Regurgitation under anesthesia in a fasted patient prescribed semaglutide for weight loss: a case report.

Purpose: Glucagon-like peptide-1 receptor agonists (GLP-1 RAs) such as semaglutide are a class of medications prescribed to treat type 2 diabetes mellitus, and more recently, as an adjunct for weight loss because of its effects of delaying gastric emptying and suppressing appetite. Semaglutide is a long-acting agent with a half-life of approximately one week, and there are currently no guidelines that address the perioperative management of such agents.

Clinical Features: We describe an unexpected case of regurgitation of a large volume of gastric contents upon induction of general anesthesia in a nondiabetic, nonobese patient despite a long preoperative fasting period (20 hr for solids and eight hours for clear fluids).

pUL21 regulation of pUs3 kinase activity influences the nature of nuclear envelope deformation by the HSV-2 nuclear egress complex.

It is well established that the herpesvirus nuclear egress complex (NEC) has an intrinsic ability to deform membranes. During viral infection, the membrane-deformation activity of the NEC must be precisely regulated to ensure efficient nuclear egress of capsids. One viral protein known to regulate herpes simplex virus type 2 (HSV-2) NEC activity is the tegument protein pUL21.

The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding.

The herpes simplex virus (HSV) UL31 gene encodes a conserved member of the herpesvirus nuclear egress complex that not only functions in the egress of DNA containing capsids from the nucleus, but is also required for optimal replication of viral DNA and its packaging into capsids. Here we report that the UL31 protein from HSV-2 can be recruited to sites of DNA damage by sequences found in its N-terminus. The N-terminus of UL31 contains sequences resembling a poly (ADP-ribose) (PAR) binding motif suggesting that PAR interactions might mediate UL31 recruitment to damaged DNA.