A Recurrent Case of Targetoid Hemosiderotic Hemangioma: A Case Report and a Comprehensive Review of the Literature

Targetoid hemosiderotic hemangioma is an acquired vascular malformation of unknown origin. We report the case of a 31-year-old man with a recurrent and spontaneous regressive targetoid hemosiderotic hemangioma. Diagnosis relied on clinical and histological findings. Physical examination revealed presence of an approximately 2 cm targetoid lesion located on the left arm, and associated with pain after pressure. No trigger agent (trauma, insect sting) was reported. Dermoscopy showed a group of red lacunae centrally, encircled by an intermediate yellow circular homogenous area and a red violaceous homogenous ring in the periphery. The histopathological examination and the immunohistochemical staining of the lesion were characteristic for a hemangioma-like proliferation of vessels in the upper part of the dermis, similar to a targetoid hemosiderotic angioma. We also review epidemiological, clinical, and histopathological findings in 6 similar cases presented in the literature. Spontaneous regression and recurrence have rarely been described in this type of skin lesion

Starting grassroots initiatives to foster equity, diversity, and inclusivity in the Chemistry Department at the University of Alberta

Abstract: The University of Alberta Working for Inclusivity in Chemistry (UAWIC) group was formed in 2017 to increase equity, diversity, and inclusion in the Department of Chemistry. With the goals of fostering a community amongst department members and retaining a diverse graduate student population, UAWIC has created initiatives addressing equity, diversity and inclusivity, professional development, and promoted visibility of diversity within the department. Training students how to overcome systemic barriers and providing platforms to share experiences will help aspiring chemists prepare for future career paths and develop a network of mentors and colleagues

Molecular diagnosis of anti-laminin 332 (epiligrin) mucous membrane pemphigoid

Background: Mucous membrane pemphigoid is a group of chronic subepithelial autoimmune blistering diseases that mainly affect mucous membranes. Laminin 332-specific autoantibodies are present in approximately 1/3 of the patients, being associated with an increased risk of malignancy. Because of the severe complications, an early recognition of the disease allowing a timely therapy is essential. The gold standard methods for detection of laminin 332-specific autoantibodies, including the immunoprecipitation and immunoblotting are non-quantitative, laborious and restricted to a few specialized laboratories worldwide. In addition, the use of radioimmunoassays, although highly sensitive and specific, are laborious, expensive and tightly regulated. Therefore, there is a stringent need for a quantitative immunoassay for the routine detection of laminin 332-specific autoantibodies more broadly available to diagnostic laboratories. The aim of this study was to compare different antigenic substrates, including native, recombinant laminin 332 and laminin 332-rich keratinocyte extracellular matrix, for development of an ELISA to detect autoantibodies in mucous membrane pemphigoid. Results: Using a relatively large number of sera from MMP patients with well-characterized autoantibody reactivity we show the suitability of ELISA systems using laminin 332 preparations as adjunct diagnostic tools in MMP. While glycosylation of laminin 332 does not appear to influence its recognition by MMP autoantibodies, ELISA systems using both purified, native and recombinant laminin 332 demonstrated a high sensitivity and good correlation with the detection of autoantibodies by immunoblotting. ELISA systems using different laminin 332 preparations represent a feasible and more accessible alternative for a broad range of laboratories. Conclusions: Our findings qualify the use of immunoassays with the laminin 332-rich preparations as an ancillary diagnostic tool in mucous membrane pemphigoid

Phenotypic and genotypic study of carbapenem-resistant Pseudomonas aeruginosa strains isolated from hospitalized patients

Introduction: Nosocomial infections caused by Pseudomonas aeruginosa producing carbapenemases represent an important cause of morbidity and mortality among immunosuppressed patients. The aim of our study was to detect the production of metallo-carbapenemases (MBLs) by phenotypic methods and to detect the presence of the MBLs encoding genes (blaIMP and blaVIM) by PCR in P. aeruginosa strains isolated from hospitalized patients to the Regional Institute of Gastroenterology and Hepatology, Cluj-Napoca

Dissecting the binding interactions of teixobactin with the bacterial cell wall precursor lipid II

The prevalence of life‐threatening, drug‐resistant microbial infections has challenged researchers to consider alternatives to currently available antibiotics. Teixobactin is a recently discovered “resistance‐proof” antimicrobial peptide that targets the bacterial cell wall precursor lipid II. In doing so, teixobactin exhibits potent antimicrobial activity against a wide range of Gram‐positive organisms. Herein we demonstrate that teixobactin and several structural analogues are capable of binding lipid II from both Gram‐positive and Gram‐negative bacteria. Furthermore, we show that when combined with known outer membrane‐disrupting peptides, teixobactin is active against Gram‐negative organisms.</p

Molecular Engineering of <i>E. coli</i> Bacterioferritin: A Versatile Nanodimensional Protein Cage

Currently, intense interest is focused on the discovery and application of new multisubunit cage proteins and spherical virus capsids to the fields of bionanotechnology, drug delivery, and diagnostic imaging as their internal cavities can serve as hosts for fluorophores or bioactive molecular cargo. Bacterioferritin is unusual in the ferritin protein superfamily of iron-storage cage proteins in that it contains twelve heme cofactors and is homomeric. The goal of the present study is to expand the capabilities of ferritins by developing new approaches to molecular cargo encapsulation employing bacterioferritin. Two strategies were explored to control the encapsulation of a diverse range of molecular guests compared to random entrapment, a predominant strategy employed in this area. The first was the inclusion of histidine-tag peptide fusion sequences within the internal cavity of bacterioferritin. This approach allowed for the successful and controlled encapsulation of a fluorescent dye, a protein (fluorescently labeled streptavidin), or a 5 nm gold nanoparticle. The second strategy, termed the heme-dependent cassette strategy, involved the substitution of the native heme with heme analogs attached to (i) fluorescent dyes or (ii) nickel-nitrilotriacetate (NTA) groups (which allowed for controllable encapsulation of a histidine-tagged green fluorescent protein). An in silico docking approach identified several small molecules able to replace the heme and capable of controlling the quaternary structure of the protein. A transglutaminase-based chemoenzymatic approach to surface modification of this cage protein was also accomplished, allowing for future nanoparticle targeting. This research presents novel strategies to control a diverse set of molecular encapsulations and adds a further level of sophistication to internal protein cavity engineering

Stretching Peptides

Advances in the modulation of protein-protein interactions (PPIs) enable the characterization of PPI networks that govern disease mechanisms and guide the design of novel therapeutics and probes. These PPIs are often characterized by complementary binding to shallow protein surfaces that are challenging to target using standard methods for high-affinity small molecule ligand generation. Compared to linear peptides, synthetically constrained epitopes provide an energetic advantage for binding PPI surfaces by decreasing unbound-state entropy. Such peptide stapling strategies promoting α-helix and β-hairpin structures are well developed. However, approaches for accessing common extended backbone structures are limited. Here we demonstrate the incorporation of a rigid, linear, diyne brace between side chains at the i to i+2 positions to generate a family of low molecular weight peptide macrocycles adopting extended backbones. We show by NMR and DFT studies that these ‘stretched peptides’ adopt rigid and stable conformations in solution which can be tuned to explore a wide range of extended peptide conformational space, including those inherent to β-strands and polyproline II (PPII) helices. The formation of the diyne brace is accomplished in excellent conversions (>95%) and is amenable to high throughput synthesis. The minimalist structure-inducing tripeptide core (< 300 Da) is amenable to further synthetic elaboration to optimize bioactivity and pharmacokinetics. We showcase the utility of diyne-braced peptides with the synthesis of macrocyclic inhibitors of bacterial signal 1 peptidase

Additional file 1: of Molecular diagnosis of anti-laminin 332 (epiligrin) mucous membrane pemphigoid

Figure S1. Comparative analysis of serum reactivity with the extracellular matrix and native laminin 332 by ELISA in control patients. Box plots represent optical density measurements of serum reactivity from patients with pemphigus vulgaris (PV, n = 20), epidermolysis bullosa acquisita (EBA, n = 20) and dermatits herpetiformis (DH, n = 20) as well as from healthy donors (n = 4) measured in parallel on native laminin 332 and laminin-rich extracellular matrix of keratinocytes. (PNG 20 kb