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        Function of VP2 Protein in the Stability of the Secondary Structure of Virus-like Particles of Genogroup II Norovirus at Different pH Levels: Function of VP2 Protein in the Stability of NoV VLPs

        Yao Lin,Li Fengling,Wang Lianzhu,Zhai Yuxiu,Jiang Yanhua 한국미생물학회 2014 The journal of microbiology Vol.52 No.11

        VP2 is the minor structural protein of noroviruses (NoV)and may function in NoV particle stability. To determinethe function of VP2 in the stability of the NoV particle, weconstructed and purified two kinds of virus-like particles(VLPs), namely, VLPs (VP1) and VLPs (VP1+VP2), fromSf9 cells infected with recombinant baculoviruses by usinga Bac-to-Bac® baculovirus expression system. The two kindsof VLPs were treated with different phosphate buffers (pH2 to pH 8); the secondary structure was then analyzed byfar UV circular dichroism (CD) spectroscopy. Results showedthat significant disruptions of the secondary structure ofproteins were not observed at pH 2 to pH 7. At pH 8, thepercentages of α-helix, β-sheet, and β-turn in VLPs (VP1)were decreased from 11% to 8%, from 37% to 32%, andfrom 20% to 16%, respectively. The percentage of coil wasincreased from 32% to 44%. By contrast, the percentages ofα-helix, β-sheet, and β-turn in VLPs (VP1+VP2) were decreasedfrom 11% to 10%, from 37% to 35%, and from 20%to 19%, respectively. The percentage of coil was increasedfrom 32% to 36%. VLPs (VP1+VP2) was likely more stablethan VLPs (VP1), as indicated by the percentage of the secondarystructures analyzed by CD. These results suggestedthat VP2 could stabilize the secondary structure of VLPsunder alkaline pH conditions. This study provided novelinsights into the molecular mechanism of the function ofVP2 in the stability of NoV particles.

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