Foamy Virus Gag p71-p68 Cleavage Is Required for Template Switch of the Reverse Transcriptase

In contrast to orthoretroviruses, processing of foamy viral p71 Gag is limited to a single cleavage site. Nevertheless, Gag maturation is essential for infectivity, but deletion of p3 results in a modest drop in infectivity. Here, we show that Gag processing of p71 to p68 and p3 is essential for full-length cDNA synthesis, while inactivation of Gag cleavage results in cDNAs containing only the RU5 region; cDNAs encompassing the U3 region were almost undetectable.     

THE EFFECT OF BIASED INCLUSION OF TAXA ON THE CORRELATION BETWEEN DISCRETE CHARACTERS IN PHYLOGENETIC TREES

In a published paper, a method for testing the correlation between two discrete characters was presented and applied to test whether in butterfly larvae origins of gregariousness are concentrated to lineages with aposematic coloration. The relationship was found to be nonsignificant. However, the butterfly data on which the test was applied had been compiled in another study to investigate evolutionary sequences and was biased, because there was an overrepresentation of aposematic, as compared to cryptic, branches in the sample. In the paper presented here, aposematic and cryptic clades of the original phylogeny were resolved to the same degree, and the resulting set of branches may be regarded as unbiased with respect to the hypothesis being tested. A method for testing the contingency of states in two characters was then applied to the new data set, resulting in a highly significant relationship between origins of gregariousness and aposematic coloration. I argue that when using statistical methods on phylogenetic data, it is crucial to resolve various parts of the phylogeny to the same comparable systematic unit in order not to get a distorted sample of taxa/branches.     

Wild-type Leishmania donovani promastigotes block maturation, increase integrin expression and inhibit detachment of human monocyte-derived dendritic cells – the influence of phosphoglycans

The protective immune response against the parasite, including the role of dendritic cells (DC) in the course of infection, plays a fundamental role. This study shows that wild-type (WT) Leishmania promastigotes and specifically the phosphoglycans family of virulence-associated antigens inhibit human monocyte-derived dendritic cells (MoDC) maturation and detachment to distinct surfaces. Immature phagocytosis of Leishmania donovani promastigotes by immature MoDC results in the increased expression of CD11b and CD51, and inhibition of cell detachment to distinct surfaces, which was dependent on the presence of phosphoglycans. These findings demonstrate that phosphoglycans of WT L. donovani might also inhibit human DC migration to lymphoid organs.     

Do human activity and infrastructure disturb domesticated reindeer? The need for the reindeer’s perspective

In recent decades, human–Rangifer (reindeer and caribou) interactions have increasingly been studied from a scientific perspective. Many of the studies have examined Norwegian wild reindeer or caribou in North America. It is often questioned whether results from these studies can be applied to reindeer in managed herds, as these animals have been exposed to domestication and are also more used to humans. In order to examine the domesticated reindeer’s reactions to various disturbance sources, we reviewed 18 studies of the effects of human activity and infrastructure on 12 populations of domesticated reindeer and compared these to studies on wild reindeer and caribou; based on this, we discuss the effects of domestication and tameness on reindeer responses to anthropogenic disturbance. We also consider the relevance of spatial and temporal scales and data collection methods when evaluating the results of these studies. The reviewed studies showed that domesticated reindeer exhibit avoidance behaviours up to 12 km away from infrastructure and sites of human activity and that the area they avoid may shift between seasons and years. Despite a long domestication process, reindeer within Sami reindeer-herding systems exhibit similar patterns of large-scale avoidance of anthropogenic disturbance as wild Rangifer, although the strength of their response may sometimes differ. This is not surprising since current Sami reindeer husbandry represents an extensive form of pastoralism, and the reindeer are not particularly tame. To obtain a true picture of how reindeer use their ranges, it is of fundamental importance to study the response pattern at a spatial and temporal scale that is relevant to the reindeer, whether domesticated or wild.     

The insert within the catalytic domain of tripeptidyl-peptidase II is important for the formation of the active complex.

Tripeptidyl-peptidase II (TPP II) is a large (Mr>10(6)) tripeptide-releasing enzyme with an active site of the subtilisin-type. Compared with other subtilases, TPP II has a 200 amino-acid insertion between the catalytic Asp44 and His264 residues, and is active as an oligomeric complex. This study demonstrates that the insert is important for the formation of the active high-molecular mass complex. A recombinant human TPP II and a murine TPP II were found to display different complex-forming characteristics when over-expressed in human 293-cells; the human enzyme was mainly in a nonassociated, inactive state whereas the murine enzyme formed active oligomers. This was surprising because native human TPP II is purified from erythrocytes as an active oligomeric complex, and the amino-acid sequences of the human and murine enzymes were 96% identical. Using a combination of chimeras and a single point mutant, the amino acid responsible for this difference was identified as Arg252 in the recombinant human sequence, which corresponds to a glycine in the murine sequence. As Gly252 is conserved in all sequenced variants of TPP II, the recombinant enzyme with Arg252 is atypical. Nevertheless, as Arg252 evidently interferes with complex formation, and this residue is close to the catalytic His264, it may also explain why oligomerization influences enzyme activity. The exact mechanism for how the G252R substitution interferes with complex formation remains to be determined, but will be of importance for the understanding of the unique properties of TPP II.