Microbial Contamination of Soft Contact Lenses Among Medical School Students in Southern Iraq.

Background: Contamination of CLs and accessories risks potentially devastating microbial keratitis. We aimed to explore the rate of microbial contamination and predisposing factors among a group of asymptomatic young medical students. Methodology: The study included 115 healthy female medical students with a mean age of 21.64 ± 2.02 years between January and November 2021. Information about CL use, wear and care was gathered. Each participant's CL and case were swabbed for microbiological identification. Univariable and multivariable analyses were conducted to look for associations with a range of factors. Results: Overall, 91 participants (79.13%) had at least one contaminated sample (lens and/or case). The rates of contamination of CL and their cases were 66% and 76.5%, respectively. Higher contamination rates were caused by gram-negative bacteria (60% of the contaminated samples) with P. aeruginosa being the most common contaminant both for CL and cases, whereas S. epidermidis and S. aureus were the most common contaminants for the CL and cases, respectively, regarding gram-positive contamination. Multivariable analysis showed younger age as a significant predictor of pseudomonas contamination of the lenses and cases (OR: 12.302, 6.555 for CL & cases, respectively; P = 0.001 for both). Older age was a significant predictor of K. pneumoniae contamination (OR: 4.154, P = 0.007). Pseudomonas contamination of both lenses and cases was predicted by the type of solution used (OR: 10.8 and 13.5, P = 0.001 and 0.003 for bottled and distilled water vs commercially available solutions for CL; OR: 4.5 and 5.8, P = 0.045 and 0.004, respectively, for cases). Pseudomonas case contamination was associated with low frequency of solution change. Conclusion: Microbial contamination rate of soft CL and their cases is high among young medical students in comparison to previously reported rates and was predisposed by several poor hygienic practices and wearing regimens.

Intracardiac Thrombus in Transit Detected by Point-of-Care Ultrasound.

Pulmonary embolism (PE) is a condition with a high rate of morbidity and mortality if it is not recognized and treated in a timely fashion. Point-of-care ultrasound (POCUS) is a useful tool that can help clinicians make prompt diagnosis. We present a case where we diagnosed massive PE through visualizing an intracardiac thrombus in transit, and we highlight some important ultrasonographic features.

Profundidad de la línea de demarcación del estroma corneal después de la reticulación del colágeno corneal usando epitelial corneal personalizado versus convencional desbridamiento / Corneal stromal demarcation line depth after corneal collagen cross-linking using customized versus conventional corneal epithelial debridement

Aim of the Study: Compare the corneal demarcation line (DL) depth after corneal collagen cross-linking (CXL) with subtotal versus customized corneal epithelium debridement using anterior segment optical coherence tomography (AS-OCT). Design: Prospective case-control study. Materials and Methods: The study enrolled 18 patients with bilateral progressive keratoconus. Both eyes treated by CXL using 3 mW/cm2 / 30 minutes setting. One eye with subtotal epithelial debridement (about 9 mm diameter) and the contralateral eye with customized debridement (approximately 1 mm single horizontal central scratch). One month postoperatively, patients had AS-OCT imaging to detect and measure the depth ofDL. Results: Patients' age mean was 25.17 years +/- 4.81 SD. Epithelial healing completed with in 3-7 days in conventional treatment group and demarcation line was evident in 16 eyes (89%) with a mean depth of 290.31 µm while in customized debridement group, the epithelial healing lasted less than 24 hours and DL was detectable in 10 patients (55.5 %) with a mean DL depth of 221 µm with a statistically significant difference (p < 0.05). Subjective postoperative pain graded as "moderate to severe" in about 77% of eyes underwent 9 mm epi-off CXL compared with 55% of those with customized debridement group. Conclusions: Although the DL if found in majority cases, but the shallow location in customized corneal debridement cases questioned the efficacy of this technique despite the quick re-epithelialization and less postoperative pain that accompanied it

Oncologic Emergencies-The Old, the New, and the Deadly.

Cancer continues to be a leading cause of death despite a broader understanding of its biology and the development of novel therapies. Nonetheless, with an increasing survival of this population, intensivists must be aware of the associated emergencies, both old and new. Oncologic emergencies can be seen as an initial presentation of the disease or precipitated by its treatment. In this review, we present key oncologic emergencies that may be encountered in daily practice, complications associated with innovative therapies, and treatment-related adverse events.

Identification of a region in the stalk domain of the nipah virus receptor binding protein that is critical for fusion activation.

Paramyxoviruses, including the emerging lethal human Nipah virus (NiV) and the avian Newcastle disease virus (NDV), enter host cells through fusion of the viral and target cell membranes. For paramyxoviruses, membrane fusion is the result of the concerted action of two viral envelope glycoproteins: a receptor binding protein and a fusion protein (F). The NiV receptor binding protein (G) attaches to ephrin B2 or B3 on host cells, whereas the corresponding hemagglutinin-neuraminidase (HN) attachment protein of NDV interacts with sialic acid moieties on target cells through two regions of its globular domain. Receptor-bound G or HN via its stalk domain triggers F to undergo the conformational changes that render it competent to mediate fusion of the viral and cellular membranes. We show that chimeric proteins containing the NDV HN receptor binding regions and the NiV G stalk domain require a specific sequence at the connection between the head and the stalk to activate NiV F for fusion. Our findings are consistent with a general mechanism of paramyxovirus fusion activation in which the stalk domain of the receptor binding protein is responsible for F activation and a specific connecting region between the receptor binding globular head and the fusion-activating stalk domain is required for transmitting the fusion signal.

Regulation of paramyxovirus fusion activation: the hemagglutinin-neuraminidase protein stabilizes the fusion protein in a pretriggered state.

The hemagglutinin (HA)-neuraminidase protein (HN) of paramyxoviruses carries out three discrete activities, each of which affects the ability of HN to promote viral fusion and entry: receptor binding, receptor cleaving (neuraminidase), and triggering of the fusion protein. Binding of HN to its sialic acid receptor on a target cell triggers its activation of the fusion protein (F), which then inserts into the target cell and mediates the membrane fusion that initiates infection. We provide new evidence for a fourth function of HN: stabilization of the F protein in its pretriggered state before activation. Influenza virus hemagglutinin protein (uncleaved HA) was used as a nonspecific binding protein to tether F-expressing cells to target cells, and heat was used to activate F, indicating that the prefusion state of F can be triggered to initiate structural rearrangement and fusion by temperature. HN expression along with uncleaved HA and F enhances the F activation if HN is permitted to engage the receptor. However, if HN is prevented from engaging the receptor by the use of a small compound, temperature-induced F activation is curtailed. The results indicate that HN helps stabilize the prefusion state of F, and analysis of a stalk domain mutant HN reveals that the stalk domain of HN mediates the F-stabilization effect.

The second receptor binding site of the globular head of the Newcastle disease virus hemagglutinin-neuraminidase activates the stalk of multiple paramyxovirus receptor binding proteins to trigger fusion.

The hemagglutinin-neuraminidase (HN) protein of paramyxoviruses carries out three distinct activities contributing to the ability of HN to promote viral fusion and entry: receptor binding, receptor cleavage (neuraminidase), and activation of the fusion protein. The relationship between receptor binding and fusion triggering functions of HN are not fully understood. For Newcastle disease virus (NDV), one bifunctional site (site I) on HN's globular head can mediate both receptor binding and neuraminidase activities, and a second site (site II) in the globular head is also capable of mediating receptor binding. The receptor analog, zanamivir, blocks receptor binding and cleavage activities of NDV HN's site I while activating receptor binding by site II. Comparison of chimeric proteins in which the globular head of NDV HN is connected to the stalk region of either human parainfluenza virus type 3 (HPIV3) or Nipah virus receptor binding proteins indicates that receptor binding to NDV HN site II not only can activate its own fusion (F) protein but can also activate the heterotypic fusion proteins. We suggest a general model for paramyxovirus fusion activation in which receptor engagement at site II plays an active role in F activation.