Age estimation using carpals: study of a Slovenian sample to test Cameriere\u2019s method

Carpals are often used as age indicators. In a recent study, Cameriere et al. studied the use of the ratio between the total area of carpal bones and epiphyses of the ulna and radius (Bo) and carpals (Ca) as age indicators. The present study, of a sample of 158 Slovenian children and adolescents aged between 6 and 16 years, focused on analysing the best regression for age estimation. The regression model yielded the following equation:age = 3.411 + 0.942g + 20.927(Bo/Ca), and explained 91.6% of total variance (R2 = 0.916). The median of the absolute values of residuals (observed age minus predicted age) was 0.09 years, with a quartile deviation of 0.786 years, and a standard error of estimate of 0.658 years. Comparisons between the previous equation referring to Slovenian children and the equivalent linear equation proposed by Cameriere et al. did not reveal any significant differences between the intercepts and slopes of the two linear models. These results suggested a common regression model for both Italian and Slovenian samples. The common regression model, describing age as a linear function of gender and Bo/Ca ratio, yielded the following linear regression formula: age = 2.907 + 0.408g + 20.757(Bo/Ca). This model explained 86% of total variance (R2 = 0.86). The median of the absolute values of residuals (observed age minus predicted age) was 0.02 years, with a quartile deviation of 1.02 years and a standard error of estimate of 0.96 years

Three-dimensional structure of a viral genome-delivery portal vertex.

DNA viruses such as bacteriophages and herpesviruses deliver their genome into and out of the capsid through large proteinaceous assemblies, known as portal proteins. Here, we report two snapshots of the dodecameric portal protein of bacteriophage P22. The 3.25-Å-resolution structure of the portal-protein core bound to 12 copies of gene product 4 (gp4) reveals a ~1.1-MDa assembly formed by 24 proteins. Unexpectedly, a lower-resolution structure of the full-length portal protein unveils the unique topology of the C-terminal domain, which forms a ~200-Å-long α-helical barrel. This domain inserts deeply into the virion and is highly conserved in the Podoviridae family. We propose that the barrel domain facilitates genome spooling onto the interior surface of the capsid during genome packaging and, in analogy to a rifle barrel, increases the accuracy of genome ejection into the host cell

Evaluation of the contribution of ion exchange in the process of demanganization with modified cation exchange resin KU-2-8.

An effective method of water purification from manganese compounds is the use of magnetite, so it is advisable to improve the way it is used. The main disadvantage of using dispersed microcrystalline magnetite is the difficulty of implementing water purification in dynamic conditions, due to the significant resistance to water filtration. In the case of the use of magnetite in static conditions, there is a constant consumption of magnetite after settling and filtration, and the demanganization process requires the use of bulky and poorly mobile installations (mixers, settling tanks and filters). Therefore, water purification from manganese ions was carried out under dynamic conditions by filtering water through a layer of strong acid cation exchange resin KU-2-8 in H+, Na+, Ca2+ forms modified with magnetite. This allows constant contact of the solution with the ion exchange material and reduces the role of the limiting diffusion factor on the water purification process. When evaluating the effectiveness of cation exchange resin KU-2-8 in the extraction of Mn2+ ions from water depending on the form of the resin, it was found that the FEDC for the resin in H+ form is 2198 mg-eq/dm3, for Na+ it is 2175 mg-eq/dm3 and for Ca2+ the value is 1717 mg-eq/dm3. Therefore, during the transition from H+ to Na+ and to Ca2+ form there is a decrease in the sorption capacity for Mn2+ ions in the cation exchange resin KU-2-8. On the cation exchange resin in Ca2+ form the efficiency of demanganization decreases with increasing concentration of manganese ions. When increasing the initial concentration from 5 to 10 and 30 mg/dm3 in distilled water, the residual concentration increases from 0.14 to 0.35 and up to 1.95 mg/dm3 when filtered through 10 cm3 of resin in Ca2+ form. When removing Mn2+ ions from artesian water, the residual concentration was 4.0; 7.0 and 27.0 mg/dm3 respectively. Thus, on magnetite-modified cation exchange resin, manganese ions are removed only partially due to ion exchange and their complete removal from water is possible only due to catalytic oxidation and deposition on magnetite

Application of aluminium coagulants for the removal of sulphate from mine water

he results of treatment of solutions with high sulphates concentration and the high rate of water hardness are given. It is shown that the significant reduction of secondary pollution by chlorides achieved through an integrated use of aluminium hydroxchloride and sodium aluminate coagulants. It was found that the efficiency of water purification of sulphates and water softening can be increased with the carbon dioxide processing

Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses

Unlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 Å resolution of Rosellinia necatrix quadrivirus 1 (RnQV1), a fungal double-stranded (ds)RNA virus. RnQV1, the type species of the family Quadriviridae, has a multipartite genome consisting of four monocistronic segments. Whereas most dsRNA virus capsids are based on dimers of a single protein, the ~450-Å-diameter, T = 1 RnQV1 capsid is built of P2 and P4 protein heterodimers, each with more than 1000 residues. Despite a lack of sequence similarity between the two proteins, they have a similar α-helical domain, the structural signature shared with the lineage of the dsRNA bluetongue virus-like viruses. Domain insertions in P2 and P4 preferential sites provide additional functions at the capsid outer surface, probably related to enzyme activity. The P2 insertion has a fold similar to that of gelsolin and profilin, two actin-binding proteins with a function in cytoskeleton metabolism, whereas the P4 insertion suggests protease activity involved in cleavage of the P2 383-residue C-terminal region, absent in the mature viral particle. Our results indicate that the intimate virus-fungus partnership has altered the capsid genome-protective and/or receptor-binding functions. Fungal virus evolution has tended to allocate enzyme activities to the virus capsid outer surface

Fructose-1,6-Bisphosphatase Overexpression in Pancreatic β-Cells Results in Reduced Insulin Secretion : A New Mechanism for Fat-Induced Impairment of β-Cell Function

OBJECTIVE—Fructose-1,6-bisphosphatase (FBPase) is a gluconeogenic enzyme that is upregulated in islets or pancreatic β-cell lines exposed to high fat. However, whether specific β-cell upregulation of FBPase can impair insulin secretory function is not known. The objective of this study therefore is to determine whether a specific increase in islet β-cell FBPase can result in reduced glucose-mediated insulin secretion

Depolarization-Evoked Secretion Requires Two Vicinal Transmembrane Cysteines of Syntaxin 1A

BACKGROUND: The interactions of the voltage-gated Ca(2+) channel (VGCC) with syntaxin 1A (Sx 1A), Synaptosome-associated protein of 25 kD (SNAP-25), and synaptotagmin, couple electrical excitation to evoked secretion. Two vicinal Cys residues, Cys 271 and Cys 272 in the Sx 1A transmembrane domain, are highly conserved and participate in modulating channel kinetics. Each of the Sx1A Cys mutants, differently modify the kinetics of Cav1.2, and neuronal Cav2.2 calcium channel. METHODOLOGY/PRINCIPLE FINDINGS: We examined the effects of various Sx1A Cys mutants and the syntaxin isoforms 2, 3, and 4 each of which lack vicinal Cys residues, on evoked secretion, monitoring capacitance transients in a functional release assay. Membrane capacitance in Xenopus oocytes co-expressing Cav1.2, Sx1A, SNAP-25 and synaptotagmin, which is Bot C- and Bot A-sensitive, was elicited by a double 500 ms depolarizing pulse to 0 mV. The evoked-release was obliterated when a single Cys Sx1A mutant or either one of the Sx isoforms were substituted for Sx 1A, demonstrating the essential role of vicinal Cys residues in the depolarization mediated process. Protein expression and confocal imaging established the level of the mutated proteins in the cell and their targeting to the plasma membrane. CONCLUSIONS/SIGNIFICANCE: We propose a model whereby the two adjacent transmembranal Cys residues of Sx 1A, lash two calcium channels. Consistent with the necessity of a minimal fusion complex termed the excitosome, each Sx1A is in a complex with SNAP-25, Syt1, and the Ca(2+) channel. A Hill coefficient >2 imply that at least three excitosome complexes are required for generating a secreting hetero-oligomer protein complex. This working model suggests that a fusion pore that opens during membrane depolarization could be lined by alternating transmembrane segments of Sx1A and VGCC. The functional coupling of distinct amino acids of Sx 1A with VGCC appears to be essential for depolarization-evoked secretion

A “Coiled-Coil” Motif Is Important for Oligomerization and DNA Binding Properties of Human Cytomegalovirus Protein UL77

Human cytomegalovirus (HCMV) UL77 gene encodes the essential protein UL77, its function is characterized in the present study. Immunoprecipitation identified monomeric and oligomeric pUL77 in HCMV infected cells. Immunostaining of purified virions and subviral fractions showed that pUL77 is a structural protein associated with capsids. In silico analysis revealed the presence of a coiled-coil motif (CCM) at the N-terminus of pUL77. Chemical cross-linking of either wild-type pUL77 or CCM deletion mutant (pUL77ΔCCM) implicated that CCM is critical for oligomerization of pUL77. Furthermore, co-immunoprecipitations of infected and transfected cells demonstrated that pUL77 interacts with the capsid-associated DNA packaging motor components, pUL56 and pUL104, as well as the major capsid protein. The ability of pUL77 to bind dsDNA was shown by an in vitro assay. Binding to certain DNA was further confirmed by an assay using biotinylated 36-, 250-, 500-, 1000-meric dsDNA and 966-meric HCMV-specific dsDNA designed for this study. The binding efficiency (BE) was determined by image processing program defining values above 1.0 as positive. While the BE of the pUL56 binding to the 36-mer bio-pac1 containing a packaging signal was 10.0±0.63, the one for pUL77 was only 0.2±0.03. In contrast to this observation the BE of pUL77 binding to bio-500 bp or bio-1000 bp was 2.2±0.41 and 4.9±0.71, respectively. By using pUL77ΔCCM it was demonstrated that this protein could not bind to dsDNA. These data indicated that pUL77 (i) could form homodimers, (ii) CCM of pUL77 is crucial for oligomerization and (iii) could bind to dsDNA in a sequence independent manner

Viral nanomotors for packaging of dsDNA and dsRNA

While capsid proteins are assembled around single-stranded genomic DNA or RNA in rod-shaped viruses, the lengthy double-stranded genome of other viruses is packaged forcefully within a preformed protein shell. This entropically unfavourable DNA or RNA packaging is accomplished by an ATP-driven viral nanomotor, which is mainly composed of two components, the oligomerized channel and the packaging enzymes. This intriguing DNA or RNA packaging process has provoked interest among virologists, bacteriologists, biochemists, biophysicists, chemists, structural biologists and computational scientists alike, especially those interested in nanotechnology, nanomedicine, AAA+ family proteins, energy conversion, cell membrane transport, DNA or RNA replication and antiviral therapy. This review mainly focuses on the motors of double-stranded DNA viruses, but double-stranded RNA viral motors are also discussed due to interesting similarities. The novel and ingenious configuration of these nanomotors has inspired the development of biomimetics for nanodevices. Advances in structural and functional studies have increased our understanding of the molecular basis of biological movement to the point where we can begin thinking about possible applications of the viral DNA packaging motor in nanotechnology and medical applications