[Nurse coordinators and IPAs in Parkinson's expert centers: what are their roles?] / Infirmières coordinatrices et IPA en centre expert Parkinson : quels sont leurs rôles ?

The creation of Parkinson's expert centers (PEC) led to the emergence of new nurses, known as coordination nurses. And in 2018, the emergence of advanced practice nursing led to the creation of a new category of professionals, advanced practice nurses (APN). Nurses coordinators and APN play a major role in meeting the public health challenges posed by Parkinson's disease. They are the guarantors of the implementation of a personalized care pathway, the aim of which is to offer patients an optimized quality of life. They forge an indispensable link between the city's healthcare services and the PEC, collaborating with the many healthcare professionals who work with people suffering from Parkinson's disease.

Image-Guided VATS in the Hybrid Operation Room Facilitates Early Diagnosis and Concurrent Treatment of Subcentimeter Nonpalpable Lung Nodules.

OBJECTIVE: As lung cancer screening increases, the detection of small, nonpalpable lung lesions is on the rise. The hybrid operation room (OR), which combines percutaneous or endobronchial fiducial placement with on-table computed tomography (CT) and fluoroscopic guidance, improves localization and facilitates the diagnosis and treatment of smaller, nonpalpable lung nodules with greater accuracy. METHODS: In 35 consecutive months, 55 veterans underwent 60 image-guided video-assisted thoracic surgery procedures for lesion resection. Of the cases, 36% were found during lung cancer screening. All patients received their care in the hybrid OR, where cone-beam CT scan technology was used to place an average of 1.6 fiducials percutaneously (n = 55) or via augmented navigational bronchoscopy (n = 5). RESULTS: A total of 66 lesions were resected. The median lesion size was 8 mm with an interquartile range of 6 to 14. The patients underwent nonanatomical resection with lymph node dissection using radiologic guidance. When indicated, an anatomical resection was subsequently performed. Of 47 total non-small cell lung cancer lesions, 83% were diagnosed at stage IA1 or IA2. The median surgical margin was 15 mm; the margin was usually 1.5 times as wide as the lesion. CONCLUSIONS: The hybrid OR technology gives a 3-dimensional assessment of the small lung lesions, allowing for a tissue-saving resection while achieving good surgical margins. During lung cancer screening, smaller, nonpalpable lung nodules are frequently found. This technology allows resection of subcentimeter lesions, which would otherwise be unresectable at this early stage, possibly improving survival.

A case of Pearsonema eggs in the urine sediment of a cat in Trinidad.

Nematodes of the urinary tract of domestic dogs and cats are a rare occurrence. The discovery of the eggs on urine sediment examination is usually an incidental finding. A twenty-one month old intact queen presented to the Veterinary Teaching Hospital with a history of a serosanguinous vaginal discharge and reddish colour urine for the last ten days. Complete blood count and biochemistry analysis revealed an inflammatory leukogram and a hyperproteinaemia. A urogenital tract infection was diagnosed as haematuria, pyuria, bacteriuria, proteinuria and alkaline urine were evident on urinalysis examination. Microscopic examination of the urine sediment also detected eggs with asymmetrical bipolar plugs characteristic for Pearsonema species. A distended uterus as well as a raised lesion in the mucosal layer of the urinary bladder were observed with ultrasonography. A routine ovariohysterectomy was performed. The cat was also treated with ivermectin and amoxicillin. The cat improved with the eventual resolution of the red colour urine and serosanguinous vaginal discharge.

A simple in vitro acylation assay based on optimized HlyA and HlyC purification.

HlyA is a toxin secreted by uropathogenic Escherichia coli strains. HlyA belongs to the repeats in the toxin protein family and needs (i) a posttranslational, fatty acylation at two internal lysines by the acyltransferase HlyC and (ii) extracellular ion binding to achieve its active conformation. Both processes are not fully understood and experiments are often limited due to the low amounts of protein available. Here, we present an optimized purification protocol for the proteins involved in HlyA activation as well as a quick and nonradioactive assay for in vitro HlyA acylation. These may simplify future experiments, e.g., activity scanning and characterization of HlyA or HlyC mutants as demonstrated with single and double HlyA lysine mutants.

Equilibrium folding of pro-HlyA from Escherichia coli reveals a stable calcium ion dependent folding intermediate.

HlyA from Escherichia coli is a member of the repeats in toxin (RTX) protein family, produced by a wide range of Gram-negative bacteria and secreted by a dedicated Type 1 Secretion System (T1SS). RTX proteins are thought to be secreted in an unfolded conformation and to fold upon secretion by Ca(2+) binding. However, the exact mechanism of secretion, ion binding and folding to the correct native state remains largely unknown. In this study we provide an easy protocol for high-level pro-HlyA purification from E. coli. Equilibrium folding studies, using intrinsic tryptophan fluorescence, revealed the well-known fact that Ca(2+) is essential for stability as well as correct folding of the whole protein. In the absence of Ca(2+), pro-HlyA adopts a non-native conformation. Such molecules could however be rescued by Ca(2+) addition, indicating that these are not dead-end species and that Ca(2+) drives pro-HlyA folding. More importantly, pro-HlyA unfolded via a two-state mechanism, whereas folding was a three-state process. The latter is indicative of the presence of a stable folding intermediate. Analysis of deletion and Trp mutants revealed that the first folding transition, at 6-7M urea, relates to Ca(2+) dependent structural changes at the extreme C-terminus of pro-HlyA, sensed exclusively by Trp914. Since all Trp residues of HlyA are located outside the RTX domain, our results demonstrate that Ca(2+) induced folding is not restricted to the RTX domain. Taken together, Ca(2+) binding to the pro-HlyA RTX domain is required to drive the folding of the entire protein to its native conformation.

The Type 1 secretion pathway - the hemolysin system and beyond.

Type 1 secretion systems (T1SS) are wide-spread among Gram-negative bacteria. An important example is the secretion of the hemolytic toxin HlyA from uropathogenic strains. Secretion is achieved in a single step directly from the cytosol to the extracellular space. The translocation machinery is composed of three indispensable membrane proteins, two in the inner membrane, and the third in the outer membrane. The inner membrane proteins belong to the ABC transporter and membrane fusion protein families (MFPs), respectively, while the outer membrane component is a porin-like protein. Assembly of the three proteins is triggered by accumulation of the transport substrate (HlyA) in the cytoplasm, to form a continuous channel from the inner membrane, bridging the periplasm and finally to the exterior. Interestingly, the majority of substrates of T1SS contain all the information necessary for targeting the polypeptide to the translocation channel - a specific sequence at the extreme C-terminus. Here, we summarize our current knowledge of regulation, channel assembly, translocation of substrates, and in the case of the HlyA toxin, its interaction with host membranes. We try to provide a complete picture of structure function of the components of the translocation channel and their interaction with the substrate. Although we will place the emphasis on the paradigm of Type 1 secretion systems, the hemolysin A secretion machinery from E. coli, we also cover as completely as possible current knowledge of other examples of these fascinating translocation systems. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.