Enzymatic cleavage promotes disassembly of GII.3 norovirus virus like particles and its binding to salivary histo-blood group antigens

摘要: In this study, we found that addition of fecal extract significantly promoted the binding GII.3 NoV VLPs to salivary HBGAs. SDS-PAGE analysis indicated major capsid proteins (VP1) were cleaved into two bands with molecular weights 26 and 31kD, respectively. Pretreatment by boiling or protease inhibitor cocktail type specific (leupeptin aprotinin) during incubation all decreased VP1 cleavage its Trypsin digestion led HBGAs, suggesting active enzyme(s) might be trypsin trypsin-like enzymes. pretreatment loss morphological intact VLPs, indicating enhanced signal was possible due increased fragmented subunits. N-terminal sequencing performed characterize sites indecisive results. vitro VLP-salivary HBGAs blockade assay using derived from different strains rabbit anti-genotype hyperimmune serum NoVs have conservative HBGA sites. summary, our results provide evidence about widespread presence enzyme in samples can cleave demonstrate which implications design multivalent vaccines.