In silico prediction of the binding structure between vitellogenin and vitellogenin receptor of Haemaphysalis longicornis.

ABSTRACT: Vitellogenin (Vtg) and its receptor (VtgR)-essential for yolk deposition and transovarial pathogen transmission in ticks-are compelling targets for antibody-based intervention. To investigate their interaction in the tick Haemaphysalis longicornis, we employed AlphaFold2 to model the β-barrel domain of the midgut-synthesized paralog HlVtg1 and the first three ligand-binding repeats (LBR1-3) of HlVtgR. Subsequent protein-protein docking in Molecular Operating Environment (MOE) revealed a recurrent binding interface centered on HlVtg1's Glu87, which formed persistent electrostatic interactions with LBR1-3 across top-ranking poses. Our results support a "monomeric engagement" model, where a single HlVtg1 monomer simultaneously engages all three low-density lipoprotein receptor class-A (LDLRA)

SUBMITTER: Behri M 

PROVIDER: S-EPMC12604960 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature