1,853 research outputs found

    Species-specific cuticular hydrocarbon stability within European Myrmica Ants

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    Recognition is a fundamental process on which all subsequent behaviors are based at every organizational level, from the gene up to the super-organism. At the whole organism level visual recognition is the best understood. However, chemical communication is far more widespread than visual communication, but despite its importance is much less understood. Ants provide an excellent model system for chemical ecology studies as it is well established that compounds known as cuticular hydrocarbons (CHCs) are used as recognition cues in ants. Therefore, stable species-specific odors should exist, irrespective of geographic locality. We tested this hypothesis by comparing the CHC profiles of workers of twelve species of Myrmica ants from four countries across Europe, from Iberia to the Balkans and from the Mediterranean to Fennoscandia. CHCs remained qualitatively stable within each species, right down to the isomer level. Despite the morphological similarity that occurs within the genus Myrmica, their CHCs were highly diverse but remarkably species-specific and stable across wide geographical areas. This indicates a genetic mechanism under strong selection that produces these species-specific chemical profiles, despite each species encountering different environmental conditions across its range

    Is the salivary gland associated with honey bee recognition compounds in worker honey bees (Apis mellifera)?

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    Cuticular hydrocarbons (CHCs) function as recognition compounds with the best evidence coming from social insects such as ants and honey bees. The major exocrine gland involved in hydrocarbon storage in ants is the post-pharyngeal gland (PPG) in the head. It is still not clearly understood where CHCs are stored in the honey bee. The aim of this study was to investigate the hydrocarbons and esters found in five major worker honey bee (Apis mellifera) exocrine glands, at three different developmental stages (newly emerged, nurse, and forager) using a high temperature GC analysis. We found the hypopharyngeal gland contained no hydrocarbons nor esters, and the thoracic salivary and mandibular glands only contained trace amounts of n-alkanes. However, the cephalic salivary gland (CSG) contained the greatest number and highest quantity of hydrocarbons relative to the five other glands with many of the hydrocarbons also found in the Dufour's gland, but at much lower levels. We discovered a series of oleic acid wax esters that lay beyond the detection of standard GC columns. As a bee's activities changed, as it ages, the types of compounds detected in the CSG also changed. For example, newly emerged bees have predominately C19-C23 n-alkanes, alkenes and methyl-branched compounds, whereas the nurses' CSG had predominately C31:1 and C33:1 alkene isomers, which are replaced by a series of oleic acid wax esters in foragers. These changes in the CSG were mirrored by corresponding changes in the adults' CHCs profile. This indicates that the CSG may have a parallel function to the PPG found in ants acting as a major storage gland of CHCs. As the CSG duct opens into the buccal cavity the hydrocarbons can be worked into the comb wax and could help explain the role of comb wax in nestmate recognition experiments

    The refined crystal structure of a fully active semisynthetic ribonuclease at 1.8 Å resolution

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    A fully active, semisynthetic analog of bovine ribonuclease A, comprised of residues 1-118 of the molecule in a noncovalent complex with the synthetic peptide analog of residues 111-124, has been crystallized in space group P3(2)21 from a solution of 1.3 M ammonium sulfate and 3.0 M cesium chloride at pH 5.2. The crystallographic structure was determined by rotation and translation searches utilizing the coordinates for ribonuclease A reported by Wlodawer and Sjolin (Wlodawer, A., and Sjolin, L. (1983) Biochemistry 22, 2720-2728) and has been refined at 1.8-A resolution to an agreement factor of 0.204. Most of the structure of the semisynthetic enzyme closely resembles that found in ribonuclease A with the synthetic peptide replacing the C-terminal elements of the naturally occurring enzyme. No redundant structure is seen; residues 114-118 of the larger chain and residues 111-113 of the peptide do not appear in our map. The positions of those residues at or near the active site are very similar to, if not identical with, those previously reported by others, except for histidine 119, which occupies predominantly the B position seen as a minor site by Borkakoti et al. (Borkakoti, N., Moss, D. S., and Palmer, R. A. (1982) Acta Crystallogr. Sect. B Struct. Crystallogr. Cryst. Chem. 38,2210-2217) and not at all by Wlodawer and Sjolin (1983)

    Effectiveness of a targeted telephone-based case management service on activity in an Emergency Department in the UK: a pragmatic difference-in-differences evaluation.

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    BACKGROUND: This study evaluates the effectiveness of a targeted telephone-based case management service that aimed to reduce ED attendance amongst frequent attenders, known to disproportionately contribute to demand. Evidence on the effectiveness of these services varies. METHODS: A 24-month controlled before-and-after study, following 808 patients (128 cases and 680 controls (41 were non-compliant)) who were offered the service in the first four months of operation within a UK ED department. Patients stratified as high-risk of reattending ED within 6 months by a predictive model were manually screened. Those positively reviewed were offered a non-clinical, nurse-led, telephone-based health coaching, consisting of care planning, coordination and goal setting for up to 9 months. Service effectiveness was estimated using a difference-in-differences (DiD) analysis. Incident rate of ED and Minor Injury Unit (MIU) attendances and average length of stay in intervention recipients and controls over 12 months after receiving their service offer following ED attendance were compared, adjusting for the prior 12-month period, sex and age, to give an incidence rate ratio (IRR). RESULTS: Intervention recipients were more likely to be female (63.3% versus 55.4%), younger (mean of 69 years versus 76 years), and have higher levels of ED activity (except for MIU) than controls. Mean rates fell between periods for all outcomes (except for MIU attendance). The Intention-to-Treat analysis indicated non-statistically significant effect of the intervention in reducing all outcomes, except for MIU attendances, with IRRs: ED attendances, 0.856 (95% CI: 0.631, 1.160); ED admissions, 0.871 (95% CI: 0.628, 1.208); length of stay for emergency and elective admissions: 0.844 (95% CI: 0.619, 1.151) and 0.781 (95% CI: 0.420, 1.454). MIU attendance increased with an IRR: 2.638 (95% CI: 1.041, 6.680). CONCLUSIONS: Telephone-based health coaching appears to be effective in reducing ED attendances and admissions, with shorter lengths of stay, in intervention recipients over controls. Future studies need to capture outcomes beyond acute activity, and better understand how services like this provide added value

    The structure of residues 7-16 of the Aɑ-chain of human fibrinogen bound to bovine thrombin at 2.3 Å resolution

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    The tetradecapeptide Ac-D-F-L-A-E-G-G-G-V-R-G-P-R-V-OMe, which mimics residues 7f-20f of the A alpha-chain of human fibrinogen, has been co-crystallized with bovine thrombin from ammonium sulfate solutions in space group P2(1) with unit cell dimensions of a = 83.0 A, b = 89.4 A, c = 99.3 A, and beta = 106.6 degrees. Three crystallographically independent complexes were located in the asymmetric unit by molecular replacement using the native bovine thrombin structure as a model. The standard crystallographic R-factor is 0.167 at 2.3-A resolution. Excellent electron density could be traced for the decapeptide, beginning with Asp-7f and ending with Arg-16f in the active site of thrombin; the remaining 4 residues, which have been cleaved from the tetradecapeptide at the Arg-16f/Gly-17f bond, are not seen. Residues 7f-11f at the NH2 terminus of the peptide form a single turn of alpha-helix that is connected by Gly-12f, which has a positive phi angle, to an extended chain containing residues 13f-16f. The major specific interactions between the peptide and thrombin are 1) a hydrophobic cage formed by residues Tyr-60A, Trp-60D, Leu-99, Ile-174, Trp-215, Leu-9f, Gly-13f, and Val-15f that surrounds Phe-8f; 2) a hydrogen bond linking Phe-8f NH to Lys-97 O;3) a salt link between Glu-11f and Arg-173; 4) two antiparallel beta-sheet hydrogen bonds between Gly-14f and Gly-216; and 5) the insertion of Arg-16f into the specificity pocket. Binding of the peptide is accompanied by a considerable shift in two of the loops near the active site relative to human D-phenyl-L-prolyl-L-arginyl chloromethyl ketone (PPACK)-thrombin

    Structural changes that accompany the reduced catalytic efficiency of two semisynthetic ribonuclease analogs

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    The structures of two catalytically defective semi-synthetic RNases obtained by replacing aspartic acid 121 with asparagine or alanine have been determined and refined at a resolution of 2.0 A (R = 0.186 and 0.172, respectively). When these structures are compared with the refined 1.8-A structure (R = 0.204) of the fully active aspartic acid-containing enzyme (Martin, P.D., Doscher, M.S., and Edwards, B. F. P. (1987) J. Biol. Chem. 262, 15930-15938), numerous and widespread changes, much greater in number and magnitude than the small structural variations noted previously between the semisynthetic complex and RNase A, are found to have occurred. These changes include the movement of the loop containing residues 65-72 away from the active site, a more or less generalized relocation of crystallographically bound water molecules, and a number of rearrangements in the hydrogen bonding network at the active site. Most changes are far removed from the immediate site of the modifications and are distributed essentially throughout the molecule. The details of many of these changes are unique to each analog. In the asparagine analog, a destabilization in the positioning of active site residue His-119 also appears to have occurred

    Ambient Air Pollution and Pregnancy Outcomes: A Review of the Literature

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    Over the last decade or so, a large number of studies have investigated the possible adverse effects of ambient air pollution on birth outcomes. We reviewed these studies, which were identified by a systematic search of the main scientific databases. Virtually all reviewed studies were population based, with information on exposure to air pollution derived from routine monitoring sources. Overall, there is evidence implicating air pollution in adverse effects on different birth outcomes, but the strength of the evidence differs between outcomes. The evidence is sufficient to infer a causal relationship between particulate air pollution and respiratory deaths in the postneonatal period. For air pollution and birth weight the evidence suggests causality, but further studies are needed to confirm an effect and its size and to clarify the most vulnerable period of pregnancy and the role of different pollutants. For preterm births and intrauterine growth retardation (IUGR) the evidence as yet is insufficient to infer causality, but the available evidence justifies further studies. Molecular epidemiologic studies suggest possible biologic mechanisms for the effect on birth weight, premature birth, and IUGR and support the view that the relation between pollution and these birth outcomes is genuine. For birth defects, the evidence base so far is insufficient to draw conclusions. In terms of exposure to specific pollutants, particulates seem the most important for infant deaths, and the effect on IUGR seems linked to polycyclic aromatic hydrocarbons, but the existing evidence does not allow precise identification of the different pollutants or the timing of exposure that can result in adverse pregnancy outcomes

    Evidence for passive chemical camouflage in the parasitic mite Varroa destructor

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    Social insect colonies provide a stable and safe environment for their members. Despite colonies been heavily guarded, parasites have evolved numerous strategies to invade and inhabit these hostile places. Two common strategies are chemical mimicry via biosynthesis of the hosts' odour or chemical camouflage were compounds are acquired straight from the host. The ectoparasitic mite Varroa destructor feeds on the heamolymph of its honeybee host Apis mellifera and uses chemical mimicry to remain undetected as it lives on the adult host during its phoretic phase or while reproducing on the honeybee brood. During the mite life cycle it switches between host adults and brood, which requires it to adjust its profile to mimic the very different odours of honeybee brood and adults. In a series of transfer experiments using adult bees and pupae, we tested whether V. destructor does this by synthesising compounds or using chemical camouflage. We show that V. destructor required direct access to the host cuticle to mimic its odour and was unable to synthesise host-specific compounds itself. Mites use chemical camouflage to mimic the host odour, even when dead, indicating a passive physico-chemical mechanism of the parasite cuticle. The chemical profile of V. destructor was adjusted within three to nine hours after switching hosts, demonstrating that passive camouflage is a highly efficient, fast and flexible way for the mite’s to adapt to a new host's profile when moving between different host life stages, or host colonies

    The mononuclear metal center of type-I dihydroorotase from aquifex aeolicus

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    Abstract Background Dihydroorotase (DHO) is a zinc metalloenzyme, although the number of active site zinc ions has been controversial. E. coli DHO was initially thought to have a mononuclear metal center, but the subsequent X-ray structure clearly showed two zinc ions, α and β, at the catalytic site. Aquifex aeolicus DHO, is a dodecamer comprised of six DHO and six aspartate transcarbamoylase (ATC) subunits. The isolated DHO monomer, which lacks catalytic activity, has an intact α-site and conserved β-site ligands, but the geometry of the second metal binding site is completely disrupted. However, the putative β-site is restored when the complex with ATC is formed and DHO activity is regained. Nevertheless, the X-ray structure of the complex revealed a single zinc ion at the active site. The structure of DHO from the pathogenic organism, S. aureus showed that it also has a single active site metal ion. Results Zinc analysis showed that the enzyme has one zinc/DHO subunit and the addition of excess metal ion did not stimulate catalytic activity, nor alter the kinetic parameters. The metal free apoenzyme was inactive, but the full activity was restored upon the addition of one equivalent of Zn2+ or Co2+. Moreover, deletion of the β-site by replacing the His180 and His232 with alanine had no effect on catalysis in the presence or absence of excess zinc. The 2.2 Å structure of the double mutant confirmed that the β-site was eliminated but that the active site remained otherwise intact. Conclusions Thus, kinetically competent A. aeolicus DHO has a mononuclear metal center. In contrast, elimination of the putative second metal binding site in amidohydrolyases with a binuclear metal center, resulted in the abolition of catalytic activity. The number of active site metal ions may be a consideration in the design of inhibitors that selectively target either the mononuclear or binuclear enzymes
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