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The surface-exposed loop region of norovirus GII.3 VP1 plays an essential role in binding histo-blood group antigens.

Arch Virol. 2019; 
Zhang G,, Wang J,, Liu J, Zheng L, Wang W, Huo Y, Sun X.
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Nucleic Acid Purification & Analysis … Briefly, VLPs with wild-type or mutant VP1 proteins precipitated with PEG 6000 were incubated with or without trypsin at 200 μg/mL in PBS-T buffer at 37 °C for 30 min, and then boiled and loaded onto precast gels (ExpressPlus™, Genscript, China) … Get A Quote

摘要

Trypsin digestion promotes disassembly of GII.3 NoV virus-like particles (VLPs) and binding of VLPs to salivary histo-blood group antigens (HBGAs), but it is not clear which specific regions or residues mediate viral attachment to HBGAs. An earlier study indicated that arginine residues in the predicted surface-exposed loop region are susceptible to trypsin digestion. Here, we introduced single or multiple substitutions of four arginine residues located in the predicted surface-exposed loop region of the GII.3 NoV capsid protein (VP1) and observed their effects on susceptibility to trypsin digestion and binding to HBGAs. All of the mutations in VP1, including single substitutions (R287G, R292G, R296G or R307G) ... More

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