Analysis of the emergence of the Scarce Chaser Libellula fulva O.F. Müller, 1764 (Odonata: Libellulidae)

The Scarce Chaser (Libellula fulva) is widespread in Europe and in many regions is relatively common. It is also abundant in the lake districts of western and northern Poland. Although the species frequently occurs in large numbers its biology is poorly known. Emergence of L. fulva was investigated in this study as a contribution to the life history of the species. Studies were carried out in the vicinity of Chojno (52°41′ N, 16°12′ E) on the edge of the Notecka Forest in 2003 and 2004. The stem habitat of the population is a stream with the adjacent swamps. Libellula fulva belongs to the spring species sensu Corbet (1999). The emergence of the studied population lasted 19 days (between 18 May and 5 June) and 31 days (between 13 May and 12 June) in 2003 and 2004, respectively. It was characterised by synchronous and, especially in the first phase, mass emergence. The high synchronisation is reflected in the fact that 50% of the population had emerged by the seventh (in 2003) and the fifth (in 2004) days of the process. This is vital to the imagines, which mature and return to the water body as soon as possible to reproduce. Timing of the end of emergence depends on atmospheric conditions during its duration and the conditions preceding the start of emergence on a given day. In the daily course there is a tendency for emergence to finish as soon as possible. Extension of the emergence is synonymous with increased mortality in the dragonfly population caused by predators.     

Convenient preparation of deuterium‐labeled analogs of peptides containing N‐substituted glycines for a stable isotope dilution LC‐MS quantitative analysis

N‐substituted glycines constitute mimics of natural amino acids that are of great interest in the peptide‐based drug development. Peptoids‐oligo(N‐substituted glycines) have been recently demonstrated to be highly active peptidomimetics in biological systems, resistant to proteolytic degradation. We developed a method of the deuterium labeling of peptidomimetics containing N‐substituted glycine residues via H/D exchange of their α‐carbon hydrogen atoms. The labeling was shown to be easy, inexpensive, and without the use of derivatization reagents or the need for a further purification. The deuterons introduced at the α‐carbon atoms do not undergo a back exchange under acidic conditions during liquid chromatography mass spectrometry (LC‐MS) analysis. The LC‐MS analysis of a mixture of isotopologues revealed a co‐elution of deuterated and nondeuterated forms of the peptidomimetics, which may be useful in the quantitative isotope dilution analysis of peptoids and other derivatives of N‐substituted glycines. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.     

Molecular determinants of the pathogenesis of disease due to non-typable Haemophilus influenzae

Non-typable Haemophilus influenzae is a common commensal organism in the human upper respiratory tract and an important cause of localized respiratory tract disease. The pathogenesis of disease begins with bacterial colonization of the nasopharynx, a process that involves establishment on the mucosal surface and evasion of local immune mechanisms. Under the proper circumstances, the organism spreads contiguously to the middle ear, the sinuses, or the lungs, and then stimulates a brisk inflammatory response, producing symptomatic infection. In this review, we summarize our present understanding of the molecular determinants of this sequence of events. Continued investigation of the molecular mechanism of non-typable H. influenzae pathogenicity should facilitate development of novel approaches to the treatment and prevention of H. influenzae disease.     

Protocadherin-18a has a role in cell adhesion, behavior and migration in zebrafish development

Protocadherin-18a (Pcdh18a) belongs to the δ2-protocadherins, which constitute the largest subgroup within the cadherin superfamily. Here we present isolation of a full-length zebrafish cDNA that encodes a protein highly similar to human and mouse Pcdh18. Zebrafish pcdh18a is expressed in a complex and dynamic pattern in the nervous system from gastrula stages onward, with lesser expression in mesodermal derivatives. Pcdh18a-eGFP fusion protein is expressed in a punctate manner on the membranes between cells. Overexpression of pcdh18a in embryos caused cyclopia, mislocalization of hatching gland tissue, and duplication or splitting of the neural tube. Most neural markers tested were expressed in an approximately correct A-P pattern. By cell transplantation we showed that overexpression of pcdh18a causes diminished cell migration and reduced cell protrusions, resulting in a tendency of cells to stay more firmly aggregated, probably due to increased cell adhesion. In contrast, knockdown of pcdh18a by a morpholino oligonucleotide caused defects in epiboly, and led to reduced cell adhesion as shown by cell dissociation, sorting and transplantation experiments. These results suggest a role for Pcdh18a in cell adhesion, migration and behavior but not cell specification during gastrula and segmentation stages of development.     

Structural characterization of the ribosomal P1A-P2B protein dimer by small-angle X-ray scattering and NMR spectroscopy

The five ribosomal P-proteins, denoted P0-(P1-P2)2, constitute the stalk structure of the large subunit of eukaryotic ribosomes. In the yeast Saccharomyces cerevisiae, the group of P1 and P2 proteins is differentiated into subgroups that form two separate P1A-P2B and P1B-P2A heterodimers on the stalk. So far, structural studies on the P-proteins have not yielded any satisfactory information using either X-ray crystallography or NMR spectroscopy, and the structures of the ribosomal stalk and its individual constituents remain obscure. Here we outline a first, coarse-grained view of the P1A-P2B solution structure obtained by a combination of small-angle X-ray scattering and heteronuclear NMR spectroscopy. The complex has an elongated shape with a length of 10 nm and a cross section of approximately 2.5 nm. 15N NMR relaxation measurements establish that roughly 30% of the residues are present in highly flexible segments, which belong primarily to the linker region and the C-terminal part of the polypeptide chain. Secondary structure predictions and NMR chemical shift analysis, together with previous results from CD spectroscopy, indicate that the structured regions involve alpha-helices. NMR relaxation data further suggest that several helices are arranged in a nearly parallel or antiparallel topology. These results provide the first structural comparison between eukaryotic P1 and P2 proteins and the prokaryotic L12 counterpart, revealing considerable differences in their overall shapes, despite similar functional roles and similar oligomeric arrangements. These results present for the first time a view of the structure of the eukaryotic stalk constituents, which is the only domain of the eukaryotic ribosome that has escaped successful structural characterization.     

Alpha2 Macroglobulin-Like Is Essential for Liver Development in Zebrafish

Background

Alpha 2 Macroglobulin family members have been studied extensively with respect to their roles in physiology and human disease including innate immunity and Alzheimer''s disease, but little is known about a possible role in liver development loss-of-function in model systems.

Principal Findings

We report the isolation of the zebrafish α2 macroglobulin-like (A2ML) gene and its specific expression in the liver during differentiation. Morpholino-based knock-down of A2ML did not block the initial formation of the liver primordium, but inhibited liver growth and differentiation.

Significance

This report on A2ML function in zebrafish development provides the first evidence for a specific role of an A2M family gene in liver formation during early embryogenesis in a vertebrate.