metamorphosis) examined, AL 5HT neurons innervate the ispsilateral AL and project to the protocerebrum. Our findings suggest that the characteristic morphology of the CSD neurons originated in the holometabolous insects (those that undergo complete metamorphosis) and were lost in the Hymenoptera. In a subset of the Diptera, the CSD neurons branch within the contralateral AL and project back to the ipsilateral AL via the antennal commissure. The evolution of AL 5HT neurons is discussed in the context of the physiological actions of 5HT observed in the lepidopteran AL.

Animals↗
PubMed2007

Peptidomics of identified neurons demonstrates a highly differentiated expression pattern of FXPRLamides in the neuroendocrine system of an insect.

FXPRLamides are insect neuropeptides that mediate such diverse functions as pheromone biosynthesis, visceral muscle contraction, and induction of diapause. Although multiple forms occur in every insect studied so far, little is known about a possible functional differentiation and/or differences in the cellular expression pattern of these messenger molecules. In this study, we performed a mass spectrometric survey of all FXPRLamide-expressing neurosecretory neurons in the CNS of Periplaneta americana. That species combines a very well characterized peptidergic system with relatively easy accessible neurosecretory cells suitable for dissection. In addition to the extensive mass spectrometric analyses of single cells, the projection of the FXPRLamide-expressing neurons was studied with three antisera specifically recognizing different FXPRLamides. The following conclusions can be drawn from this first comprehensive peptidomic approach on insect neurons. 1) A high degree of differentiation in the expression of FXPRLamides exists; not fewer then four cell types containing different sets of FXPRLamides were observed. 2) A low level of colocalization with other neuropeptides was found in these neurons. 3) A comparison with FXPRLamide-expressing neurons of other insects shows a high degree of conservation in the localization and projection of these neurons, which is not corroborated by a similar conservation of the corresponding peptide sequences. 4) Although the methods for cell identification, dissection, and sample preparation for mass spectrometry were kept as simple as possible, it was unambiguously shown that this approach is generally suitable for routine analysis of single identified neurons of insects.

Animals↗
PubMed2002

Dynamic structural changes of synaptic contacts in the visual system of insects.

The visual system of insects provides an excellent model to study processes of transduction and transmission of photic information, synaptogenesis, synaptic plasticity, and wiring between photoreceptors and their visual interneurons in the optic lobe. This review describes synaptic contacts between photoreceptors and other neurons in the visual system of insects, especially in the fly's first optic neuropile (the lamina), and summarizes changes observed in the synapses of visual cells that have been reported both in phylogeny and ontogeny, and also examples of synaptic plasticity in adult insects that have been evoked by intrinsic and extrinsic factors. Plasticity observed in synapses of the insect's visual system seems to exemplify not only synaptic contacts in insects but, given that similar examples of plasticity have been found in other animal groups, may also be a general phenomenon in the nervous system.

Animals↗
PubMed2007

Conifer defense against insects: proteome analysis of Sitka spruce (Picea sitchensis) bark induced by mechanical wounding or feeding by white pine weevils (Pissodes strobi).

Feeding insects can have major ecological and economic impacts on both natural and planted forests. Understanding the molecular and biochemical mechanisms by which conifers defend themselves from insect pests is a major goal of ongoing research in forest health genomics. In previous work, we demonstrated a complex system of anatomical, chemical, and transcriptome responses in Sitka spruce (Picea sitchensis) upon feeding by the economically significant insect pest, the white pine weevil (Pissodes strobi). In this study, changes to the proteome of Sitka spruce bark tissue were examined subsequent to feeding by white pine weevils or mechanical wounding. 2-D PAGE and high-throughput MS/MS were used to examine induced changes in protein abundance and protein modification. Significant changes were observed as early as 2 h following the onset of insect feeding. Among the insect-induced proteins are a series of related small heat shock proteins, other stress response proteins, proteins involved in secondary metabolism, oxidoreductases, and a novel spruce protein. Comparison of protein expression and cDNA microarray profiles of induced spruce stem tissues reveals the complementary nature of transcriptome and proteome analyses and the need to apply a multifaceted approach to the large-scale analysis of plant defense systems.

Animals↗
PubMed2004

Activity of spinosad on stored-tobacco insects and persistence on cured tobacco stripst.

Every year raw tobacco and manufactured tobacco products are lost to two major storage pests, the cigarette beetle, Lasioderma serricorne (F) and the tobacco moth, Ephestia elutella (Hiibner). Post-harvest management of both insects is achieved through sanitation, insect monitoring and fumigation with phosphine. However, insect resistance to phosphine and control failures have been reported, and fumigants are under constant regulatory pressure. Here we report the evaluation of spinosad, a bioinsecticide derived from the fermentation of the soil micro-organism Saccharopolyspora spinosa Mertz & Yao. Spinosad was first registered in 1997 and is now widely used as a field pest control agent on many crops, including tobacco. The insecticidal activity of the fermentation product (technical spinosad, TS) was measured by diet incorporation assays against L serricorne and E elutella larvae. Mortality levels were determined on newly hatched larvae and over the whole insect life cycle. For both species, no emergence of adult insects was observed in cured tobacco sprayed with 50mg TS kg(-1) and inoculated with eggs or newly hatched larvae. These results indicated that spinosad has potential for the control of both species in stored tobacco, since 100% control of both pests could be achieved at 50 mg TS kg(-1), and with almost full control (90-95%) at 10 mg kg(-1). We also monitored the stability of the product on cured tobacco. The original concentration of the main active component of TS, spinosyn A, did not change significantly over 18 months, indicating no loss of spinosad during a typical leaf storage period of time. Bioassays against larvae confirmed that the bioinsecticidal activity of spinosad was retained.

Animals↗
PubMed1995

Carboxy-terminal truncation of oryzacystatin II by oryzacystatin-insensitive insect digestive proteinases.

The biochemical interactions between digestive proteinases of the Coleoptera pest black vine weevil (Otiorynchus sulcatus) and two plant cysteine proteinase inhibitors, oryzacystatin I (OCI) and oryzacystatin II (OCII), were assessed using gelatin-polyacrylamide gel electrophoresis, OCI-affinity chromatography, and recombinant forms of the two plant inhibitors. The insect proteinases were resolved in gelatin-containing polyacrylamide gels as five major bands, only three of them being totally or partially inactivated by OCI and OCII. The maximal inhibitory effect of both OCs at pH 5.0 was estimated at 40% and the inhibition was stable with time despite the presence of OC-insensitive proteases, indicating the stability of the OCI and OCII effects. After removing OC-sensitive proteinases from the insect crude extract by OCI-affinity chromatography, the effects of the insect cystatin-insensitive proteases on the structural integrity of the free OCs were analyzed. While OCI remained stable, OCII was subjected to limited proteolysis leading to its gradual transformation into a approximately 10.5-kDa unstable intermediate, OCIIi. As shown by the degradation pattern of a glutathione S-transferase (GST)/OCII fusion protein, the appearance of OCIIi resulted from the C-terminal truncation of OCII. Either free or linked to GST, OCIIi was as active against papain and human cathepsin H as OCII, and the initial specificities of the inhibitor for these two cysteine proteinases were conserved after cleavage. Although these observations indicate the high conformational stability of OCII near its active (inhibitory) site, they also suggest a general conformational destabilization of this inhibitor following its initial cleavage, subsequently leading to its complete hydrolysis. This apparent susceptibility of OCII to proteolytic cleavage by the insect proteinases could have major implications when planning the use of this plant cystatin for insect pest control.

Animals↗
PubMed2002

Insects, oxygen, and iron.

Konrad Bloch developed an interest in insects because they are unable to make sterols, and in yeast because these cells need oxygen to make sterols and unsaturated fatty acids. Insects, like all other organisms, must deal with the toxic effects of oxygen in the presence of iron, which itself is a vital nutrient. They do so by making proteins with high affinity for ferric or ferrous ions. Two such proteins are transferrins and ferritins. Insects produce both of these proteins, but use them in different ways from most other organisms. Insect transferrins appear to be involved in innate immunity, perhaps by sequestering ferric ions to prevent pathogens and parasites from utilizing them. Insect ferritins, unlike those of any other group of organisms, are exported into the extracellular space (hemolymph). They may be involved in iron transport and/or protection against iron overload in the diet.

Animals↗
PubMed2001

Mammalian glycosyltransferase expression allows sialoglycoprotein production by baculovirus-infected insect cells.

The baculovirus-insect cell expression system is widely used to produce recombinant mammalian glycoproteins, but the glycosylated end products are rarely authentic. This is because insect cells are typically unable to produce glycoprotein glycans containing terminal sialic acid residues. In this study, we examined the influence of two mammalian glycosyltransferases on N-glycoprotein sialylation by the baculovirus-insect cell system. This was accomplished by using a novel baculovirus vector designed to express a mammalian alpha2,6-sialyltransferase early in infection and a new insect cell line stably transformed to constitutively express a mammalian beta1,4-galactosyltransferase. Various biochemical assays showed that a foreign glycoprotein was sialylated by this virus-host combination, but not by a control virus-host combination, which lacked the mammalian glycosyltransferase genes. Thus, this study demonstrates that the baculovirus-insect cell expression system can be metabolically engineered for N-glycoprotein sialylation by the addition of two mammalian glycosyltransferase genes.

Animals↗
PubMed2000

Safety and advantages of Bacillus thuringiensis-protected plants to control insect pests.

Plants modified to express insecticidal proteins from Bacillus thuringiensis (referred to as Bt-protected plants) provide a safe and highly effective method of insect control. Bt-protected corn, cotton, and potato were introduced into the United States in 1995/1996 and grown on a total of approximately 10 million acres in 1997, 20 million acres in 1998, and 29 million acres globally in 1999. The extremely rapid adoption of these Bt-protected crops demonstrates the outstanding grower satisfaction of the performance and value of these products. These crops provide highly effective control of major insect pests such as the European corn borer, southwestern corn borer, tobacco budworm, cotton bollworm, pink bollworm, and Colorado potato beetle and reduce reliance on conventional chemical pesticides. They have provided notably higher yields in cotton and corn. The estimated total net savings to the grower using Bt-protected cotton in the United States was approximately $92 million in 1998. Other benefits of these crops include reduced levels of the fungal toxin fumonisin in corn and the opportunity for supplemental pest control by beneficial insects due to the reduced use of broad-spectrum insecticides. Insect resistance management plans are being implemented to ensure the prolonged effectiveness of these products. Extensive testing of Bt-protected crops has been conducted which establishes the safety of these products to humans, animals, and the environment. Acute, subchronic, and chronic toxicology studies conducted over the past 40 years establish the safety of the microbial Bt products, including their expressed insecticidal (Cry) proteins, which are fully approved for marketing. Mammalian toxicology and digestive fate studies, which have been conducted with the proteins produced in the currently approved Bt-protected plant products, have confirmed that these Cry proteins are nontoxic to humans and pose no significant concern for allergenicity. Food and feed derived from Bt-protected crops which have been fully approved by regulatory agencies have been shown to be substantially equivalent to the food and feed derived from conventional crops. Nontarget organisms exposed to high levels of Cry protein are virtually unaffected, except for certain insects that are closely related to the target pests. Because the Cry protein is contained within the plant (in microgram quantities), the potential for exposure to farm workers and nontarget organisms is extremely low. The Cry proteins produced in Bt-protected crops have been shown to rapidly degrade when crop residue is incorporated into the soil. Thus the environmental impact of these crops is negligible. The human and environmental safety of Bt-protected crops is further supported by the long history of safe use for Bt microbial pesticides around the world.

Animals↗
PubMed1997

Varicella-zoster virus glycoproteins E and I expressed in insect cells form a heterodimer that requires the N-terminal domain of glycoprotein I.

Varicella-zoster virus (VZV) glycoproteins E and I (gE and gI), which are major components of the virion envelope, form a noncovalently linked complex. To understand their properties and functions, we expressed and purified soluble forms of gE and gI in the baculovirus system. Extracellular domains of gE and gI were cloned into baculoviruses, using either native or insect-derived signal peptides. Each recombinant virus yielded soluble protein in culture medium although a higher level of secretion was achieved with insect-derived signal peptides in recombinant gE baculoviruses. A soluble gE-gI complex was formed by co-infecting insect cells with recombinant gE and gI baculoviruses and detected by immunoprecipitation followed by Western blotting analyses. By gel filtration and cross-linking studies, we showed that the VZV gE-gI complex expressed in insect cells is a heterodimer. Interestingly, two recombinant gI proteins in which signal peptides were replaced with insect-derived signal peptides did not associate with gE. Amino-terminal sequencing and site-specific mutational studies showed that the replacement of only the signal peptides did not prevent complex formation but alterations in the processed amino-terminus of gI abrogated its ability to complex with gE. These findings indicate that the mature amino-terminus of gI is required for gE-gI complex formation by the external domains of VZV gE and gI.

Animals↗
PubMed1997

Liquefaction of Autographa californica nucleopolyhedrovirus-infected insects is dependent on the integrity of virus-encoded chitinase and cathepsin genes.

We examined the role of the Autographa californica nucleopolyhedrovirus (AcMNPV)-encoded chitinase in virus pathogenesis in Trichoplusia ni larvae. In conjunction with the AcMNPV-encoded cathepsin, it promotes liquefaction of the host in the latter stages of infection. Insects infected with virus mutants lacking either the chitinase A gene (chiA) or cathepsin gene (cath) remained intact several days after death. However, if both viruses were used to infect insects, liquefaction of the host was restored. Chitinase was readily detected in AcMNPV-infected insects using a chitinase-specific antibody, but it was absent from insects infected with a chiA deletion mutant (AcchiA-). The chitinase was also detected in polyhedra purified from AcMNPV-infected insects but not in those from AcchiA-. However, polyhedra derived from a virus lacking an intact chiA were no less effective in initiating an infection in second instar T. ni larvae than those of the unmodified AcMNPV. It was also demonstrated that the virus chitinase retained high levels of activity between pH 3.0 and 10.0. In contrast, chitinases isolated from Serratia marcescens, although active under acidic conditions, rapidly lost activity above pH 7.0 illustrating that despite 57% sequence identity, the two proteins have distinct enzymic activities.

Animals↗
PubMed1993

Acetylcholine receptor/channel molecules of insects.

Acetylcholine-gated ion channels of the nicotinic type are abundant in the nervous system of insects. The channels are permeable to Na+, K+ and probably Ca(2+), and unlike most vertebrate neuronal nicotinic acetylcholine receptors the receptor/channel molecule is blocked by alpha-bungarotoxin (alpha-Bgt). Such alpha-Bgt-sensitive receptors are present at synapses and on cell bodies of insect neurones. Single channel recordings have shown the existence of multiple conductances of nAChRs. Studies on several different insect preparations have provided evidence for more than one open state and several closed states of insect nAChRs. Functional insect nAChR channels have now been investigated in situ, following reconstitution of a purified protein in bilayers, and as a result of expressing in Xenopus oocytes messenger RNA encoding receptor subunits.

Acetylcholine↗
PubMed1992

Insect muscle actins differ distinctly from invertebrate and vertebrate cytoplasmic actins.

Invertebrate actins resemble vertebrate cytoplasmic actins, and the distinction between muscle and cytoplasmic actins in invertebrates is not well established as for vertebrate actins. However, Bombyx and Drosophila have actin genes specifically expressed in muscles. To investigate if the distinction between muscle and cytoplasmic actins evidenced by gene expression analysis is related to the sequence of corresponding genes, we compare the sequences of actin genes of these two insect species and of other Metazoa. We find that insect muscle actins form a family of related proteins characterized by about 10 muscle-specific amino acids. Insect muscle actins have clearly diverged from cytoplasmic actins and form a monophyletic group emerging from a cluster of closely related proteins including insect and vertebrate cytoplasmic actins and actins of mollusc, cestode, and nematode. We propose that muscle-specific actin genes have appeared independently at least twice during the evolution of animals: insect muscle actin genes have emerged from an ancestral cytoplasmic actin gene within the arthropod phylum, whereas vertebrate muscle actin genes evolved within the chordate lineage as previously described.

Actins↗
PubMed1988

Individual differences and variability in the timing of motor activity during walking in insects.

The uniformity of the neural physiology of an animal population is a fundamental, rarely tested assumption in most neurophysiological work. In this study, the variability of the timing between the movements of pairs of legs during free walking in cockroaches was assessed. Phases (a measure of timing) of motor bursts in muscles of legs in the American cockroach, Periplaneta americana, were calculated for insects walking straight over a flat, level surface. Student's t, Wallraff, Mann Whitney and Watson U2 two-sample tests were used to compare the phases of motor bursts of the same pairs of legs in different insects. The comparisons showed that in spite of the homogeneity both of the animal population and of the conditions under which the insects walked, most of the inter-leg phases of the animals that were compared were significantly different statistically. Further testing of greater numbers of insects using analysis of variance to test for population uniformity confirmed that the insects we tested were not members of a single statistical population with respect to the timing of motor bursts of the legs during walking. We infer that this unexpectedly large variability in a population thought to be relatively homogeneous reflects subtle but biologically significant differences between animals. The possible sources of these differences and their consequences for the study of behavior and its physiological basis are discussed.

Animals↗
PubMed1984

Immunocytochemical localization of gastrin-releasing peptide/bombesin-like immunoreactive neurons in insects.

GRP/bombesin-like immunoreactive material was immunocytochemically detected in neurons of seven insect species belonging to seven orders, while such neurons were not found in three insect species belonging to two other orders. In some insect species certain neurons were found in corresponding places and approximately the same numbers. It seems likely that such neurons have a common evolutionary origin and are homologous. The fact that the GRP-antiserum reveals such homologous neurons in species belonging to different orders, suggests that the part of the GRP/bombesin-like peptide recognized by the antiserum has been relatively stable during evolution. As the GRP-antiserum had to be used in much higher concentrations on insect tissue than for GRP endocrine cells in chicken proventriculus, the chemical resemblance of the insect peptide(s) to GRP and bombesin may be limited.

Animals↗
PubMed1986

The ATPase kinetics of insect fibrillar flight muscle myosin subfragment-1.

Myosin subfragment-1 (S1) has been prepared from the fibrillar flight muscles of the giant water bug Lethocerus by chymotryptic digestion of myofibrillar suspensions in the absence of magnesium ions. The S1 obtained has a single light chain and a heavy chain with molecular weights of about 18 kDa and 90 kDa respectively. The kinetics of the elementary steps of the magnesium-dependent ATPase of insect S1 and rabbit S1 are similar, both with ATP and with ATP analogues as substrates. However, the presence of variable amounts of inactive protein within our preparation means that several rate constants cannot be obtained with as much precision in the case of insect S1. The most striking differences between the rabbit and insect S1 are values for the Vmax and the Km of actin during actin-activation of the MgATPase activity, which are up to an order of magnitude lower and greater in the insect than in the rabbit, respectively. The mechanical properties of strain activation and of capacity to do extended oscillatory work are unique to insect fibrillar flight muscle and distinguish it from vertebrate striated muscle. It is likely that these properties reflect differences in the organization of actin and myosin within the respective filament lattices rather than intrinsic differences in the ATPase mechanisms of the isolated myosin molecules from the two types of muscle.

Actomyosin↗