A widespread family of viral sponge proteins reveals specific inhibition of nucleotide signals in anti-phage defense.

Cyclic oligonucleotide-based antiviral signaling systems (CBASS) are bacterial anti-phage defense operons that use nucleotide signals to control immune activation. Here we biochemically screen 57 diverse and phages for the ability to disrupt CBASS immunity and discover anti-CBASS 4 (Acb4) from the phage SPO1 as the founding member of a large family of >1,300 immune evasion proteins. A 2.

Overcoming drug resistance through extracellular vesicle-based drug delivery system in cancer treatment.

Drug resistance is a major challenge in cancer therapy that often leads to treatment failure and disease relapse. Despite advancements in chemotherapeutic agents and targeted therapies, cancers often develop drug resistance, making these treatments ineffective. Extracellular vesicles (EVs) have gained attention for their potential applications in drug delivery because of their natural origin, biocompatibility, and ability to cross biological barriers.

Risk of SARS-CoV-2 infection and adverse outcomes among vaccinated patients with tuberculosis.

Objectives: Limited data are available to assess breakthrough SARS-CoV-2 infections, medical utilization, and mortality in patients with tuberculosis (TB). The aim of this study was to examine the risk of COVID-19 and severe outcomes in patients with TB between January 2020 and March 2022.

Study Design: US electronic medical records were used to identify TB and non-TB patients who completed the primary series of vaccination and had no prior COVID-19.

Dynamic Peptide Nanoframework-Guided Protein Coassembly: Advancing Adhesion Performance with Hierarchical Structures.

Hierarchical structures are essential in natural adhesion systems. Replicating these in synthetic adhesives is challenging due to intricate molecular mechanisms and multiscale processes. Here, we report three phosphorylated peptides featuring a hydrophobic self-assembly motif linked to a hydrophilic phosphorylated sequence (pSGSS), forming peptide fibril nanoframeworks.

Changes of shrimp myofibrillar proteins hydrolyzed by Virgibacillus proteases: Structural characterization, mechanism visualization, and flavor compound formation.

To explore the mechanism of Virgibacillus proteases on hydrolysis of shrimp myofibrillar protein (SMP) and formation of volatile compounds, the fermented broth of Virgibacillus halodenitrificans was purified and the protease was identified as peptidase S8. The enzyme had optimum activity at pH 7.0-8.