Influence of N-Glycosylation on Virus–Host Interactions in Halorubrum lacusprofundi

N-glycosylation is a post-translational modification of proteins that occurs across all three domains life. In Archaea, crucial for cell stability and motility, but importantly also has significant implications virus–host interactions. While some archaeal viruses present glycosylated or interact with host proteins, the direct influence on interactions remains to be elucidated. this study, we generated an N-glycosylation-deficient mutant Halorubrum lacusprofundi, halophilic archaeon commonly used study cold adaptation, examined impact compromised infection dynamics two very diverse viruses. had no life cycle head-tailed virus HRTV-DL1, observed effect membrane-containing HFPV-1. Both intracellular genome numbers extracellular particle HFPV-1 were increased in strain, which attribute instability surface-layer builds protein envelope cell. When testing plasmid vesicles, specialized membrane vesicles transfer between cells, determined vesicle strongly dependent glycosylation machinery. Our thus provides important insight into role while pointing how differs amongst various virus-like elements.