Small glycomimetic antagonists of the cytomegalovirus glycoprotein UL141 prevent binding to TRAIL death receptor.

ABSTRACT: Human cytomegalovirus (HCMV) UL141 inhibits immune recognition of virally infected cells by natural killer cells and cytotoxic T cells through modulation of cellular receptors (e.g., TRAIL-R2/-R1, CD155, CD112). Recent findings suggest that UL141 is also a critical component of the HCMV virion, further emphasizing its significance. In this study, we aimed to develop a small synthetic compound as a UL141 antagonist. Building on our crystal structure analysis, we designed compounds to specifically bind viral UL141, thereby blocking its interaction with target receptors thus inhibiting its immunoevasive functions. We evaluated a small library of synthesized compounds composed of diverse saccharide units conjugated with nonsaccharide moieties, such as nonionic glycolipids, pyrrolidines, and "c

SUBMITTER: Nemcovicova I 

PROVIDER: S-EPMC12140054 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature