An Intraneural Ganglion Cyst causing Foot Drop: A Case Report

A 46 year old male with a past medical history of HTN and chronic pancreatitis presented to clinic with a chief complaint of right leg weakness and numbness/tingling that developed suddenly two months prior to presentation. He denied history of trauma or surgery to the right lower extremity. Physical exam revealed a right foot drop on ambulation with slight circumduction of right leg. Further neurological exam was remarkable for 2/5 muscle strength in right ankle dorsiflexion and eversion, with decreased sensation noted on right foot dorsal surface and lateral calf. EMG demonstrated a right common peroneal mononeuropathy at the knee with demyelinating and axonal features with active denervation. Ultrasound of the right knee showed enlargement of the right common peroneal nerve at the level of the fibular head with a1.1 x 0.5 x 1.6 cm hypoechoic collection in the region of the tibiofibular joint, possibly representing a ganglion cyst from the adjacent joint or an intraneural ganglion cyst. Follow-up MRI re-demonstrated a cystic lesion just medial to the common peroneal nerve and posterior to the proximal tibiofibular joint, which is suspected to arise from the articular branch of the common peroneal nerve. Patient had symptomatic improvement with physical therapy and use of a AFO boot for 2 months. The most common cause of foot drop is a compression peroneal neuropathy, often at the location of the neck of the fibula. In rare instances, the compression can occur due to a ganglion cyst, which is a benign tumor consisting of gelatinous material that is typically asymptomatic. Ganglion cysts compressing the peroneal nerve can be either intraneural or extraneural, with differentiation occurring via imaging. Intraneural ganglion cysts are non-neoplastic mucinous cysts located within the epineurium of a nerve. Although the exact pathogenesis of these cysts are unknown, it has been show in multiple case reports that as these cysts expand within the epineurium, they can cause compression of the adjacent nerve fascicles. Diagnosis is primarily via MRI; although an EMG study may assist in correlating clinical findings by distinguishing the extent of sensory and motor impairment. Treatment guidelines of peroneal intraneural ganglia are controversial. Current first line treatment recommendations endorse surgical removal of the ganglion cyst; however, it may be less invasive and beneficial to start with a conservative approach to minimize unwarranted procedures in patients. Ultimately, successful outcomes are based on early diagnosis and treatment.https://scholarlycommons.henryford.com/merf2020caserpt/1092/thumbnail.jp

Diffusion and Dopant Activation in Germanium:Insights from Recent Experimental and Theoretical Results

Germanium is an important mainstream material for many nanoelectronic and sensor applications. The understanding of diffusion at an atomic level is important for fundamental and technological reasons. In the present review, we focus on the description of recent studies concerning n-type dopants, isovalent atoms, p-type dopants, and metallic and oxygen diffusion in germanium. Defect engineering strategies considered by the community over the past decade are discussed in view of their potential application to other systems

Rifampicin-Independent Interactions between the Pregnane X Receptor Ligand Binding Domain and Peptide Fragments of Coactivator and Corepressor Proteins

The pregnane X receptor (PXR), a member of the nuclear receptor superfamily, regulates the expression of drug-metabolizing enzymes in a ligand-dependent manner. The conventional view of nuclear receptor action is that ligand binding enhances the receptor's affinity for coactivator proteins, while decreasing its affinity for corepressors. To date, however, no known rigorous biophysical studies have been conducted to investigate the interaction among PXR, its coregulators, and ligands. In this work, steady-state total internal reflection fluorescence microscopy (TIRFM) and total internal reflection with fluorescence recovery after photobleaching were used to measure the thermodynamics and kinetics of the interaction between the PXR ligand binding domain and a peptide fragment of the steroid receptor coactivator-1 (SRC-1) in the presence and absence of the established PXR agonist, rifampicin. Equilibrium dissociation and dissociation rate constants of ~5 μM and ~2 s(-1), respectively, were obtained in the presence and absence of rifampicin, indicating that the ligand does not enhance the affinity of the PXR and SRC-1 fragments. Additionally, TIRFM was used to examine the interaction between PXR and a peptide fragment of the corepressor protein, the silencing mediator for retinoid and thyroid receptors (SMRT). An equilibrium dissociation constant of ~70 μM was obtained for SMRT in the presence and absence of rifampicin. These results strongly suggest that the mechanism of ligand-dependent activation in PXR differs significantly from that seen in many other nuclear receptors

Structure and lithium transport pathways in Li₂FeSiO₄ cathodes for lithium batteries

The importance of exploring new low-cost and safe cathodes for large-scale lithium batteries has led to increasing interest in Li(2)FeSiO(4). The structure of Li(2)FeSiO(4) undergoes significant change on cycling, from the as-prepared γ(s) form to an inverse β(II) polymorph; therefore it is important to establish the structure of the cycled material. In γ(s) half the LiO(4), FeO(4), and SiO(4) tetrahedra point in opposite directions in an ordered manner and exhibit extensive edge sharing. Transformation to the inverse β(II) polymorph on cycling involves inversion of half the SiO(4), FeO(4), and LiO(4) tetrahedra, such that they all now point in the same direction, eliminating edge sharing between cation sites and flattening the oxygen layers. As a result of the structural changes, Li(+) transport paths and corresponding Li-Li separations in the cycled structure are quite different from the as-prepared material, as revealed here by computer modeling, and involve distinct zigzag paths between both Li sites and through intervening unoccupied octahedral sites that share faces with the LiO(4) tetrahedra

Tumor Cell Marker PVRL4 (Nectin 4) Is an Epithelial Cell Receptor for Measles Virus

Vaccine and laboratory adapted strains of measles virus can use CD46 as a receptor to infect many human cell lines. However, wild type isolates of measles virus cannot use CD46, and they infect activated lymphocytes, dendritic cells, and macrophages via the receptor CD150/SLAM. Wild type virus can also infect epithelial cells of the respiratory tract through an unidentified receptor. We demonstrate that wild type measles virus infects primary airway epithelial cells grown in fetal calf serum and many adenocarcinoma cell lines of the lung, breast, and colon. Transfection of non-infectable adenocarcinoma cell lines with an expression vector encoding CD150/SLAM rendered them susceptible to measles virus, indicating that they were virus replication competent, but lacked a receptor for virus attachment and entry. Microarray analysis of susceptible versus non-susceptible cell lines was performed, and comparison of membrane protein gene transcripts produced a list of 11 candidate receptors. Of these, only the human tumor cell marker PVRL4 (Nectin 4) rendered cells amenable to measles virus infections. Flow cytometry confirmed that PVRL4 is highly expressed on the surfaces of susceptible lung, breast, and colon adenocarcinoma cell lines. Measles virus preferentially infected adenocarcinoma cell lines from the apical surface, although basolateral infection was observed with reduced kinetics. Confocal immune fluorescence microscopy and surface biotinylation experiments revealed that PVRL4 was expressed on both the apical and basolateral surfaces of these cell lines. Antibodies and siRNA directed against PVRL4 were able to block measles virus infections in MCF7 and NCI-H358 cancer cells. A virus binding assay indicated that PVRL4 was a bona fide receptor that supported virus attachment to the host cell. Several strains of measles virus were also shown to use PVRL4 as a receptor. Measles virus infection reduced PVRL4 surface expression in MCF7 cells, a property that is characteristic of receptor-associated viral infections

Structural and Mechanistic Studies of Measles Virus Illuminate Paramyxovirus Entry

Measles virus (MeV), a member of the paramyxovirus family of enveloped RNA viruses and one of the most infectious viral pathogens identified, accounts for major pediatric morbidity and mortality worldwide although coordinated efforts to achieve global measles control are in place. Target cell entry is mediated by two viral envelope glycoproteins, the attachment (H) and fusion (F) proteins, which form a complex that achieves merger of the envelope with target cell membranes. Despite continually expanding knowledge of the entry strategies employed by enveloped viruses, our molecular insight into the organization of functional paramyxovirus fusion complexes and the mechanisms by which the receptor binding by the attachment protein triggers the required conformational rearrangements of the fusion protein remain incomplete. Recently reported crystal structures of the MeV attachment protein in complex with its cellular receptors CD46 or SLAM and newly developed functional assays have now illuminated some of the fundamental principles that govern cell entry by this archetype member of the paramyxovirus family. Here, we review these advances in our molecular understanding of MeV entry in the context of diverse entry strategies employed by other members of the paramyxovirus family

The First Human Epitope Map of the Alphaviral E1 and E2 Proteins Reveals a New E2 Epitope with Significant Virus Neutralizing Activity

Although the murine immune response to Venezuelan equine encephalitis virus (VEEV) is well-characterized, little is known about the human antibody response to VEEV. In this study we used phage display technology to isolate a panel of 11 VEEV-specfic Fabs from two human donors. Seven E2-specific and four E1-specific Fabs were identified and mapped to five E2 epitopes and three E1 epitopes. Two neutralizing Fabs were isolated, E2-specific F5 and E1-specific L1A7, although the neutralizing capacity of L1A7 was 300-fold lower than F5. F5 Fab was expressed as a complete IgG1 molecule, F5 native (n) IgG. Neutralization-escape VEEV variants for F5 nIgG were isolated and their structural genes were sequenced to determine the theoretical binding site of F5. Based on this sequence analysis as well as the ability of F5 to neutralize four neutralization-escape variants of anti-VEEV murine monoclonal antibodies (mapped to E2 amino acids 182–207), a unique neutralization domain on E2 was identified and mapped to E2 amino acids 115–119