Discovery of a heparan sulfate binding domain in monkeypox virus H3 as an anti-poxviral drug target combining AI and MD simulations.

Viral adhesion to host cells is a critical step in infection for many viruses, including monkeypox virus (MPXV). In MPXV, the H3 protein mediates viral adhesion through its interaction with heparan sulfate (HS), yet the structural details of this interaction have remained elusive. Using AI-based structural prediction tools and molecular dynamics (MD) simulations, we identified a novel, positively charged α-helical domain in H3 that is essential for HS binding.

Auto Arginine-GlcNAcylation Is Crucial for Bacterial Pathogens in Regulating Host Cell Death.

Many Gram-negative bacterial pathogens utilize the type III secretion system (T3SS) to inject virulence factors, named effectors, into host cells. These T3SS effectors manipulate host cellular signaling pathways to facilitate bacterial pathogenesis. Death receptor signaling plays an important role in eukaryotic cell death pathways.

Borneol increases blood-tumour barrier permeability by regulating the expression levels of tight junction-associated proteins.

Context: Selectively opening the blood-tumour barrier (BTB) is critical to deliver antitumour drugs from blood to tumour tissues. The BTB problem is attributed to the tight junctions (TJs), which consist of several transmembrane proteins.

Objective: To investigate whether borneol could open the BTB by affecting TJ-associated proteins ZO-1, occludin, claudin-5 and F-actin in the rat model of C6 glioma.