Feasibility and Potential for Real-Time 3D Vitreoretinal Surgery Telementoring.

PURPOSE: To demonstrate the potential for real-time, three-dimensional (3D) surgical telementoring to enhance vitreoretinal surgical education. METHODS: The 3D video feed from a high dynamic range surgical camera (NGENUITY) was run through a 4K video capture device (Magewell USB 4K) and set as the video input for a video conferencing application (Zoom). Remote surgical viewing was then performed in two-dimensions (2D) on a computer or in 3D with a virtual reality headset (Oculus Quest 2). RESULTS: Ten surgical cases were successfully live streamed in real time to two separate surgeons in the United States. Specific details of the case were visualized with low latency and interaction with the operating surgeon was possible without affecting the surgical display quality. Excluding the NGENUITY system and personal computers, ancillary equipment costs (video capture card and virtual reality headset) were kept to below $1,000. CONCLUSION: Our study demonstrates that 3D surgical video streaming can be achieved in real time with minimal latency through the use of low-cost video capture equipment and video conferencing/streaming software. The use of this technology gives educators the ability to mentor trainees without the traditional geographic and physical constraints of in-person surgical viewing.

Self-Assembly Simulations of Classic Claudins-Insights into the Pore Structure, Selectivity, and Higher Order Complexes.

Tight junction (TJ) protein assembly controls permeability across epithelial and endothelial cells; thus, biochemical interactions that control the TJ assembly have physiological and biomedical significance. In this work, we employed multiscale simulations to probe the TJ self-assembly of five classic claudins (-1, -2, -4, -15, and -19). Claudin proteins assembled into dimeric and occasionally trimeric interfaces that subsequently formed larger polymeric strands. Using orientation-angle analysis to decompose polymeric strands, we found that individual claudins prefer certain dimer interfaces to others. Despite variations in the exact dimer populations observed in individual claudins, there appears to be an overall conformational uniformity in the type of dimeric interactions formed by the claudin family of proteins. A detailed structural characterization of the trimeric assemblies revealed that they could be putative receptors for trimeric Clostridium perfringens enterotoxin. Full characterization of the claudin-2 dimer interface revealed a cysteine cross-linkable interaction, which could be assembled into a symmetric pore of 7.4 Å average diameter. We extended the analysis of pore structure to other classic claudins and found that the distribution of polar residues lining the pore volume varied considerably between the barrier- and pore-forming claudins, potentially delineating the functionality in classic claudins.