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B형 간염 바이러스 DNA중합효소 RNase H domain 의 C-말단이 바이러스 증식에 미치는 영향
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.advisor | 김경민 | - |
| dc.contributor.author | Kim,Taeyeung | - |
| dc.date.accessioned | 2019-10-21T07:17:14Z | - |
| dc.date.available | 2019-10-21T07:17:14Z | - |
| dc.date.issued | 2011-02 | - |
| dc.identifier.other | 11459 | - |
| dc.identifier.uri | https://dspace.ajou.ac.kr/handle/2018.oak/17805 | - |
| dc.description | 학위논문(석사)--아주대학교 일반대학원 :의생명학과,2011. 2 | - |
| dc.description.tableofcontents | Ⅰ. INTRODUCTION 1 Ⅱ. MATERIALS AND METHODS 5 A. HBV plasmid DNA construction 5 B. Cell culture and transfection 8 C. Isolation of core particles 9 D. RNase protection assay (RPA) 9 E. Core particle Western blotting 10 F. Southern blotting 11 G. SDS-PAGE and Western blotting 11 Ⅲ. RESULT 12 A. HBV P constructs containing DHBV P residues in RNase H domain 12 B. Amino acid residues from 800 to 826 in C-terminus of the RNase H are critical for pgRNA encapsidaion and DNA synthesis. 14 C. The small motif substituted HBV RNase H domain mutants at C-terminus have ability to support HBV DNA synthesis. 21 D. The small motif substituted HBV RNase H domain mutants at C-terminus have ability to support HBV pgRNA encapsidation. 23 E. A leucine residue at position 806 in HBV P protein is important for viral genome replication. 26 F. A leucine residue at position 806 in HBV P protein is important for pgRNA encapsidation. 28 Ⅳ. DISCUSSION 29 Ⅴ. CONCLUSION 31 REFERENCES 32 국문요약 38 | - |
| dc.language.iso | eng | - |
| dc.publisher | The Graduate School, Ajou University | - |
| dc.rights | 아주대학교 논문은 저작권에 의해 보호받습니다. | - |
| dc.title | B형 간염 바이러스 DNA중합효소 RNase H domain 의 C-말단이 바이러스 증식에 미치는 영향 | - |
| dc.title.alternative | Taeyeung Kim | - |
| dc.type | Thesis | - |
| dc.contributor.affiliation | 아주대학교 일반대학원 | - |
| dc.contributor.alternativeName | Taeyeung Kim | - |
| dc.contributor.department | 일반대학원 의생명과학과 | - |
| dc.date.awarded | 2011. 2 | - |
| dc.description.degree | Master | - |
| dc.identifier.localId | 569198 | - |
| dc.identifier.url | http://dcoll.ajou.ac.kr:9080/dcollection/jsp/common/DcLoOrgPer.jsp?sItemId=000000011459 | - |
| dc.subject.keyword | HBV | - |
| dc.subject.keyword | RNase H | - |
| dc.subject.keyword | B형 간염 | - |
| dc.description.alternativeAbstract | Hepatitis B Virus (HBV) DNA polymerase (P) protein consisting of terminal protein (TP), spacer, reverse transcriptase (RT), and RNase H, plays critical roles in viral assembly and replication. RNase H domain is required for HBV DNA replication, however critical motif or amino acid residues in the RNase H domain for the HBV replication has not been extrensively demonstrated yet. In the present study, several chimeras of P protein by substituting Duck hepatitis B virus (DHBV) sequences were constructed. Accordingly, we tested a series of P protein chimeras in which several substitution mutants were disigned to contain various amino acids of DHBV P protein. It is found that amino acid residues from 800 to 826 (800SRPLLRLPFQPTTGRTSLYAVSPSVPS826) in C -terminus of the RNase H domain are required to complete HBV replication. HBV P protein mutants in which single amino acid residue was substituted were examined for the rescue of HBV replication. Among these mutants tested, L806T mutant P protein have a defect in pgRNA encapsidation and viral DNA synthesis, demonstrating that leucine at position 806 is critical for HBV replication. | - |
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