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      저자 : Zhai Yuxiu (검색결과 2 건)
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        Discovery of genes associated with cadmium accumulation from gill of scallop Chlamys farreri based on high-throughput sequencing

        Yuxiu Zhai,Hui Zhang,Lin Yao,Yanhua Jiang,Fengling Li 한국유전학회 2016 Genes & Genomics Vol.38 No.5

        Chlamys farreri is an important economic mollusk and is able to accumulate cadmium (Cd) excessively. Two cDNA libraries from gill of C. farreri which were Cd treated or not were generated based on the Illumina sequencing platform in order to identify differentially expressed genes (DEGs) associated with cadmium accumulation. The analysis of comparative transcriptomics identified 82,800 unigenes and 128 differentially expressed genes. Of these, 8 of the most significant DEGs were verified by real-time PCR, showing consistent trends in expression patterns between the two techniques. KEGG pathways analysis revealed that 37 associated processes were highly enriched. A set of key DEGs were identified that may play important roles in cadmium exposure. Our work presents an overview of gene expression change during cadmium exposure to C. farreri and identifies a series of candidate genes and pathways for further research on the molecular mechanisms of cadmium accumulation.

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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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