Modern approach for complex treatment of odontogenic maxillary sinusitis

Introduction: Odontogenic maxillary sinusitis is associated with diseases of the maxillary teeth. The close anatomical relationship of these teeth with the floor of the maxillary sinus leads to violation of the integrity of its mucosa and creates prerequisites for the infection to pass into the sinus cavity. Odontogenic maxillary sinusitis is characterized by dental complaints and the typical symptoms of all rhinosinusitis. There is lack of consensus in the literature on the algorithm of behaviour in these cases.Aim: To recommend a contemporary algorythm of management in patients with odontogenic maxillary sinuitis, which is consistent with both the established rules for the treatment of rhinosinusitis and the individual characteristics of each clinical case.Materials and methods: For the period 2001-2021, 157 patients were treated at St. George University Hospital, after extraction of an upper tooth (4-6) or with symptoms of nasal breathing difficulties and unilateral whitish secretion with an unpleasant odour. All of them had a history of dental intervention and CT data for changes in the osteomeatal complex or „foreign bodies“ in the maxillary sinus.Results: All patients were discharged on the third day after admission in improved general condition without complaints. No late postoperative complications were observed. In 8 of the patients with sinuscopy, after the control CT examination, performed a month later, a second intervention was necessary for the extraction of residual fungal material.Conclusion: The treatment of odontogenic maxillary sinusitis involves interdisciplinary approach of otorhinolaryngologists and dental specialists. However, modern understanding of the functioning of the nasal cavities and the development of pathological processes in them help us to build and present an adequate concept for diagnosis and therapeutic behavior

The youth movement Nashi: contentious politics, civil society, and party politics

The youth movement Nashi was established in Russia with the support of the Putin regime in 2005. The success of anti-regime demonstrators in Ukraine's ‘Orange Revolution’ in 2004 had been noted in Moscow, and Nashi's role was to serve as a pro-regime force to be mobilised against the opposition. Its focus was the contentious politics of the street. Nashi represents an interesting theoretical case from the perspective of contentious politics and its relationship with civil society and formal party politics. Nashi's role has developed to include facilitating young people's engagement with party politics and business. Its early centralised control has been ameliorated somewhat by a reorganisation focused on local action. Nonetheless, Nashi exists with state support. Its continued role in contentious politics in support of the Putin regime, for example, countering opposition demonstrations in Moscow in December 2011, makes its identification as a component of democratic civil society problematic

Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM

The β-barrel assembly machinery (BAM) is a ~203 kDa complex of five proteins (BamA-E) which is essential for viability in E. coli. BAM promotes the folding and insertion of β-barrel proteins into the outer membrane via a poorly understood mechanism. Several current models suggest that BAM functions through a ‘lateral gating’ motion of the β-barrel of BamA. Here we present a cryo-EM structure of the BamABCDE complex, at 4.9 Å resolution. The structure is in a laterally open conformation showing that gating is independent of BamB binding. We describe conformational changes throughout the complex, and interactions between BamA, B, D, and E and the detergent micelle that suggest communication between BAM and the lipid bilayer. Finally, using an enhanced reconstitution protocol and functional assays, we show that for the outer membrane protein OmpT, efficient folding in vitro requires lateral gating in BAM

Identification and Characterization of the Lamprey High-Mobility Group Box 1 Gene

High-mobility group box 1 (HMGB1), a highly conserved DNA-binding protein, plays an important role in maintaining nucleosome structures, transcription, and inflammation. We identified a homolog of HMGB1 in the Japanese lamprey (Lampetra japonica). The Lampetra japonica HMGB1 gene (Lj-HMGB1) has over 70% sequence identity with its homologs in jawed vertebrates. Despite the reasonably high sequence identity with other HMGB1 proteins, Lj-HMGB1 did not group together with these proteins in a phylogenetic analysis. We examined Lj-HMGB1 expression in lymphocyte-like cells, and the kidneys, heart, gills, and intestines of lampreys before and after the animals were challenged with lipopolysaccharide (LPS) and concanavalin A (ConA). Lj-HMGB1 was initially expressed at a higher level in the heart, but after treatment with LPS and ConA only the gills demonstrated a significant up-regulation of expression. The recombinant Lj-HMGB1 (rLj-HMGB1) protein bound double-stranded DNA and induced the proliferation of human adenocarcinoma cells to a similar extent as human HMGB1. We further revealed that Lj-HMGB1 was able to induce the production of tumor necrosis factor-α (TNF-α), a pro-inflammatory mediator, in activated human acute monocytic leukemia cells. These results suggest that lampreys use HMGB1 to activate their innate immunity for the purpose of pathogen defense

A Modular BAM Complex in the Outer Membrane of the α-Proteobacterium Caulobacter crescentus

Mitochondria are organelles derived from an intracellular α-proteobacterium. The biogenesis of mitochondria relies on the assembly of β-barrel proteins into the mitochondrial outer membrane, a process inherited from the bacterial ancestor. Caulobacter crescentus is an α-proteobacterium, and the BAM (β-barrel assembly machinery) complex was purified and characterized from this model organism. Like the mitochondrial sorting and assembly machinery complex, we find the BAM complex to be modular in nature. A ∼150 kDa core BAM complex containing BamA, BamB, BamD, and BamE associates with additional modules in the outer membrane. One of these modules, Pal, is a lipoprotein that provides a means for anchorage to the peptidoglycan layer of the cell wall. We suggest the modular design of the BAM complex facilitates access to substrates from the protein translocase in the inner membrane

Laforin, a Dual Specificity Phosphatase Involved in Lafora Disease, Is Present Mainly as Monomeric Form with Full Phosphatase Activity

Lafora Disease (LD) is a fatal neurodegenerative epileptic disorder that presents as a neurological deterioration with the accumulation of insoluble, intracellular, hyperphosphorylated carbohydrates called Lafora bodies (LBs). LD is caused by mutations in either the gene encoding laforin or malin. Laforin contains a dual specificity phosphatase domain and a carbohydrate-binding module, and is a member of the recently described family of glucan phosphatases. In the current study, we investigated the functional and physiological relevance of laforin dimerization. We purified recombinant human laforin and subjected the monomer and dimer fractions to denaturing gel electrophoresis, mass spectrometry, phosphatase assays, protein-protein interaction assays, and glucan binding assays. Our results demonstrate that laforin prevalently exists as a monomer with a small dimer fraction both in vitro and in vivo. Of mechanistic importance, laforin monomer and dimer possess equal phosphatase activity, and they both associate with malin and bind glucans to a similar extent. However, we found differences between the two states' ability to interact simultaneously with malin and carbohydrates. Furthermore, we tested other members of the glucan phosphatase family. Cumulatively, our data suggest that laforin monomer is the dominant form of the protein and that it contains phosphatase activity