Tick species from cattle in the Adama Region of Ethiopia and pathogens detected

Ticks will diminish productivity among farm animals and transmit zoonotic diseases. We conducted a study to identify tick species infesting slaughter bulls from Adama City and to screen them for tick-borne pathogens. In 2016, 291 ticks were collected from 37 bulls in Adama, which were ready for slaughter. Ticks were identified morphologically. Total genomic DNA was extracted from ticks and used to test for Rickettsia spp. with real-time PCR. Species identification was done by phylogenetic analysis using sequencing that targeted the 23S-5S intergenic spacer region and ompA genes. Four tick species from two genera, Amblyomma and Rhipicephalus, were identified. Amblyomma cohaerens was the dominant species (n = 241, 82.8%), followed by Amblyomma variegatum (n = 22, 7.5%), Rhipicephalus pulchellus (n = 19, 6.5%), and Rhipicephalus decoloratus (n = 9, 3.0%). Among all ticks, 32 (11%) were positive for Rickettsia spp. and 15 (5.2%) of these were identified as R. africae comprising at least two genetic clades, occurring in A. variegatum (n = 10) and A. cohaerens (n = 5). The remainder of Rickettsia-positive samples could not be amplified due to low DNA yield. Furthermore, another 15 (5.2%) samples carried other pathogenic bacteria: Ehrlichia ruminantium (n = 9; 3.1%) in A. cohaerens, Ehrlichia sp. (n = 3; 1%) in Rh. pulchellus and A. cohaerens, Anaplasma sp. (n = 1; 0.5%) in A. cohaerens, and Neoehrlichia mikurensis (n = 2; 0.7%) in A. cohaerens. All ticks were negative for Bartonella spp., Babesia spp., Theileria spp., and Hepatozoon spp. We reported for the first time E. ruminatium, N. mikurensis, Ehrlichia sp., and Anaplasma sp. in A. cohaerens. Medically and veterinarily important pathogens were mostly detected from A. variegatum and A. cohaerens. These data are relevant for a One-health approach for monitoring and prevention of tick-borne disease transmission

An expanded protein folding cage in the GroEL-gp31 complex

Bacteriophage T4 produces a GroES analogue, gp31, which cooperates with the Escherichia coli GroEL to fold its major coat protein gp23. We have used cryo-electron microscopy and image processing to obtain three-dimensional structures of the E. coli chaperonin GroEL complexed with gp31, in the presence of both ATP and ADP. The GroEL-gp31-ADP map has a resolution of 8.2 Å, which allows accurate fitting of the GroEL and gp31 crystal structures. Comparison of this fitted structure with that of the GroEL-GroES-ADP structure previously determined by cryo-electron microscopy shows that the folding cage is expanded. The enlarged volume for folding is consistent with the size of the bacteriophage coat protein gp23, which is the major substrate of GroEL-gp31 chaperonin complex. At 56 kDa, gp23 is close to the maximum size limit of a polypeptide that is thought to fit inside the GroEL-GroES folding cage. © 2006 Elsevier Ltd. All rights reserved

EU Resource efficiency perspectives in a global context

This study explores the relevance and implications of resource efficiency for five distinct, vitally important resource themes: energy, land, phosphorus, fresh water and fish stocks. Natural resources underpin the functioning of both the European and the global economy. They critically shape prospects for current and future quality of life over the coming decades. Key questions addressed in this study are: What are the impacts of current and projected resource use up to 2050 and in which parts of the world will they be felt most? What are the potential effects of boosting resource efficiency in different world regions? Is policy intervention conceivable? How would such interventions interact with other resources not targeted; and how does resource efficiency relate to efforts to mitigate climate change

Evolution of lacewings and allied orders using anchored phylogenomics (Neuroptera, Megaloptera, Raphidioptera)

Analysis of anchored hybrid enrichment (AHE) data under a variety of analytical parameters for a broadly representative sample of taxa (136 species representing all extant families) recovered a well-resolved and strongly supported tree for the higher phylogeny of Neuropterida that is highly concordant with previous estimates based on DNA sequence data. Important conclusions include: Megaloptera is sister to Neuroptera; Coniopterygidae is sister to all other lacewings; Osmylidae, Nevrorthidae and Sisyridae are recovered as a monophyletic Osmyloidea, and Rhachiberothidae and Berothidae were recovered within a paraphyletic Mantispidae. Contrary to previous studies, Chrysopidae and Hemerobiidae were not recovered as sister families and morphological similarities between larvae of both families supporting this assumption are reinterpreted as symplesiomorphies. Relationships among myrmeleontoid families are similar to recent studies except Ithonidae are placed as sister to Nymphidae. Notably, Ascalaphidae render Myrmeleontidae paraphyletic, again calling into question the status of Ascalaphidae as a separate family. Using statistical binning of partitioned loci based on a branch-length proxy, we found that the diversity of phylogenetic signal across partitions was minimal from the slowest to the fastest evolving loci and varied little over time. Ancestral character-state reconstruction of the sclerotization of the gular region in the larval head found that although it is present in Coleoptera, Raphidioptera and Megaloptera, it is lost early in lacewing evolution and then regained twice as a nonhomologous gula-like sclerite in distantly related clades. Reconstruction of the ancestral larval habitat also indicates that the ancestral neuropteridan larva was aquatic, regardless of the assumed condition (i.e., aquatic or terrestrial) of the outgroup (Coleopterida)

Chaperonin complex with a newly folded protein encapsulated in the folding chamber

A subset of essential cellular proteins requires the assistance of chaperonins (in Escherichia coli, GroEL and GroES), double-ring complexes in which the two rings act alternately to bind, encapsulate and fold a wide range of nascent or stress-denatured proteins1, 2, 3, 4, 5. This process starts by the trapping of a substrate protein on hydrophobic surfaces in the central cavity of a GroEL ring6, 7, 8, 9, 10. Then, binding of ATP and co-chaperonin GroES to that ring ejects the non-native protein from its binding sites, through forced unfolding or other major conformational changes, and encloses it in a hydrophilic chamber for folding11, 12, 13, 14, 15. ATP hydrolysis and subsequent ATP binding to the opposite ring trigger dissociation of the chamber and release of the substrate protein3. The bacteriophage T4 requires its own version of GroES, gp31, which forms a taller folding chamber, to fold the major viral capsid protein gp23 (refs 16–20). Polypeptides are known to fold inside the chaperonin complex, but the conformation of an encapsulated protein has not previously been visualized. Here we present structures of gp23–chaperonin complexes, showing both the initial captured state and the final, close-to-native state with gp23 encapsulated in the folding chamber. Although the chamber is expanded, it is still barely large enough to contain the elongated gp23 monomer, explaining why the GroEL–GroES complex is not able to fold gp23 and showing how the chaperonin structure distorts to enclose a large, physiological substrate protein